ID   A0A075U492_9LACT        Unreviewed;       846 AA.
AC   A0A075U492;
DT   29-OCT-2014, integrated into UniProtKB/TrEMBL.
DT   29-OCT-2014, sequence version 1.
DT   29-APR-2015, entry version 7.
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}, 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: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}.
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DR   EMBL; CP007588; AIG64947.1; -; Genomic_DNA.
DR   EMBL; CP009223; AIM62259.1; -; Genomic_DNA.
DR   EnsemblBacteria; AIG64947; AIG64947; WS08_0008.
DR   EnsemblBacteria; AIM62259; AIM62259; WS74_0007.
DR   EnsemblBacteria; AIM63597; AIM63597; WS105_0007.
DR   Proteomes; UP000028491; 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:UP000029079};
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
//