(data stored in SCRATCH3701 zone)

SWISSPROT: GYRA_PSEAE

ID   GYRA_PSEAE              Reviewed;         923 AA.
AC   P48372;
DT   01-FEB-1996, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1996, sequence version 1.
DT   11-DEC-2019, entry version 127.
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};
GN   Name=gyrA {ECO:0000255|HAMAP-Rule:MF_01897}; OrderedLocusNames=PA3168;
OS   Pseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM
OS   14847 / LMG 12228 / 1C / PRS 101 / PAO1).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC   Pseudomonadaceae; Pseudomonas.
OX   NCBI_TaxID=208964;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C /
RC   PRS 101 / PAO1;
RX   PubMed=7811002; DOI=10.1128/aac.38.9.1944;
RA   Kureishi A., Diver J.M., Beckthold B., Schollaardt T., Bryan L.E.;
RT   "Cloning and nucleotide sequence of Pseudomonas aeruginosa DNA gyrase gyrA
RT   gene from strain PAO1 and quinolone-resistant clinical isolates.";
RL   Antimicrob. Agents Chemother. 38:1944-1952(1994).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C /
RC   PRS 101 / PAO1;
RX   PubMed=10984043; DOI=10.1038/35023079;
RA   Stover C.K., Pham X.-Q.T., Erwin A.L., Mizoguchi S.D., Warrener P.,
RA   Hickey M.J., Brinkman F.S.L., Hufnagle W.O., Kowalik D.J., Lagrou M.,
RA   Garber R.L., Goltry L., Tolentino E., Westbrock-Wadman S., Yuan Y.,
RA   Brody L.L., Coulter S.N., Folger K.R., Kas A., Larbig K., Lim R.M.,
RA   Smith K.A., Spencer D.H., Wong G.K.-S., Wu Z., Paulsen I.T., Reizer J.,
RA   Saier M.H. Jr., Hancock R.E.W., Lory S., Olson M.V.;
RT   "Complete genome sequence of Pseudomonas aeruginosa PAO1, an opportunistic
RT   pathogen.";
RL   Nature 406:959-964(2000).
CC   -!- FUNCTION: A type II topoisomerase that negatively supercoils closed
CC       circular double-stranded (ds) DNA in an ATP-dependent manner to
CC       modulate DNA topology and maintain chromosomes in an underwound state.
CC       Negative supercoiling favors strand separation, and DNA replication,
CC       transcription, recombination and repair, all of which involve strand
CC       separation. Also able to catalyze the interconversion of other
CC       topological isomers of dsDNA rings, including catenanes and knotted
CC       rings. Type II topoisomerases break and join 2 DNA strands
CC       simultaneously in an ATP-dependent manner. {ECO:0000255|HAMAP-
CC       Rule:MF_01897}.
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-
CC         Rule:MF_01897};
CC   -!- SUBUNIT: Heterotetramer, composed of two GyrA and two GyrB chains. In
CC       the heterotetramer, GyrA contains the active site tyrosine that forms a
CC       transient covalent intermediate with DNA, while GyrB binds cofactors
CC       and catalyzes ATP hydrolysis. {ECO:0000255|HAMAP-Rule:MF_01897}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_01897}.
CC   -!- MISCELLANEOUS: Few gyrases are as efficient as E.coli at forming
CC       negative supercoils. Not all organisms have 2 type II topoisomerases;
CC       in organisms with a single type II topoisomerase this enzyme also has
CC       to decatenate newly replicated chromosomes. {ECO:0000255|HAMAP-
CC       Rule:MF_01897}.
CC   -!- SIMILARITY: Belongs to the type II topoisomerase GyrA/ParC subunit
CC       family. {ECO:0000255|HAMAP-Rule:MF_01897}.
DR   EMBL; L29417; AAA68625.1; -; Genomic_DNA.
DR   EMBL; AE004091; AAG06556.1; -; Genomic_DNA.
DR   PIR; H83248; H83248.
DR   RefSeq; NP_251858.1; NC_002516.2.
DR   RefSeq; WP_003091448.1; NZ_QZGE01000023.1.
DR   SMR; P48372; -.
DR   ChEMBL; CHEMBL3390828; -.
DR   PaxDb; P48372; -.
DR   PRIDE; P48372; -.
DR   EnsemblBacteria; AAG06556; AAG06556; PA3168.
DR   GeneID; 882800; -.
DR   KEGG; pae:PA3168; -.
DR   PATRIC; fig|208964.12.peg.3311; -.
DR   PseudoCAP; PA3168; -.
DR   eggNOG; ENOG4105C24; Bacteria.
DR   eggNOG; COG0188; LUCA.
DR   HOGENOM; HOG000076278; -.
DR   InParanoid; P48372; -.
DR   KO; K02469; -.
DR   OMA; THHWLLF; -.
DR   PhylomeDB; P48372; -.
DR   BioCyc; PAER208964:G1FZ6-3228-MONOMER; -.
DR   Proteomes; UP000002438; Chromosome.
DR   GO; GO:0005694; C:chromosome; IEA:InterPro.
DR   GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR   GO; GO:0009330; C:DNA topoisomerase type II (double strand cut, ATP-hydrolyzing) complex; IBA:GO_Central.
DR   GO; GO:0005524; F:ATP binding; IBA:GO_Central.
DR   GO; GO:0003677; F:DNA binding; IBA:GO_Central.
DR   GO; GO:0003918; F:DNA topoisomerase type II (double strand cut, ATP-hydrolyzing) activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0006265; P:DNA topological change; IBA:GO_Central.
DR   GO; GO:0006261; P:DNA-dependent DNA replication; IEA:UniProtKB-UniRule.
DR   CDD; cd00187; TOP4c; 1.
DR   Gene3D; 1.10.268.10; -; 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   3: Inferred from homology;
DR   PRODOM; P48372.
DR   SWISS-2DPAGE; P48372.
KW   ATP-binding; Cytoplasm; DNA-binding; Isomerase; Nucleotide-binding;
KW   Reference proteome; Topoisomerase.
FT   CHAIN           1..923
FT                   /note="DNA gyrase subunit A"
FT                   /id="PRO_0000145245"
FT   MOTIF           561..567
FT                   /note="GyrA-box"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01897"
FT   ACT_SITE        122
FT                   /note="O-(5'-phospho-DNA)-tyrosine intermediate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01897"
SQ   SEQUENCE   923 AA;  101135 MW;  0025DFE08CDD1BEC CRC64;
     MGELAKEILP VNIEDELKQS YLDYAMSVIV GRALPDARDG LKPVHRRVLY AMSELGNDWN
     KPYKKSARVV GDVIGKYHPH GDTAVYDTIV RMAQPFSLRY MLVDGQGNFG SVDGDNAAAM
     RYTEVRMAKL AHELLADLEK ETVDWVPNYD GTEQIPAVMP TKIPNLLVNG SSGIAVGMAT
     NIPPHNLGEV IDGCLALMDN PDLTVDELMQ YIPGPDFPTA GIINGRAGII EAYRTGRGRI
     YIRARAVVEE MEKGGGREQI IITELPYQLN KARLIEKIAE LVKEKKIEGI SELRDESDKD
     GMRVVIELRR GEVGEVVLNN LYAQTQLQSV FGINVVALVD GQPRTLNLKD MLEVFVRHRR
     EVVTRRTVYE LRKARERGHI LEGQAVALSN IDPVIELIKS SPTPAEAKER LIATAWESSA
     VEAMVERAGA DACRPEDLDP QYGLRDGKYY LSPEQAQAIL ELRLHRLTGL EHEKLLSEYQ
     EILNLIGELI RILTNPARLM EVIREELEAV KAEFGDARRT EIVASQVDLT IADLITEEDR
     VVTISHGGYA KSQPLAAYQA QRRGGKGKSA TGMKDEDYIE HLLVANSHAT LLLFSSKGKV
     YWLRTFEIPE ASRTARGRPL VNLLPLDEGE RITAMLQIDL EALQQNGGAD DDLDEAEGAV
     LEGEVVEAAE VEEVEGETAE LVAEPTGAYI FMATAFGTVK KTPLVQFSRP RSSGLIALKL
     EEGDTLIAAA ITDGAKEVML FSSAGKVIRF AESVVRIMGR NARGVRGMRL GKGQQLISML
     IPESGAQILT ASERGFGKRT PLSKFPRRGR GGQGVIAMVT NERNGALIAA VQVQEGEEIM
     LISDQGTLVR TRVDEVSLSG RNTQGVTLIK LASDEVLVGL ERVQEPSGGD DEDLPEGEEA
     AESLGESAES ESEPAAEAEG NEE
//

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