(data stored in SCRATCH zone)

SWISSPROT: Q7BSI8_LISMN

ID   Q7BSI8_LISMN            Unreviewed;       646 AA.
AC   Q7BSI8;
DT   16-MAY-2012, integrated into UniProtKB/TrEMBL.
DT   16-MAY-2012, sequence version 1.
DT   11-DEC-2019, entry version 80.
DE   RecName: Full=DNA gyrase subunit B {ECO:0000256|HAMAP-Rule:MF_01898};
DE            EC=5.6.2.2 {ECO:0000256|HAMAP-Rule:MF_01898};
GN   Name=gyrB {ECO:0000256|HAMAP-Rule:MF_01898,
GN   ECO:0000313|EMBL:AAM48481.1};
GN   ORFNames=ARJ20_03940 {ECO:0000313|EMBL:MCO31180.1}, B4Y57_09145
GN   {ECO:0000313|EMBL:MIV56673.1}, D3B94_08710
GN   {ECO:0000313|EMBL:RJB33312.1}, FORC68_0006
GN   {ECO:0000313|EMBL:QBZ17234.1}, LmNIHS28_00171
GN   {ECO:0000313|EMBL:GAM94239.1};
OS   Listeria monocytogenes.
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Listeriaceae; Listeria.
OX   NCBI_TaxID=1639 {ECO:0000313|EMBL:AAM48481.1};
RN   [1] {ECO:0000313|EMBL:AAM48481.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=EGD {ECO:0000313|EMBL:AAM48481.1};
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:GAM94239.1, ECO:0000313|Proteomes:UP000032903}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NIHS-28 {ECO:0000313|EMBL:GAM94239.1,
RC   ECO:0000313|Proteomes:UP000032903};
RX   PubMed=25492229;
RA   Kyoui D., Takahashi H., Miya S., Kuda T., Igimi S., Kimura B.;
RT   "Genetic distance in the whole-genome perspective on Listeria monocytogenes
RT   strains F2-382 and NIHS-28 that show similar subtyping results.";
RL   BMC Microbiol. 14:309-309(2014).
RN   [3] {ECO:0000313|EMBL:QBZ17234.1, ECO:0000313|Proteomes:UP000295446}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NCCP 15743 {ECO:0000313|EMBL:QBZ17234.1,
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   [4] {ECO:0000313|EMBL:MCO31180.1, ECO:0000313|Proteomes:UP000275497}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CFSAN060949 {ECO:0000313|EMBL:MIV56673.1,
RC   ECO:0000313|Proteomes:UP000270746}, and FDA00005457
RC   {ECO:0000313|EMBL:MCO31180.1, ECO:0000313|Proteomes:UP000275497};
RG   GenomeTrakr: Next Generation Sequencing Network for Food Pathogen Tracability;
RL   Submitted (JUL-2018) to the EMBL/GenBank/DDBJ databases.
RN   [5] {ECO:0000313|EMBL:RJB33312.1, ECO:0000313|Proteomes:UP000283665}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=N13-0048 {ECO:0000313|EMBL:RJB33312.1,
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_01898}.
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_01898,
CC         ECO:0000256|SAAS:SAAS01220860};
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000256|SAAS:SAAS00612567};
CC   -!- COFACTOR:
CC       Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC         Evidence={ECO:0000256|SAAS:SAAS00709652};
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_01898}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_01898}.
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_01898}.
CC   -!- SIMILARITY: Belongs to the type II topoisomerase family.
CC       {ECO:0000256|HAMAP-Rule:MF_01898}.
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DR   EMBL; AF084042; AAM48481.1; -; Genomic_DNA.
DR   EMBL; BAZD01000001; GAM94239.1; -; Genomic_DNA.
DR   EMBL; RCSC01000002; MCO31180.1; -; Genomic_DNA.
DR   EMBL; RSVN01000002; MIV56673.1; -; Genomic_DNA.
DR   EMBL; CP029175; QBZ17234.1; -; Genomic_DNA.
DR   EMBL; QYFE01000003; RJB33312.1; -; Genomic_DNA.
DR   PIR; AG1075; AG1075.
DR   RefSeq; WP_003723769.1; NZ_VPFG01000060.1.
DR   EnsemblBacteria; AGR14570; AGR14570; M643_09920.
DR   EnsemblBacteria; GAM94239; GAM94239; LmNIHS28_00171.
DR   EnsemblBacteria; OET99549; OET99549; AJL40_06900.
DR   GeneID; 39648721; -.
DR   KEGG; lmoe:BN418_0006; -.
DR   KEGG; lmok:CQ02_00030; -.
DR   KEGG; lmom:IJ09_10380; -.
DR   KEGG; lmv:Y193_01270; -.
DR   PATRIC; fig|1234141.3.peg.6; -.
DR   eggNOG; ENOG4105C7D; Bacteria.
DR   eggNOG; COG0187; LUCA.
DR   KO; K02470; -.
DR   OrthoDB; 205481at2; -.
DR   Proteomes; UP000032903; Unassembled WGS sequence.
DR   Proteomes; UP000270746; Unassembled WGS sequence.
DR   Proteomes; UP000275497; 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-KW.
DR   GO; GO:0003918; F:DNA topoisomerase type II (double strand cut, ATP-hydrolyzing) activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
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; cd03366; TOPRIM_TopoIIA_GyrB; 1.
DR   Gene3D; 3.30.230.10; -; 1.
DR   Gene3D; 3.30.565.10; -; 1.
DR   Gene3D; 3.40.50.670; -; 1.
DR   HAMAP; MF_01898; GyrB; 1.
DR   InterPro; IPR002288; DNA_gyrase_B_C.
DR   InterPro; IPR011557; GyrB.
DR   InterPro; IPR003594; HATPase_C.
DR   InterPro; IPR036890; HATPase_C_sf.
DR   InterPro; IPR020568; Ribosomal_S5_D2-typ_fold.
DR   InterPro; IPR014721; Ribosomal_S5_D2-typ_fold_subgr.
DR   InterPro; IPR001241; Topo_IIA.
DR   InterPro; IPR013760; Topo_IIA-like_dom_sf.
DR   InterPro; IPR013759; Topo_IIA_B_C.
DR   InterPro; IPR013506; Topo_IIA_bsu_dom2.
DR   InterPro; IPR018522; TopoIIA_CS.
DR   InterPro; IPR006171; TOPRIM_domain.
DR   InterPro; IPR034160; TOPRIM_GyrB.
DR   Pfam; PF00204; DNA_gyraseB; 1.
DR   Pfam; PF00986; DNA_gyraseB_C; 1.
DR   Pfam; PF02518; HATPase_c; 1.
DR   Pfam; PF01751; Toprim; 1.
DR   SMART; SM00387; HATPase_c; 1.
DR   SMART; SM00433; TOP2c; 1.
DR   SUPFAM; SSF54211; SSF54211; 1.
DR   SUPFAM; SSF55874; SSF55874; 1.
DR   SUPFAM; SSF56719; SSF56719; 1.
DR   TIGRFAMs; TIGR01059; gyrB; 1.
DR   PROSITE; PS00177; TOPOISOMERASE_II; 1.
DR   PROSITE; PS50880; TOPRIM; 1.
PE   3: Inferred from homology;
DR   PRODOM; Q7BSI8.
DR   SWISS-2DPAGE; Q7BSI8.
KW   ATP-binding {ECO:0000256|HAMAP-Rule:MF_01898,
KW   ECO:0000256|SAAS:SAAS00528655};
KW   Cytoplasm {ECO:0000256|HAMAP-Rule:MF_01898};
KW   DNA-binding {ECO:0000256|SAAS:SAAS00709661};
KW   Isomerase {ECO:0000256|HAMAP-Rule:MF_01898, ECO:0000256|SAAS:SAAS00470744,
KW   ECO:0000313|EMBL:MCO31180.1}; Magnesium {ECO:0000256|SAAS:SAAS00445358};
KW   Metal-binding {ECO:0000256|SAAS:SAAS00445373};
KW   Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_01898,
KW   ECO:0000256|SAAS:SAAS00528653};
KW   Topoisomerase {ECO:0000256|HAMAP-Rule:MF_01898,
KW   ECO:0000256|SAAS:SAAS00528650}.
FT   DOMAIN          430..544
FT                   /note="Toprim"
FT                   /evidence="ECO:0000259|PROSITE:PS50880"
SQ   SEQUENCE   646 AA;  72814 MW;  CA7722CB65AD3184 CRC64;
     MSEENITNVQ ENASDYNEDQ IQVLEGLEAV RKRPGMYIGS TSQRGLHHLV WEIVDNAIDE
     ALAGFCTEIE ITIEADNSIT VRDNGRGIPT GINEKIGRPT VEVIFTVLHA GGKFGGGGYK
     VSGGLHGVGA SVVNALSTSL EVYVHREGQK YYQRFERGDV VMDMEEQGET DYRGTIVHFT
     PDPQIFTETT EFDFDTLRTR TRELAFLNRG LTISIEDKRE EHKVRKDFHY EGGIRSYVEH
     LNKAKDVIHE PPIYLEGERD DIMVEISMQY NTGFSSNIIS FANNIHTYEG GTHESGFKTA
     LTRVINDYAR RNKLFKDSDD NLSGEDVREG LTAIISIKHP DPQFEGQTKT KLGNSEARSI
     TDKLFSEALN KFMMENPDVA KKIVEKGVVA SRARLAAKRA REVARKSSGL EISSLPGKLA
     DCSSRNPEIS ELYIVEGDSA GGSAKQGRDR LFQAILPIRG KILNVEKARL DRILANEEIR
     TIFTAMGTGF GGDFDVSKSR YHKLIIMTDA DVDGAHIRTL LLTLFYRYMR PLLDAGYIYI
     AQPPLYQIKH GKQIEYVYSD GQLEDYLASL DGDTKYSIQR YKGLGEMNPE QLWDTTMNPE
     HRTLLQVNIK DAIDADETFE MLMGDRVEPR RKFIEDNAQY VKNLDV
//

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