(data stored in SCRATCH3701 zone)

SWISSPROT: Q7BSI9_LISMN

ID   Q7BSI9_LISMN            Unreviewed;       842 AA.
AC   Q7BSI9;
DT   16-MAY-2012, integrated into UniProtKB/TrEMBL.
DT   16-MAY-2012, sequence version 1.
DT   11-DEC-2019, entry version 76.
DE   RecName: Full=DNA gyrase subunit A {ECO:0000256|HAMAP-Rule:MF_01897};
DE            EC=5.6.2.2 {ECO:0000256|HAMAP-Rule:MF_01897};
GN   Name=gyrA {ECO:0000256|HAMAP-Rule:MF_01897,
GN   ECO:0000313|EMBL:AAM48483.1};
GN   ORFNames=B4Y57_09150 {ECO:0000313|EMBL:MIV56674.1}, D3B94_08705
GN   {ECO:0000313|EMBL:RJB33311.1}, FORC68_0007
GN   {ECO:0000313|EMBL:QBZ17235.1};
OS   Listeria monocytogenes.
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Listeriaceae; Listeria.
OX   NCBI_TaxID=1639 {ECO:0000313|EMBL:AAM48483.1};
RN   [1] {ECO:0000313|EMBL:AAM48483.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=EGD {ECO:0000313|EMBL:AAM48483.1};
RX   PubMed=12039883; DOI=10.1093/jac/dkf065;
RA   Lampidis R., Kostrewa D., Hof H.;
RT   "Molecular characterization of the genes encoding DNA gyrase and
RT   topoisomerase IV of Listeria monocytogenes.";
RL   J. Antimicrob. Chemother. 49:917-924(2002).
RN   [2] {ECO:0000313|EMBL:QBZ17235.1, ECO:0000313|Proteomes:UP000295446}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NCCP 15743 {ECO:0000313|EMBL:QBZ17235.1,
RC   ECO:0000313|Proteomes:UP000295446};
RA   Kim J., Ryu S.;
RT   "Complete genome sequence of Listeria monocytogenes FORC_68 chromosome.";
RL   Submitted (MAY-2018) to the EMBL/GenBank/DDBJ databases.
RN   [3] {ECO:0000313|EMBL:MIV56674.1, ECO:0000313|Proteomes:UP000270746}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CFSAN060949 {ECO:0000313|EMBL:MIV56674.1,
RC   ECO:0000313|Proteomes:UP000270746};
RG   GenomeTrakr: Next Generation Sequencing Network for Food Pathogen Tracability;
RL   Submitted (AUG-2018) to the EMBL/GenBank/DDBJ databases.
RN   [4] {ECO:0000313|EMBL:RJB33311.1, ECO:0000313|Proteomes:UP000283665}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=N13-0048 {ECO:0000313|EMBL:RJB33311.1,
RC   ECO:0000313|Proteomes:UP000283665};
RA   Haigh R.D., Ralph J.D., Zamudio R., De Ste Croix M., Tasara T., Kwun M.J.,
RA   Croucher N.J., Bentley S.D., Stephan R., Oggioni M.R.;
RT   "Draft genome sequence of 150 Swiss Listeria monocytogenes isolates from
RT   food and human origin.";
RL   Submitted (SEP-2018) to the EMBL/GenBank/DDBJ databases.
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:0000256|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:0000256|HAMAP-Rule:MF_01897,
CC         ECO:0000256|SAAS:SAAS01218217};
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:0000256|HAMAP-Rule:MF_01897}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|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:0000256|HAMAP-
CC       Rule:MF_01897}.
CC   -!- SIMILARITY: Belongs to the topoisomerase GyrA/ParC subunit family.
CC       {ECO:0000256|HAMAP-Rule:MF_01897}.
CC   -!- SIMILARITY: Belongs to the type II topoisomerase GyrA/ParC subunit
CC       family. {ECO:0000256|SAAS:SAAS01062860}.
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DR   EMBL; AF084042; AAM48483.1; -; Genomic_DNA.
DR   EMBL; RSVN01000002; MIV56674.1; -; Genomic_DNA.
DR   EMBL; CP029175; QBZ17235.1; -; Genomic_DNA.
DR   EMBL; QYFE01000003; RJB33311.1; -; Genomic_DNA.
DR   PIR; AH1432; AH1432.
DR   RefSeq; WP_003723770.1; NZ_VOXL01000014.1.
DR   GeneID; 39647402; -.
DR   KEGG; lmoe:BN418_0007; -.
DR   KEGG; lmom:IJ09_10375; -.
DR   PATRIC; fig|1234141.3.peg.7; -.
DR   eggNOG; ENOG4105C24; Bacteria.
DR   eggNOG; COG0188; LUCA.
DR   KO; K02469; -.
DR   Proteomes; UP000270746; Unassembled WGS sequence.
DR   Proteomes; UP000283665; Unassembled WGS sequence.
DR   Proteomes; UP000295446; Chromosome.
DR   GO; GO:0005694; C:chromosome; IEA:InterPro.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0003677; F:DNA binding; IEA:UniProtKB-UniRule.
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; IEA:UniProtKB-UniRule.
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; 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   3: Inferred from homology;
DR   PRODOM; Q7BSI9.
DR   SWISS-2DPAGE; Q7BSI9.
KW   ATP-binding {ECO:0000256|HAMAP-Rule:MF_01897,
KW   ECO:0000256|SAAS:SAAS01062880}; Coiled coil {ECO:0000256|SAM:Coils};
KW   Cytoplasm {ECO:0000256|HAMAP-Rule:MF_01897};
KW   DNA-binding {ECO:0000256|HAMAP-Rule:MF_01897,
KW   ECO:0000256|SAAS:SAAS01062879};
KW   Isomerase {ECO:0000256|HAMAP-Rule:MF_01897, ECO:0000256|SAAS:SAAS00972514,
KW   ECO:0000313|EMBL:RJB33311.1};
KW   Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_01897,
KW   ECO:0000256|SAAS:SAAS01062871};
KW   Topoisomerase {ECO:0000256|HAMAP-Rule:MF_01897,
KW   ECO:0000256|SAAS:SAAS00974554}.
FT   DOMAIN          12..465
FT                   /note="TOP4c"
FT                   /evidence="ECO:0000259|SMART:SM00434"
FT   REGION          807..842
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          437..485
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   MOTIF           527..533
FT                   /note="GyrA-box"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01897"
FT   ACT_SITE        123
FT                   /note="O-(5'-phospho-DNA)-tyrosine intermediate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01897"
SQ   SEQUENCE   842 AA;  94743 MW;  7D47F0EF0B9CE652 CRC64;
     MAETPNQRIT EINLNKEMRT SFLDYAMSVI VARALPDVRD GLKPVHRRIL YAMNDLGMTS
     DKAYKKSARI VGEVIGKYHP HGDTAVYFTM VRMAQDFSYR NMLVDGHGNF GSVDGDMAAA
     MRYTEARMSK ISMELLRDIN KDTIDYADNY DGSEREPVIL PARFPNLLVN GSSGIAVGMA
     TNIPTHHLGE VIDGVLALSH DPEITIRDLM EYIPGPDFPT AGMIMGRSGI RRAYESGRGS
     ITVRGRVDIE EKKNGKETIV ITEIPYQVNK ARLVERIAEL AREKKIDGIT SLNDESDRSG
     MRIVIEVRRD ISASVIVNNL FKMTALQTTF GINMLALVDN HPKVLNLKEI LYYYLEHQKV
     VIRRRTEFEL RKAEARAHIL EGLRIALDNI DAIIKLIRGS KTSDVAKEGL MTQFNLSDKQ
     AQAILDMRLQ RLTGLEREKI EEEYQNLVAL INDLKAILAD DERILEIIRE ELEEIKVKYA
     DKRRTEILAG DLVSLEDEDL IPEEEVAITL TKRGYIKRLP LSTYRSQRRG GRGIQGMSTH
     EDDFVEHLVA TSTHDTLLFF TNTGKVYRSK GYEVPEYGRT AKGIPIINLL GIESQEQVNA
     VINLSEFTDD SYLFFTTKHG VVKRTTLSQF AKIRQSGLRA VELRENDELI SVQMTDGSKN
     MIIATKHGQS IYFPEENIRV MGRTAAGVRG IRLREDDEVI GMEVLEDDEK VLVVTEKGYG
     KQTPASQYPL RNRGGMGVKT VTITEKNGNL VAMKTVTGEE DLMLMTVSGV LIRFEIDTVS
     QTGRSAMGVK LIRLDEDEKV ATVAKVPKEE DEVELEEEID ETLITQVPDE SFEDAPGSDI
     EE
//

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