ID A0A075U492_9LACT Unreviewed; 846 AA. AC A0A075U492; DT 29-OCT-2014, integrated into UniProtKB/TrEMBL. DT 29-OCT-2014, sequence version 1. DT 04-MAR-2015, entry version 5. DE RecName: Full=DNA gyrase subunit A {ECO:0000256|HAMAP-Rule:MF_01897}; DE EC=5.99.1.3 {ECO:0000256|HAMAP-Rule:MF_01897}; GN Name=gyrA {ECO:0000256|HAMAP-Rule:MF_01897, GN ECO:0000313|EMBL:AIG64947.1}; GN ORFNames=WS08_0008 {ECO:0000313|EMBL:AIG64947.1}, WS105_0007 GN {ECO:0000313|EMBL:AIM63597.1}, WS74_0007 GN {ECO:0000313|EMBL:AIM62259.1}; OS Weissella ceti. OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Leuconostocaceae; OC Weissella. OX NCBI_TaxID=759620 {ECO:0000313|EMBL:AIG64947.1, ECO:0000313|Proteomes:UP000028491}; RN [1] {ECO:0000313|EMBL:AIG64947.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=WS08 {ECO:0000313|EMBL:AIG64947.1}; RA Figueiredo H.C.P., Leal C.A.G., Pereira F.L., Soares S.C., RA Dorella F.A., Carvalho A.F., Pereira U.P., Azevedo V.A.C.; RT "Complete genome of Weissella ceti strain WS08 isolated from diseased RT rainbow trout in Brazil."; RL Submitted (APR-2014) to the EMBL/GenBank/DDBJ databases. RN [2] {ECO:0000313|EMBL:AIM63597.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=WS105 {ECO:0000313|EMBL:AIM63597.1}; RA Figueiredo H.C.P., Leal C.A.G., Pereira F.L., Soares S.C., RA Dorella F.A., Carvalho A.F., Azevedo V.A.C.; RT "Complete genome of Weissella ceti strain WS105 isolated from diseased RT rainbow trout in Brazil."; RL Submitted (AUG-2014) to the EMBL/GenBank/DDBJ databases. RN [3] {ECO:0000313|EMBL:AIM62259.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=WS74 {ECO:0000313|EMBL:AIM62259.1}; RA Figueiredo H.C.P., Leal C.A.G., Pereira F.L., Soares S.C., RA Dorella F.A., Carvalho A.F., Azevedo V.A.C.; RT "Complete genome of Weissella ceti strain WS74 isolated from diseased RT rainbow trout in Brazil."; RL Submitted (AUG-2014) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: DNA gyrase negatively supercoils closed circular double- CC stranded DNA in an ATP-dependent manner and also catalyzes the CC interconversion of other topological isomers of double-stranded CC DNA rings, including catenanes and knotted rings. CC {ECO:0000256|HAMAP-Rule:MF_01897}. CC -!- CATALYTIC ACTIVITY: ATP-dependent breakage, passage and rejoining CC of double-stranded DNA. {ECO:0000256|HAMAP-Rule:MF_01897, CC ECO:0000256|SAAS:SAAS00075911}. CC -!- SUBUNIT: Heterotetramer, composed of two GyrA and two GyrB chains. CC Within the heterotetramer, GyrA contains the active site tyrosine CC that forms a covalent intermediate with the DNA, while GyrB CC contributes the cofactor binding sites and catalyzes ATP CC hydrolysis. {ECO:0000256|HAMAP-Rule:MF_01897}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_01897}. CC -!- SIMILARITY: Belongs to the topoisomerase GyrA/ParC subunit family. CC {ECO:0000256|HAMAP-Rule:MF_01897}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; CP007588; AIG64947.1; -; Genomic_DNA. DR EMBL; CP009223; AIM62259.1; -; Genomic_DNA. DR EMBL; CP009224; AIM63597.1; -; Genomic_DNA. DR Proteomes; UP000028491; Chromosome. DR Proteomes; UP000029039; Chromosome. DR Proteomes; UP000029079; 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-HAMAP. DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003918; F:DNA topoisomerase type II (ATP-hydrolyzing) activity; IEA:UniProtKB-HAMAP. DR GO; GO:0006265; P:DNA topological change; IEA:InterPro. DR GO; GO:0006261; P:DNA-dependent DNA replication; IEA:UniProtKB-HAMAP. DR Gene3D; 3.30.1360.40; -; 1. DR Gene3D; 3.90.199.10; -; 2. DR HAMAP; MF_01897; GyrA; 1. DR InterPro; IPR024946; Arg_repress_C-like. DR InterPro; IPR005743; GyrA. DR InterPro; IPR006691; GyrA/parC_pinwhl. DR InterPro; IPR002205; Topo_IIA_A/C. DR InterPro; IPR013758; Topo_IIA_A/C_ab. DR InterPro; IPR013760; Topo_IIA_like_dom. DR Pfam; PF03989; DNA_gyraseA_C; 6. DR Pfam; PF00521; DNA_topoisoIV; 1. DR SMART; SM00434; TOP4c; 1. DR SUPFAM; SSF56719; SSF56719; 1. DR TIGRFAMs; TIGR01063; gyrA; 1. PE 3: Inferred from homology; KW ATP-binding {ECO:0000256|HAMAP-Rule:MF_01897, KW ECO:0000256|SAAS:SAAS00049104}; KW Complete proteome {ECO:0000313|Proteomes:UP000028491, KW ECO:0000313|Proteomes:UP000029039}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_01897}; KW DNA-binding {ECO:0000256|HAMAP-Rule:MF_01897, KW ECO:0000256|SAAS:SAAS00076180}; KW Isomerase {ECO:0000256|HAMAP-Rule:MF_01897, KW ECO:0000256|SAAS:SAAS00076195}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_01897, KW ECO:0000256|SAAS:SAAS00049236}; KW Reference proteome {ECO:0000313|Proteomes:UP000029079}; KW Topoisomerase {ECO:0000256|HAMAP-Rule:MF_01897, KW ECO:0000256|SAAS:SAAS00075980}. FT ACT_SITE 125 125 O-(5'-phospho-DNA)-tyrosine intermediate. FT {ECO:0000256|HAMAP-Rule:MF_01897}. SQ SEQUENCE 846 AA; 93795 MW; 9782A42B9FFCBF29 CRC64; MTENEQNISR TVNANIGEQM KSSFLDYAMS VIVARALPDV RDGMKPVHRR IMYGMNELGV MPDKPYKKSA RIVGDVMGKY HPHGDSAIYE SMVRMAQDFS YRYMLVDGHG NFGSIDGDSA AAMRYTEARL SKIATEMLRD INKNTVNFVD NYDGTDREPA VLPARFPNLL VNGANGIAVG MATNIPPHNL GEIISAIHLL MENPDVTTAE LMEAVPGPDF PTGGIALGKS GIRKAYETGK GTVTVRSKVE IETEKSGKER IIVTELPYMV NKARLIERIA ELARDKRIEG ITSINDESDR EGYRIAIDIR RDVSASVVLN NLYKNTLMQT NFSFNMLAVQ DGRPKLLSLK DMLKAYLKHQ QEVIRRRTEF ELKKAEARAH ILEGLRIALD HIDAIIKIIR SSTTAEIAKT QLISDYALSD KQAQAILDMR LVRLTGLERD KIEKEYQELM AEIAEFKDIL SKPERIDQII YTELLEIQEK HGDDRRTELQ IGDVTSIEDE DLIEEEDVIV SLTRGGYIKR MAQSEFRAQN RGGRGVQGMG VNDDDFIDQI AGTSTHDTLL FFTNAGKVYK LKGYEIPEYG RTAKGIPVIN LLGIESGETI QTMISVNDDP ENSDDYLFFT TRDGVVKRTA ISEFGNIRAH GLRAINLREN DELIKVMKTV DSDNILIATQ GGYAVSFKMD TIRAMGRTAA GVRGINLREN DMVIGAEVLV DDAHVLVITQ NGYGKKTAVS EYPIKGRGGK GIKTAQITEK NGPLAGVAVV QGGEDVVLTT NMGVMIRFNV ATVSETGRAT QGVRLIRLDE EATVATFTTV EPEPEEDTTV TDDSMTEQVE ALVDRAMSEE ADTTEA //