(data stored in SCRATCH zone)

SWISSPROT: GYRA_ECOLI

ID   GYRA_ECOLI              Reviewed;         875 AA.
AC   P0AES4; P09097;
DT   20-DEC-2005, integrated into UniProtKB/Swiss-Prot.
DT   20-DEC-2005, sequence version 1.
DT   11-DEC-2019, entry version 141.
DE   RecName: Full=DNA gyrase subunit A {ECO:0000255|HAMAP-Rule:MF_01897};
DE            EC=5.6.2.2 {ECO:0000255|HAMAP-Rule:MF_01897, ECO:0000269|PubMed:12051842, ECO:0000269|PubMed:18642932, ECO:0000269|PubMed:186775, ECO:0000269|PubMed:19965760, ECO:0000269|PubMed:9278055};
GN   Name=gyrA {ECO:0000255|HAMAP-Rule:MF_01897};
GN   Synonyms=hisW, nalA {ECO:0000303|PubMed:337300}, parD;
GN   OrderedLocusNames=b2231, JW2225;
OS   Escherichia coli (strain K12).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=83333;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=2828631; DOI=10.1016/0022-2836(87)90479-7;
RA   Swanberg S.L., Wang J.C.;
RT   "Cloning and sequencing of the Escherichia coli gyrA gene coding for the A
RT   subunit of DNA gyrase.";
RL   J. Mol. Biol. 197:729-736(1987).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=K12 / KL16;
RX   PubMed=2830458; DOI=10.1007/bf00338386;
RA   Yoshida H., Kojima T., Yamagishi J., Nakamura S.;
RT   "Quinolone-resistant mutations of the gyrA gene of Escherichia coli.";
RL   Mol. Gen. Genet. 211:1-7(1988).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANTS QUINOLONE-RESISTANTS ASN-87
RP   AND ILE-MET-MET-ILE-798.
RC   STRAIN=OV6;
RX   PubMed=2834621; DOI=10.1111/j.1365-2958.1987.tb01932.x;
RA   Hussain K., Elliott E.J., Salmond G.P.C.;
RT   "The parD- mutant of Escherichia coli also carries a gyrAam mutation. The
RT   complete sequence of gyrA.";
RL   Mol. Microbiol. 1:259-273(1987).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANTS QUINOLONE-RESISTANT GLU-678
RP   AND SER-828.
RC   STRAIN=227;
RX   PubMed=2548439; DOI=10.1128/aac.33.6.886;
RA   Cullen M.E., Wyke A.W., Kuroda R., Fisher L.M.;
RT   "Cloning and characterization of a DNA gyrase A gene from Escherichia coli
RT   that confers clinical resistance to 4-quinolones.";
RL   Antimicrob. Agents Chemother. 33:886-894(1989).
RN   [5]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX   PubMed=9205837; DOI=10.1093/dnares/4.2.91;
RA   Yamamoto Y., Aiba H., Baba T., Hayashi K., Inada T., Isono K., Itoh T.,
RA   Kimura S., Kitagawa M., Makino K., Miki T., Mitsuhashi N., Mizobuchi K.,
RA   Mori H., Nakade S., Nakamura Y., Nashimoto H., Oshima T., Oyama S.,
RA   Saito N., Sampei G., Satoh Y., Sivasundaram S., Tagami H., Takahashi H.,
RA   Takeda J., Takemoto K., Uehara K., Wada C., Yamagata S., Horiuchi T.;
RT   "Construction of a contiguous 874-kb sequence of the Escherichia coli-K12
RT   genome corresponding to 50.0-68.8 min on the linkage map and analysis of
RT   its sequence features.";
RL   DNA Res. 4:91-113(1997).
RN   [6]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=K12 / MG1655 / ATCC 47076;
RX   PubMed=9278503; DOI=10.1126/science.277.5331.1453;
RA   Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V.,
RA   Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F.,
RA   Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B.,
RA   Shao Y.;
RT   "The complete genome sequence of Escherichia coli K-12.";
RL   Science 277:1453-1462(1997).
RN   [7]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX   PubMed=16738553; DOI=10.1038/msb4100049;
RA   Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S.,
RA   Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.;
RT   "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655
RT   and W3110.";
RL   Mol. Syst. Biol. 2:E1-E5(2006).
RN   [8]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-88, AND PARTIAL PROTEIN SEQUENCE.
RX   PubMed=3029031; DOI=10.1128/jb.169.3.1272-1278.1987;
RA   Menzel R., Gellert M.;
RT   "Fusions of the Escherichia coli gyrA and gyrB control regions to the
RT   galactokinase gene are inducible by coumermycin treatment.";
RL   J. Bacteriol. 169:1272-1278(1987).
RN   [9]
RP   PROTEIN SEQUENCE OF 17-24; 61-66 AND 123-126, FUNCTION, ACTIVE SITE,
RP   REACTION MECHANISM, AND DNA-BINDING.
RX   PubMed=3031051;
RA   Horowitz D.S., Wang J.C.;
RT   "Mapping the active site tyrosine of Escherichia coli DNA gyrase.";
RL   J. Biol. Chem. 262:5339-5344(1987).
RN   [10]
RP   FUNCTION IN GENERATING NEGATIVELY SUPERCOILED DNA, CATALYTIC ACTIVITY, AND
RP   ATP-DEPENDENCE.
RX   PubMed=186775; DOI=10.1073/pnas.73.11.3872;
RA   Gellert M., Mizuuchi K., O'Dea M.H., Nash H.A.;
RT   "DNA gyrase: an enzyme that introduces superhelical turns into DNA.";
RL   Proc. Natl. Acad. Sci. U.S.A. 73:3872-3876(1976).
RN   [11]
RP   FUNCTION IN RELAXING SUPERCOILED DNA, AND ACTIVITY REGULATION.
RX   PubMed=337300; DOI=10.1073/pnas.74.11.4772;
RA   Gellert M., Mizuuchi K., O'Dea M.H., Itoh T., Tomizawa J.I.;
RT   "Nalidixic acid resistance: a second genetic character involved in DNA
RT   gyrase activity.";
RL   Proc. Natl. Acad. Sci. U.S.A. 74:4772-4776(1977).
RN   [12]
RP   VARIANTS QUINOLONE-RESISTANT SER-67; CYS-81; LEU-83; TRP-83; PRO-84; ASN-87
RP   AND HIS-106.
RC   STRAIN=K12 / KL16;
RX   PubMed=2168148; DOI=10.1128/aac.34.6.1271;
RA   Yoshida H., Bogaki M., Nakamura M., Nakamura S.;
RT   "Quinolone resistance-determining region in the DNA gyrase gyrA gene of
RT   Escherichia coli.";
RL   Antimicrob. Agents Chemother. 34:1271-1272(1990).
RN   [13]
RP   VARIANTS QUINOLONE-RESISTANT LEU-83; TRP-83 AND VAL-87.
RX   PubMed=1850972; DOI=10.1128/aac.35.2.387;
RA   Oram M., Fisher L.M.;
RT   "4-quinolone resistance mutations in the DNA gyrase of Escherichia coli
RT   clinical isolates identified by using the polymerase chain reaction.";
RL   Antimicrob. Agents Chemother. 35:387-389(1991).
RN   [14]
RP   MUTAGENESIS OF SER-83 AND GLN-106.
RC   STRAIN=K12;
RX   PubMed=1850970; DOI=10.1128/aac.35.2.335;
RA   Hallett P., Maxwell A.;
RT   "Novel quinolone resistance mutations of the Escherichia coli DNA gyrase A
RT   protein: enzymatic analysis of the mutant proteins.";
RL   Antimicrob. Agents Chemother. 35:335-340(1991).
RN   [15]
RP   INHIBITION BY TOXIN PROTEIN CCDB, AND MUTAGENESIS OF ARG-462.
RC   STRAIN=K12;
RX   PubMed=1324324; DOI=10.1016/0022-2836(92)90629-x;
RA   Bernard P., Couturier M.;
RT   "Cell killing by the F plasmid CcdB protein involves poisoning of DNA-
RT   topoisomerase II complexes.";
RL   J. Mol. Biol. 226:735-745(1992).
RN   [16]
RP   MUTAGENESIS OF ARG-462.
RX   PubMed=8254658; DOI=10.1006/jmbi.1993.1609;
RA   Bernard P., Kezdy K.E., Van Melderen L., Steyaert J., Wyns L., Pato M.L.,
RA   Higgins P.N., Couturier M.;
RT   "The F plasmid CcdB protein induces efficient ATP-dependent DNA cleavage by
RT   gyrase.";
RL   J. Mol. Biol. 234:534-541(1993).
RN   [17]
RP   FUNCTION, AND ACTIVITY REGULATION.
RX   PubMed=7811004; DOI=10.1128/aac.38.9.1966;
RA   Nakada N., Gmuender H., Hirata T., Arisawa M.;
RT   "Mechanism of inhibition of DNA gyrase by cyclothialidine, a novel DNA
RT   gyrase inhibitor.";
RL   Antimicrob. Agents Chemother. 38:1966-1973(1994).
RN   [18]
RP   INHIBITION BY TOXIN PROTEIN CCDB, REJUVENATION BY CCDA, AND SUBUNIT.
RX   PubMed=8604132; DOI=10.1006/jmbi.1996.0102;
RA   Maki S., Takiguchi S., Horiuchi T., Sekimizu K., Miki T.;
RT   "Partner switching mechanisms in inactivation and rejuvenation of
RT   Escherichia coli DNA gyrase by F plasmid proteins LetD (CcdB) and LetA
RT   (CcdA).";
RL   J. Mol. Biol. 256:473-482(1996).
RN   [19]
RP   FUNCTION, AND DOMAIN.
RX   PubMed=8962066; DOI=10.1073/pnas.93.25.14416;
RA   Kampranis S.C., Maxwell A.;
RT   "Conversion of DNA gyrase into a conventional type II topoisomerase.";
RL   Proc. Natl. Acad. Sci. U.S.A. 93:14416-14421(1996).
RN   [20]
RP   FUNCTION, ACTIVITY REGULATION, SUBUNIT, AND DNA-BINDING.
RC   STRAIN=K12 / N2879;
RX   PubMed=9148951; DOI=10.1074/jbc.272.20.13302;
RA   Funatsuki K., Tanaka R., Inagaki S., Konno H., Katoh K., Nakamura H.;
RT   "acrB mutation located at carboxyl-terminal region of gyrase B subunit
RT   reduces DNA binding of DNA gyrase.";
RL   J. Biol. Chem. 272:13302-13308(1997).
RN   [21]
RP   IDENTIFICATION BY 2D-GEL.
RX   PubMed=9298644; DOI=10.1002/elps.1150180805;
RA   VanBogelen R.A., Abshire K.Z., Moldover B., Olson E.R., Neidhardt F.C.;
RT   "Escherichia coli proteome analysis using the gene-protein database.";
RL   Electrophoresis 18:1243-1251(1997).
RN   [22]
RP   FUNCTION.
RX   PubMed=9334322; DOI=10.1101/gad.11.19.2580;
RA   Zechiedrich E.L., Khodursky A.B., Cozzarelli N.R.;
RT   "Topoisomerase IV, not gyrase, decatenates products of site-specific
RT   recombination in Escherichia coli.";
RL   Genes Dev. 11:2580-2592(1997).
RN   [23]
RP   IDENTIFICATION AND DISCUSSION OF GYRA-BOX, AND DOMAIN.
RX   PubMed=9426128; DOI=10.1046/j.1365-2958.1997.6242005.x;
RA   Ward D.V., Newton A.;
RT   "Requirement of topoisomerase IV parC and parE genes for cell cycle
RT   progression and developmental regulation in Caulobacter crescentus.";
RL   Mol. Microbiol. 26:897-910(1997).
RN   [24]
RP   FUNCTION, CATALYTIC ACTIVITY, SUBUNIT, AND MUTAGENESIS OF ARG-32; ARG-47;
RP   HIS-78 AND HIS-80.
RX   PubMed=12051842; DOI=10.1016/s0022-2836(02)00048-7;
RA   Hockings S.C., Maxwell A.;
RT   "Identification of four GyrA residues involved in the DNA breakage-reunion
RT   reaction of DNA gyrase.";
RL   J. Mol. Biol. 318:351-359(2002).
RN   [25]
RP   FUNCTION, AND MUTAGENESIS OF 560-GLN--GLY-566.
RX   PubMed=16332690; DOI=10.1074/jbc.m511160200;
RA   Kramlinger V.M., Hiasa H.;
RT   "The 'GyrA-box' is required for the ability of DNA gyrase to wrap DNA and
RT   catalyze the supercoiling reaction.";
RL   J. Biol. Chem. 281:3738-3742(2006).
RN   [26]
RP   FUNCTION.
RC   STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX   PubMed=17400739; DOI=10.1128/jb.00083-07;
RA   Champion K., Higgins N.P.;
RT   "Growth rate toxicity phenotypes and homeostatic supercoil control
RT   differentiate Escherichia coli from Salmonella enterica serovar
RT   Typhimurium.";
RL   J. Bacteriol. 189:5839-5849(2007).
RN   [27]
RP   FUNCTION, CATALYTIC ACTIVITY, AND SUBUNIT.
RX   PubMed=18642932; DOI=10.1021/bi800480j;
RA   Sissi C., Chemello A., Vazquez E., Mitchenall L.A., Maxwell A., Palumbo M.;
RT   "DNA gyrase requires DNA for effective two-site coordination of divalent
RT   metal ions: further insight into the mechanism of enzyme action.";
RL   Biochemistry 47:8538-8545(2008).
RN   [28]
RP   FUNCTION, AND ACTIVITY REGULATION.
RX   PubMed=19060136; DOI=10.1128/jb.01205-08;
RA   Merens A., Matrat S., Aubry A., Lascols C., Jarlier V., Soussy C.J.,
RA   Cavallo J.D., Cambau E.;
RT   "The pentapeptide repeat proteins MfpAMt and QnrB4 exhibit opposite effects
RT   on DNA gyrase catalytic reactions and on the ternary gyrase-DNA-quinolone
RT   complex.";
RL   J. Bacteriol. 191:1587-1594(2009).
RN   [29]
RP   FUNCTION, AND ACTIVITY REGULATION.
RX   PubMed=20356737; DOI=10.1016/j.bmcl.2010.03.052;
RA   Ronkin S.M., Badia M., Bellon S., Grillot A.L., Gross C.H., Grossman T.H.,
RA   Mani N., Parsons J.D., Stamos D., Trudeau M., Wei Y., Charifson P.S.;
RT   "Discovery of pyrazolthiazoles as novel and potent inhibitors of bacterial
RT   gyrase.";
RL   Bioorg. Med. Chem. Lett. 20:2828-2831(2010).
RN   [30]
RP   FUNCTION, DOMAIN, DNA-BINDING, AND MUTAGENESIS OF 842-PRO--ALA-856 AND
RP   854-SER--GLU-875.
RX   PubMed=22457353; DOI=10.1074/jbc.m112.345678;
RA   Tretter E.M., Berger J.M.;
RT   "Mechanisms for defining supercoiling set point of DNA gyrase orthologs: I.
RT   A nonconserved acidic C-terminal tail modulates Escherichia coli gyrase
RT   activity.";
RL   J. Biol. Chem. 287:18636-18644(2012).
RN   [31]
RP   FUNCTION, DNA-BINDING, AND MUTAGENESIS OF 842-PRO--ALA-856.
RX   PubMed=22457352; DOI=10.1074/jbc.m112.345736;
RA   Tretter E.M., Berger J.M.;
RT   "Mechanisms for defining supercoiling set point of DNA gyrase orthologs:
RT   II. The shape of the GyrA subunit C-terminal domain (CTD) is not a sole
RT   determinant for controlling supercoiling efficiency.";
RL   J. Biol. Chem. 287:18645-18654(2012).
RN   [32]
RP   FUNCTION, AND ACTIVITY REGULATION.
RX   PubMed=23294697; DOI=10.1016/j.bmcl.2012.11.073;
RA   Trzoss M., Bensen D.C., Li X., Chen Z., Lam T., Zhang J., Creighton C.J.,
RA   Cunningham M.L., Kwan B., Stidham M., Nelson K., Brown-Driver V.,
RA   Castellano A., Shaw K.J., Lightstone F.C., Wong S.E., Nguyen T.B., Finn J.,
RA   Tari L.W.;
RT   "Pyrrolopyrimidine inhibitors of DNA gyrase B (GyrB) and topoisomerase IV
RT   (ParE), Part II: development of inhibitors with broad spectrum, Gram-
RT   negative antibacterial activity.";
RL   Bioorg. Med. Chem. Lett. 23:1537-1543(2013).
RN   [33]
RP   X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS) OF 30-522, AND CATALYTIC ACTIVITY.
RX   PubMed=9278055; DOI=10.1038/42294;
RA   Morais Cabral J.H., Jackson A.P., Smith C.V., Shikotra N., Maxwell A.,
RA   Liddington R.C.;
RT   "Crystal structure of the breakage-reunion domain of DNA gyrase.";
RL   Nature 388:903-906(1997).
RN   [34]
RP   X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS) OF 363-494 IN COMPLEX WITH CCBD, AND
RP   SUBUNIT.
RX   PubMed=15854646; DOI=10.1016/j.jmb.2005.03.049;
RA   Dao-Thi M.H., Van Melderen L., De Genst E., Afif H., Buts L., Wyns L.,
RA   Loris R.;
RT   "Molecular basis of gyrase poisoning by the addiction toxin CcdB.";
RL   J. Mol. Biol. 348:1091-1102(2005).
RN   [35]
RP   X-RAY CRYSTALLOGRAPHY (2.6 ANGSTROMS) OF 535-841, AND DOMAIN.
RC   STRAIN=K12;
RX   PubMed=15897198; DOI=10.1074/jbc.m502838200;
RA   Ruthenburg A.J., Graybosch D.M., Huetsch J.C., Verdine G.L.;
RT   "A superhelical spiral in the Escherichia coli DNA gyrase A C-terminal
RT   domain imparts unidirectional supercoiling bias.";
RL   J. Biol. Chem. 280:26177-26184(2005).
RN   [36]
RP   X-RAY CRYSTALLOGRAPHY (2.62 ANGSTROMS) OF 1-525 IN COMPLEX WITH ANTIBIOTIC,
RP   FUNCTION, CATALYTIC ACTIVITY, AND SUBUNIT.
RX   PubMed=19965760; DOI=10.1126/science.1179123;
RA   Edwards M.J., Flatman R.H., Mitchenall L.A., Stevenson C.E., Le T.B.,
RA   Clarke T.A., McKay A.R., Fiedler H.P., Buttner M.J., Lawson D.M.,
RA   Maxwell A.;
RT   "A crystal structure of the bifunctional antibiotic simocyclinone D8, bound
RT   to DNA gyrase.";
RL   Science 326:1415-1418(2009).
CC   -!- FUNCTION: A type II topoisomerase that negatively supercoils closed
CC       circular double-stranded (ds) DNA in an ATP-dependent manner to
CC       maintain chromosomes in an underwound state (PubMed:3031051,
CC       PubMed:186775, PubMed:7811004, PubMed:9148951, PubMed:12051842,
CC       PubMed:18642932, PubMed:19060136, PubMed:20356737, PubMed:22457353,
CC       PubMed:23294697, PubMed:19965760). This makes better substrates for
CC       topoisomerase IV (ParC and ParE) which is the main enzyme that unlinks
CC       newly replicated chromosomes in E.coli (PubMed:9334322). Gyrase
CC       catalyzes the interconversion of other topological isomers of dsDNA
CC       rings, including catenanes (PubMed:22457352). Relaxes negatively
CC       supercoiled DNA in an ATP-independent manner (PubMed:337300). E.coli
CC       gyrase has higher supercoiling activity than many other bacterial
CC       gyrases; at comparable concentrations E.coli gyrase introduces more
CC       supercoils faster than M.tuberculosis gyrase, while M.tuberculosis
CC       gyrase has higher decatenation than supercoiling activity compared to
CC       E.coli (PubMed:22457352). E.coli makes 15% more negative supercoils in
CC       pBR322 plasmid DNA than S.typhimurium; the S.typhimurium GyrB subunit
CC       is toxic in E.coli, while the E.coli copy can be expressed in
CC       S.typhimurium even though the 2 subunits have 777/804 residues
CC       identical (PubMed:17400739). The enzymatic differences between E.coli
CC       gyrase and topoisomerase IV are largely due to the GyrA C-terminal
CC       domain (approximately residues 524-841) and specifically the GyrA-box
CC       (PubMed:8962066, PubMed:16332690). {ECO:0000269|PubMed:12051842,
CC       ECO:0000269|PubMed:16332690, ECO:0000269|PubMed:17400739,
CC       ECO:0000269|PubMed:18642932, ECO:0000269|PubMed:186775,
CC       ECO:0000269|PubMed:19060136, ECO:0000269|PubMed:19965760,
CC       ECO:0000269|PubMed:20356737, ECO:0000269|PubMed:22457352,
CC       ECO:0000269|PubMed:22457353, ECO:0000269|PubMed:23294697,
CC       ECO:0000269|PubMed:3031051, ECO:0000269|PubMed:337300,
CC       ECO:0000269|PubMed:7811004, ECO:0000269|PubMed:8962066,
CC       ECO:0000269|PubMed:9148951, ECO:0000269|PubMed:9334322}.
CC   -!- FUNCTION: Negative supercoiling favors strand separation, and DNA
CC       replication, transcription, recombination and repair, all of which
CC       involve strand separation. Type II topoisomerases break and join 2 DNA
CC       strands simultaneously in an ATP-dependent manner.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP-dependent breakage, passage and rejoining of double-
CC         stranded DNA.; EC=5.6.2.2; Evidence={ECO:0000255|HAMAP-Rule:MF_01897,
CC         ECO:0000269|PubMed:12051842, ECO:0000269|PubMed:18642932,
CC         ECO:0000269|PubMed:186775, ECO:0000269|PubMed:19965760,
CC         ECO:0000269|PubMed:9278055};
CC   -!- ACTIVITY REGULATION: Gyrase is the target of many classes of
CC       inhibitors, including coumarins, cyclothialidines, pyrrolopyrimidines,
CC       pyrazolthiazoles and (fluoro)quinolones. Quinolones bind GyrA when the
CC       enzyme is complexed with DNA and trap the enzyme in a covalent reaction
CC       intermediate with DNA (PubMed:3031051, PubMed:12051842). Coumarins bind
CC       to GyrB and are competitive inhibitors of its ATPase activity
CC       (PubMed:7811004). Cyclothialidines also bind GyrB and are ATPase
CC       competitive inhibitors; they seem to act differently from coumarins
CC       (PubMed:7811004). Pyrrolopyrimidines inhibit both GyrB and its paralog
CC       in topoisomerase IV (parE) (PubMed:23294697). Pyrazolthiazoles also
CC       inhibit the ATPase activity of GyrB (PubMed:20356737). DNA supercoiling
CC       and relaxation are both inhibited by oxolinic acid (PubMed:337300).
CC       Acriflavine inhibits supercoiling activity and DNA-stimulated ATPase
CC       activity (PubMed:9148951). DNA supercoiling activity is protected from
CC       fluoroquinolone inhibition by QnrB4; QnrB4 has no effect on
CC       supercoiling activity alone (PubMed:19060136).
CC       {ECO:0000269|PubMed:19060136, ECO:0000269|PubMed:20356737,
CC       ECO:0000269|PubMed:23294697, ECO:0000269|PubMed:337300,
CC       ECO:0000269|PubMed:7811004, ECO:0000269|PubMed:9148951}.
CC   -!- SUBUNIT: Heterotetramer, composed of two GyrA and two GyrB chains
CC       (PubMed:9148951, PubMed:12051842). In the heterotetramer, GyrA contains
CC       the active site tyrosine that forms a transient covalent intermediate
CC       with the DNA, while GyrB binds cofactors and catalyzes ATP hydrolysis
CC       (PubMed:12051842, PubMed:18642932, PubMed:19965760, PubMed:9148951).
CC       Can form a 2:2 complex with toxin CcdB in which GyrA is inactive;
CC       rejuvenation of GyrA(2)CcdB(2) is effected by CcdA (PubMed:15854646,
CC       PubMed:1324324, PubMed:8254658, PubMed:8604132).
CC       {ECO:0000269|PubMed:12051842, ECO:0000269|PubMed:1324324,
CC       ECO:0000269|PubMed:15854646, ECO:0000269|PubMed:18642932,
CC       ECO:0000269|PubMed:19965760, ECO:0000269|PubMed:8254658,
CC       ECO:0000269|PubMed:8604132, ECO:0000269|PubMed:9148951}.
CC   -!- INTERACTION:
CC       Self; NbExp=5; IntAct=EBI-547129, EBI-547129;
CC       P0AES6:gyrB; NbExp=7; IntAct=EBI-547129, EBI-541911;
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_01897}.
CC   -!- DOMAIN: An N-terminal fragment (residues 1-523) can be reconstituted
CC       with GyrB, but the complex no longer has negative supercoiling or ATP-
CC       independent DNA relaxation activities, although it is capable of DNA
CC       cleavage; ATP-dependent relaxation is inhibited by novobiocin and non-
CC       hydrolyzable ATP analogs (PubMed:8962066). The fragment has ATP-
CC       dependent DNA relaxation and 30-fold improved decatenation activities,
CC       unlike holoenzyme it preferentially binds supercoiled DNA
CC       (PubMed:8962066). This N-terminal fragment becomes a topoisomerase IV-
CC       like enzyme; it poorly complements a temperature-sensitive parC
CC       mutation (parC is the topoisomerase IV paralog of gyrA)
CC       (PubMed:8962066). {ECO:0000269|PubMed:8962066}.
CC   -!- DOMAIN: The C-terminal domain (CTD, approximately residues 535-841)
CC       contains 6 tandemly repeated subdomains known as blades, each of which
CC       is composed of a 4-stranded antiparallel beta-sheet (PubMed:15897198).
CC       The blades form a circular-shaped beta-pinwheel fold arranged in a
CC       spiral around a screw axis, to which DNA probably binds, inducing
CC       strong positive superhelicity (about 0.8 links/protein)
CC       (PubMed:15897198). The non-conserved, C-terminal acidic tail (residues
CC       842-875) regulates wrapping and DNA-binding by the CTD; deletions
CC       within the tail show it is autoinhibitory for DNA wrapping and binding,
CC       and couples ATP hydrolysis to DNA strand passage (PubMed:22457353). The
CC       GyrA-box is a 7 amino acid motif found in the first blade of the CTD
CC       which is discriminative for gyrase versus topoisomerase IV activity
CC       (PubMed:9426128). The GyrA-box is required for wrapping of DNA around
CC       gyrase, and thus is essential for the DNA supercoiling activity but not
CC       DNA relaxation or decatenation activities of gyrase (PubMed:16332690).
CC       {ECO:0000269|PubMed:15897198, ECO:0000269|PubMed:16332690,
CC       ECO:0000269|PubMed:22457353, ECO:0000305|PubMed:9426128}.
CC   -!- MISCELLANEOUS: When the enzyme transiently cleaves DNA a
CC       phosphotyrosine bond is formed between GyrA and DNA (PubMed:3031051).
CC       In the presence of quinolones this intermediate can be trapped and is
CC       used as an indicator of drug toxicity (PubMed:12051842). The enzyme-DNA
CC       intermediate is also the target of a number of topoisomerase poisons,
CC       including toxin CcdB (PubMed:1324324, PubMed:8254658).
CC       {ECO:0000269|PubMed:1324324, ECO:0000269|PubMed:3031051,
CC       ECO:0000269|PubMed:8254658, ECO:0000305|PubMed:12051842}.
CC   -!- MISCELLANEOUS: Few gyrases are as efficient as E.coli at forming
CC       negative supercoils (PubMed:22457352, PubMed:17400739). Not all
CC       organisms have 2 type II topoisomerases; in organisms with a single
CC       type II topoisomerase this enzyme also has to decatenate newly
CC       replicated chromosomes. {ECO:0000255|HAMAP-Rule:MF_01897,
CC       ECO:0000269|PubMed:17400739, ECO:0000269|PubMed:22457352}.
CC   -!- SIMILARITY: Belongs to the type II topoisomerase GyrA/ParC subunit
CC       family. {ECO:0000255|HAMAP-Rule:MF_01897}.
DR   EMBL; X06373; CAA29676.1; -; Genomic_DNA.
DR   EMBL; X06744; CAA29919.1; -; Genomic_DNA.
DR   EMBL; M15631; AAA23948.1; -; Genomic_DNA.
DR   EMBL; U00096; AAC75291.1; -; Genomic_DNA.
DR   EMBL; AP009048; BAA16048.1; -; Genomic_DNA.
DR   EMBL; Y00544; CAA68611.1; -; Genomic_DNA.
DR   PIR; S02340; ITECAP.
DR   RefSeq; NP_416734.1; NC_000913.3.
DR   RefSeq; WP_001281242.1; NZ_LN832404.1.
DR   PDB; 1AB4; X-ray; 2.80 A; A=30-522.
DR   PDB; 1X75; X-ray; 2.80 A; A/B=363-494.
DR   PDB; 1ZI0; X-ray; 2.60 A; A/B=535-841.
DR   PDB; 2Y3P; X-ray; 2.62 A; A/B=2-523.
DR   PDB; 3NUH; X-ray; 3.10 A; A=1-525.
DR   PDB; 4ELY; X-ray; 1.93 A; A/B=363-497.
DR   PDBsum; 1AB4; -.
DR   PDBsum; 1X75; -.
DR   PDBsum; 1ZI0; -.
DR   PDBsum; 2Y3P; -.
DR   PDBsum; 3NUH; -.
DR   PDBsum; 4ELY; -.
DR   SMR; P0AES4; -.
DR   BioGrid; 4262132; 294.
DR   ComplexPortal; CPX-2177; GyrA-GyrB complex.
DR   DIP; DIP-36179N; -.
DR   IntAct; P0AES4; 53.
DR   MINT; P0AES4; -.
DR   STRING; 511145.b2231; -.
DR   BindingDB; P0AES4; -.
DR   ChEMBL; CHEMBL1858; -.
DR   DrugBank; DB00537; Ciprofloxacin.
DR   DrugBank; DB11943; Delafloxacin.
DR   DrugCentral; P0AES4; -.
DR   SWISS-2DPAGE; P0AES4; -.
DR   EPD; P0AES4; -.
DR   jPOST; P0AES4; -.
DR   PaxDb; P0AES4; -.
DR   PRIDE; P0AES4; -.
DR   EnsemblBacteria; AAC75291; AAC75291; b2231.
DR   EnsemblBacteria; BAA16048; BAA16048; BAA16048.
DR   GeneID; 946614; -.
DR   KEGG; ecj:JW2225; -.
DR   KEGG; eco:b2231; -.
DR   PATRIC; fig|1411691.4.peg.4; -.
DR   EchoBASE; EB0418; -.
DR   eggNOG; ENOG4105C24; Bacteria.
DR   eggNOG; COG0188; LUCA.
DR   HOGENOM; HOG000076278; -.
DR   InParanoid; P0AES4; -.
DR   KO; K02469; -.
DR   PhylomeDB; P0AES4; -.
DR   BioCyc; EcoCyc:EG10423-MONOMER; -.
DR   BioCyc; ECOL316407:JW2225-MONOMER; -.
DR   BioCyc; MetaCyc:EG10423-MONOMER; -.
DR   EvolutionaryTrace; P0AES4; -.
DR   PRO; PR:P0AES4; -.
DR   Proteomes; UP000000318; Chromosome.
DR   Proteomes; UP000000625; Chromosome.
DR   GO; GO:0005694; C:chromosome; IEA:InterPro.
DR   GO; GO:0005737; C:cytoplasm; IDA:EcoliWiki.
DR   GO; GO:0005829; C:cytosol; IDA:EcoCyc.
DR   GO; GO:0009330; C:DNA topoisomerase type II (double strand cut, ATP-hydrolyzing) complex; IBA:GO_Central.
DR   GO; GO:0016020; C:membrane; HDA:UniProtKB.
DR   GO; GO:0005524; F:ATP binding; IBA:GO_Central.
DR   GO; GO:0003677; F:DNA binding; IDA:EcoliWiki.
DR   GO; GO:0034335; F:DNA negative supercoiling activity; IDA:UniProtKB.
DR   GO; GO:0003918; F:DNA topoisomerase type II (double strand cut, ATP-hydrolyzing) activity; IDA:CACAO.
DR   GO; GO:0008094; F:DNA-dependent ATPase activity; IDA:EcoliWiki.
DR   GO; GO:0042802; F:identical protein binding; IPI:IntAct.
DR   GO; GO:0006265; P:DNA topological change; IMP:EcoliWiki.
DR   GO; GO:0006261; P:DNA-dependent DNA replication; IEA:UniProtKB-UniRule.
DR   GO; GO:0046677; P:response to antibiotic; IEA:UniProtKB-KW.
DR   GO; GO:0042493; P:response to drug; IMP:EcoliWiki.
DR   GO; GO:0006351; P:transcription, DNA-templated; IDA:EcoliWiki.
DR   CDD; cd00187; TOP4c; 1.
DR   Gene3D; 1.10.268.10; -; 1.
DR   Gene3D; 2.120.10.90; -; 1.
DR   Gene3D; 3.90.199.10; -; 1.
DR   HAMAP; MF_01897; GyrA; 1.
DR   InterPro; IPR005743; GyrA.
DR   InterPro; IPR006691; GyrA/parC_rep.
DR   InterPro; IPR035516; Gyrase/topoIV_suA_C.
DR   InterPro; IPR013760; Topo_IIA-like_dom_sf.
DR   InterPro; IPR002205; Topo_IIA_A/C.
DR   InterPro; IPR013758; Topo_IIA_A/C_ab.
DR   InterPro; IPR013757; Topo_IIA_A_a_sf.
DR   Pfam; PF03989; DNA_gyraseA_C; 6.
DR   Pfam; PF00521; DNA_topoisoIV; 1.
DR   SMART; SM00434; TOP4c; 1.
DR   SUPFAM; SSF101904; SSF101904; 1.
DR   SUPFAM; SSF56719; SSF56719; 1.
PE   1: Evidence at protein level;
DR   PRODOM; P0AES4.
DR   SWISS-2DPAGE; P0AES4.
KW   3D-structure; Antibiotic resistance; ATP-binding; Cytoplasm;
KW   Direct protein sequencing; DNA-binding; Isomerase; Nucleotide-binding;
KW   Reference proteome; Topoisomerase.
FT   INIT_MET        1
FT                   /note="Removed"
FT                   /evidence="ECO:0000269|PubMed:3029031"
FT   CHAIN           2..875
FT                   /note="DNA gyrase subunit A"
FT                   /id="PRO_0000145232"
FT   REGION          531..841
FT                   /note="C-terminal domain (CTD)"
FT                   /evidence="ECO:0000303|PubMed:15897198"
FT   REGION          842..875
FT                   /note="Acidic tail"
FT                   /evidence="ECO:0000303|PubMed:22457353"
FT   MOTIF           560..566
FT                   /note="GyrA-box"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01897,
FT                   ECO:0000303|PubMed:9426128"
FT   ACT_SITE        122
FT                   /note="O-(5'-phospho-DNA)-tyrosine intermediate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01897,
FT                   ECO:0000269|PubMed:3031051"
FT   VARIANT         67
FT                   /note="A -> S (in PPA-10; quinolone-resistant)"
FT                   /evidence="ECO:0000269|PubMed:2168148"
FT   VARIANT         81
FT                   /note="G -> C (in NAL-97; quinolone-resistant)"
FT                   /evidence="ECO:0000269|PubMed:2168148"
FT   VARIANT         83
FT                   /note="S -> L (in NAL-51, NAL-112, NAL-118, NAL-119 and
FT                   strains 58, 158, 218, 231 and 235; quinolone-resistant)"
FT                   /evidence="ECO:0000269|PubMed:1850972,
FT                   ECO:0000269|PubMed:2168148"
FT   VARIANT         83
FT                   /note="S -> W (in PPA-18 and strains 233 and 227;
FT                   quinolone-resistant)"
FT                   /evidence="ECO:0000269|PubMed:1850972,
FT                   ECO:0000269|PubMed:2168148, ECO:0000269|PubMed:2548439"
FT   VARIANT         84
FT                   /note="A -> P (in PPA-05; quinolone-resistant)"
FT                   /evidence="ECO:0000269|PubMed:2168148"
FT   VARIANT         87
FT                   /note="D -> N (in NAL-113 and OV6; quinolone-resistant)"
FT                   /evidence="ECO:0000269|PubMed:2168148,
FT                   ECO:0000269|PubMed:2834621"
FT   VARIANT         87
FT                   /note="D -> V (in strain: 202; partially quinolone-
FT                   resistant)"
FT                   /evidence="ECO:0000269|PubMed:1850972"
FT   VARIANT         106
FT                   /note="Q -> H (in NAL-89; quinolone-resistant)"
FT                   /evidence="ECO:0000269|PubMed:2168148"
FT   VARIANT         678
FT                   /note="D -> E (in strain: 227)"
FT                   /evidence="ECO:0000269|PubMed:2548439"
FT   VARIANT         798
FT                   /note="I -> IMMI (in strain OV6; quinolone-resistant)"
FT                   /evidence="ECO:0000269|PubMed:2834621"
FT   VARIANT         828
FT                   /note="A -> S (in strain: 227)"
FT                   /evidence="ECO:0000269|PubMed:2548439"
FT   MUTAGEN         32
FT                   /note="R->A,Q: Nearly abolishes DNA supercoiling. Reduces
FT                   quinolone-induced DNA cleavage and relaxation."
FT                   /evidence="ECO:0000269|PubMed:12051842"
FT   MUTAGEN         47
FT                   /note="R->Q: Nearly abolishes DNA supercoiling. Reduces
FT                   quinolone-induced DNA cleavage. Slightly reduces DNA
FT                   relaxation."
FT                   /evidence="ECO:0000269|PubMed:12051842"
FT   MUTAGEN         78
FT                   /note="H->A: Nearly abolishes DNA supercoiling. Reduces
FT                   quinolone-induced DNA cleavage and DNA relaxation."
FT                   /evidence="ECO:0000269|PubMed:12051842"
FT   MUTAGEN         80
FT                   /note="H->A: Reduces DNA supercoiling. Slightly reduces
FT                   quinolone-induced DNA cleavage. No effect on DNA
FT                   relaxation."
FT                   /evidence="ECO:0000269|PubMed:12051842"
FT   MUTAGEN         83
FT                   /note="S->A: Resistant to fluoroquinolones."
FT                   /evidence="ECO:0000269|PubMed:1850970"
FT   MUTAGEN         106
FT                   /note="Q->R: Resistant to fluoroquinolones."
FT                   /evidence="ECO:0000269|PubMed:1850970"
FT   MUTAGEN         462
FT                   /note="R->C: In gyrA462; resistant to cytotoxic protein
FT                   CcdB, but not to the quinoline antibiotic enoxacin, has no
FT                   effect on DNA supercoiling. Does not interact with CcdB."
FT                   /evidence="ECO:0000269|PubMed:1324324,
FT                   ECO:0000269|PubMed:8254658"
FT   MUTAGEN         560..566
FT                   /note="QRRGGKG->AAAAAAA: Loss of gyrase-mediated DNA
FT                   wrapping, nearly complete loss of DNA supercoiling
FT                   activity, no change in DNA supercoil relaxation or DNA
FT                   decatenation activity."
FT                   /evidence="ECO:0000269|PubMed:16332690"
FT   MUTAGEN         560..566
FT                   /note="Missing: Loss of gyrase-mediated DNA wrapping,
FT                   nearly complete loss of DNA supercoiling activity, no
FT                   change in DNA supercoil relaxation or DNA decatenation
FT                   activity."
FT                   /evidence="ECO:0000269|PubMed:16332690"
FT   MUTAGEN         842..856
FT                   /note="Missing: Gains ability to wrap DNA around itself in
FT                   the absence of GyrB; holoenzyme gains ability to wrap DNA
FT                   in the absence of ATP analogs, but reduces ATP-dependent
FT                   supercoiling activity 50-fold, DNA is not as extensively
FT                   negatively supercoiled, has 10-fold less ATP-independent
FT                   negative supercoiled DNA relaxation activity, no change in
FT                   ATPase activity of holoenzyme, no change in decatenation
FT                   ability. Isolated CTD gains ability to wrap DNA around
FT                   itself in the absence of GyrB, binds DNA better than wild-
FT                   type CTD."
FT                   /evidence="ECO:0000269|PubMed:22457352,
FT                   ECO:0000269|PubMed:22457353"
FT   MUTAGEN         854..875
FT                   /note="Missing: Isolated CTD gains ability to wrap DNA
FT                   around itself in the absence of GyrB, binds DNA better than
FT                   wild-type CTD."
FT                   /evidence="ECO:0000269|PubMed:22457353"
FT   TURN            31..33
FT                   /evidence="ECO:0000244|PDB:1AB4"
FT   TURN            37..39
FT                   /evidence="ECO:0000244|PDB:1AB4"
FT   HELIX           43..54
FT                   /evidence="ECO:0000244|PDB:1AB4"
FT   STRAND          59..61
FT                   /evidence="ECO:0000244|PDB:1AB4"
FT   HELIX           66..76
FT                   /evidence="ECO:0000244|PDB:1AB4"
FT   HELIX           82..91
FT                   /evidence="ECO:0000244|PDB:1AB4"
FT   TURN            95..97
FT                   /evidence="ECO:0000244|PDB:1AB4"
FT   STRAND          102..107
FT                   /evidence="ECO:0000244|PDB:1AB4"
FT   TURN            120..122
FT                   /evidence="ECO:0000244|PDB:1AB4"
FT   STRAND          124..127
FT                   /evidence="ECO:0000244|PDB:1AB4"
FT   HELIX           131..134
FT                   /evidence="ECO:0000244|PDB:1AB4"
FT   TURN            136..141
FT                   /evidence="ECO:0000244|PDB:1AB4"
FT   STRAND          145..147
FT                   /evidence="ECO:0000244|PDB:1AB4"
FT   STRAND          151..158
FT                   /evidence="ECO:0000244|PDB:1AB4"
FT   HELIX           165..169
FT                   /evidence="ECO:0000244|PDB:1AB4"
FT   STRAND          171..173
FT                   /evidence="ECO:0000244|PDB:1AB4"
FT   STRAND          180..182
FT                   /evidence="ECO:0000244|PDB:1AB4"
FT   HELIX           187..199
FT                   /evidence="ECO:0000244|PDB:1AB4"
FT   HELIX           205..208
FT                   /evidence="ECO:0000244|PDB:1AB4"
FT   TURN            209..211
FT                   /evidence="ECO:0000244|PDB:1AB4"
FT   HELIX           227..235
FT                   /evidence="ECO:0000244|PDB:1AB4"
FT   STRAND          236..243
FT                   /evidence="ECO:0000244|PDB:1AB4"
FT   STRAND          245..249
FT                   /evidence="ECO:0000244|PDB:1AB4"
FT   STRAND          258..263
FT                   /evidence="ECO:0000244|PDB:1AB4"
FT   HELIX           270..281
FT                   /evidence="ECO:0000244|PDB:1AB4"
FT   TURN            282..284
FT                   /evidence="ECO:0000244|PDB:1AB4"
FT   STRAND          292..294
FT                   /evidence="ECO:0000244|PDB:1AB4"
FT   STRAND          298..300
FT                   /evidence="ECO:0000244|PDB:1AB4"
FT   STRAND          303..305
FT                   /evidence="ECO:0000244|PDB:1AB4"
FT   HELIX           314..323
FT                   /evidence="ECO:0000244|PDB:1AB4"
FT   STRAND          327..333
FT                   /evidence="ECO:0000244|PDB:1AB4"
FT   STRAND          335..338
FT                   /evidence="ECO:0000244|PDB:1AB4"
FT   STRAND          341..344
FT                   /evidence="ECO:0000244|PDB:1AB4"
FT   HELIX           347..388
FT                   /evidence="ECO:0000244|PDB:1AB4"
FT   HELIX           390..399
FT                   /evidence="ECO:0000244|PDB:1AB4"
FT   STRAND          400..402
FT                   /evidence="ECO:0000244|PDB:1X75"
FT   HELIX           403..412
FT                   /evidence="ECO:0000244|PDB:1AB4"
FT   HELIX           419..421
FT                   /evidence="ECO:0000244|PDB:1AB4"
FT   STRAND          441..449
FT                   /evidence="ECO:0000244|PDB:1AB4"
FT   HELIX           452..459
FT                   /evidence="ECO:0000244|PDB:1AB4"
FT   HELIX           463..466
FT                   /evidence="ECO:0000244|PDB:1AB4"
FT   HELIX           468..493
FT                   /evidence="ECO:0000244|PDB:1AB4"
FT   HELIX           495..513
FT                   /evidence="ECO:0000244|PDB:1AB4"
FT   STRAND          519..521
FT                   /evidence="ECO:0000244|PDB:1AB4"
FT   STRAND          538..544
FT                   /evidence="ECO:0000244|PDB:1ZI0"
FT   STRAND          547..553
FT                   /evidence="ECO:0000244|PDB:1ZI0"
FT   HELIX           556..560
FT                   /evidence="ECO:0000244|PDB:1ZI0"
FT   STRAND          578..585
FT                   /evidence="ECO:0000244|PDB:1ZI0"
FT   STRAND          589..594
FT                   /evidence="ECO:0000244|PDB:1ZI0"
FT   STRAND          597..603
FT                   /evidence="ECO:0000244|PDB:1ZI0"
FT   HELIX           604..606
FT                   /evidence="ECO:0000244|PDB:1ZI0"
FT   STRAND          612..614
FT                   /evidence="ECO:0000244|PDB:1ZI0"
FT   HELIX           619..621
FT                   /evidence="ECO:0000244|PDB:1ZI0"
FT   STRAND          631..638
FT                   /evidence="ECO:0000244|PDB:1ZI0"
FT   STRAND          645..650
FT                   /evidence="ECO:0000244|PDB:1ZI0"
FT   STRAND          653..659
FT                   /evidence="ECO:0000244|PDB:1ZI0"
FT   HELIX           660..663
FT                   /evidence="ECO:0000244|PDB:1ZI0"
FT   STRAND          671..674
FT                   /evidence="ECO:0000244|PDB:1ZI0"
FT   STRAND          682..688
FT                   /evidence="ECO:0000244|PDB:1ZI0"
FT   STRAND          693..698
FT                   /evidence="ECO:0000244|PDB:1ZI0"
FT   STRAND          701..707
FT                   /evidence="ECO:0000244|PDB:1ZI0"
FT   HELIX           708..710
FT                   /evidence="ECO:0000244|PDB:1ZI0"
FT   STRAND          732..736
FT                   /evidence="ECO:0000244|PDB:1ZI0"
FT   STRAND          743..748
FT                   /evidence="ECO:0000244|PDB:1ZI0"
FT   STRAND          751..756
FT                   /evidence="ECO:0000244|PDB:1ZI0"
FT   HELIX           758..760
FT                   /evidence="ECO:0000244|PDB:1ZI0"
FT   STRAND          771..774
FT                   /evidence="ECO:0000244|PDB:1ZI0"
FT   TURN            778..780
FT                   /evidence="ECO:0000244|PDB:1ZI0"
FT   STRAND          782..789
FT                   /evidence="ECO:0000244|PDB:1ZI0"
FT   STRAND          794..801
FT                   /evidence="ECO:0000244|PDB:1ZI0"
FT   STRAND          804..808
FT                   /evidence="ECO:0000244|PDB:1ZI0"
FT   HELIX           809..811
FT                   /evidence="ECO:0000244|PDB:1ZI0"
FT   STRAND          833..838
FT                   /evidence="ECO:0000244|PDB:1ZI0"
SQ   SEQUENCE   875 AA;  96964 MW;  3FD5BD52A5969069 CRC64;
     MSDLAREITP VNIEEELKSS YLDYAMSVIV GRALPDVRDG LKPVHRRVLY AMNVLGNDWN
     KAYKKSARVV GDVIGKYHPH GDSAVYDTIV RMAQPFSLRY MLVDGQGNFG SIDGDSAAAM
     RYTEIRLAKI AHELMADLEK ETVDFVDNYD GTEKIPDVMP TKIPNLLVNG SSGIAVGMAT
     NIPPHNLTEV INGCLAYIDD EDISIEGLME HIPGPDFPTA AIINGRRGIE EAYRTGRGKV
     YIRARAEVEV DAKTGRETII VHEIPYQVNK ARLIEKIAEL VKEKRVEGIS ALRDESDKDG
     MRIVIEVKRD AVGEVVLNNL YSQTQLQVSF GINMVALHHG QPKIMNLKDI IAAFVRHRRE
     VVTRRTIFEL RKARDRAHIL EALAVALANI DPIIELIRHA PTPAEAKTAL VANPWQLGNV
     AAMLERAGDD AARPEWLEPE FGVRDGLYYL TEQQAQAILD LRLQKLTGLE HEKLLDEYKE
     LLDQIAELLR ILGSADRLME VIREELELVR EQFGDKRRTE ITANSADINL EDLITQEDVV
     VTLSHQGYVK YQPLSEYEAQ RRGGKGKSAA RIKEEDFIDR LLVANTHDHI LCFSSRGRVY
     SMKVYQLPEA TRGARGRPIV NLLPLEQDER ITAILPVTEF EEGVKVFMAT ANGTVKKTVL
     TEFNRLRTAG KVAIKLVDGD ELIGVDLTSG EDEVMLFSAE GKVVRFKESS VRAMGCNTTG
     VRGIRLGEGD KVVSLIVPRG DGAILTATQN GYGKRTAVAE YPTKSRATKG VISIKVTERN
     GLVVGAVQVD DCDQIMMITD AGTLVRTRVS EISIVGRNTQ GVILIRTAED ENVVGLQRVA
     EPVDEEDLDT IDGSAAEGDD EIAPEVDVDD EPEEE
//

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