ID   A0A075U492_9LACT        Unreviewed;       846 AA.
AC   A0A075U492;
DT   29-OCT-2014, integrated into UniProtKB/TrEMBL.
DT   29-OCT-2014, sequence version 1.
DT   27-SEP-2017, entry version 23.
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   ORFNames=WS74_0007 {ECO:0000313|EMBL:AIM62259.1};
OS   Weissella ceti.
OC   Bacteria; Firmicutes; Bacilli; Lactobacillales; Leuconostocaceae;
OC   Weissella.
OX   NCBI_TaxID=759620 {ECO:0000313|EMBL:AIM62259.1, ECO:0000313|Proteomes:UP000029079};
RN   [1] {ECO:0000313|Proteomes:UP000029079}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=WS74 {ECO:0000313|Proteomes:UP000029079};
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: A type II topoisomerase that negatively supercoils
CC       closed circular double-stranded (ds) DNA in an ATP-dependent
CC       manner to modulate DNA topology and maintain chromosomes in an
CC       underwound state. Negative supercoiling favors strand separation,
CC       and DNA replication, transcription, recombination and repair, all
CC       of which involve strand separation. Also able to catalyze the
CC       interconversion of other topological isomers of dsDNA rings,
CC       including catenanes and knotted rings. Type II topoisomerases
CC       break and join 2 DNA strands simultaneously in an ATP-dependent
CC       manner. {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:SAAS00846455}.
CC   -!- SUBUNIT: Heterotetramer, composed of two GyrA and two GyrB chains.
CC       In the heterotetramer, GyrA contains the active site tyrosine that
CC       forms a transient covalent intermediate with DNA, while GyrB binds
CC       cofactors and catalyzes ATP hydrolysis. {ECO:0000256|HAMAP-
CC       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
CC       topoisomerases; in organisms with a single type II topoisomerase
CC       this enzyme also has to decatenate newly replicated chromosomes.
CC       {ECO:0000256|HAMAP-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:SAAS00846457}.
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DR   EMBL; CP009223; AIM62259.1; -; Genomic_DNA.
DR   RefSeq; WP_009765218.1; NZ_CP009224.1.
DR   EnsemblBacteria; AIM62259; AIM62259; WS74_0007.
DR   KEGG; wce:WS08_0008; -.
DR   KEGG; wci:WS105_0007; -.
DR   KEGG; wct:WS74_0007; -.
DR   PATRIC; fig|759620.7.peg.7; -.
DR   KO; K02469; -.
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-UniRule.
DR   GO; GO:0003677; F:DNA binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0003918; F:DNA topoisomerase type II (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   Gene3D; 1.10.268.10; -; 1.
DR   Gene3D; 3.30.1360.40; -; 1.
DR   Gene3D; 3.90.199.10; -; 1.
DR   HAMAP; MF_01897; GyrA; 1.
DR   InterPro; IPR024946; Arg_repress_C-like.
DR   InterPro; IPR005743; GyrA.
DR   InterPro; IPR006691; GyrA/parC_rep.
DR   InterPro; IPR035516; Gyrase/topoIV_suA_C.
DR   InterPro; IPR013760; Topo_IIA-like_dom.
DR   InterPro; IPR002205; Topo_IIA_A/C.
DR   InterPro; IPR013758; Topo_IIA_A/C_ab.
DR   InterPro; IPR013757; Topo_IIA_A_a.
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;
KW   ATP-binding {ECO:0000256|HAMAP-Rule:MF_01897,
KW   ECO:0000256|SAAS:SAAS00846465};
KW   Complete proteome {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:SAAS00846460};
KW   Isomerase {ECO:0000256|HAMAP-Rule:MF_01897,
KW   ECO:0000256|SAAS:SAAS00846445};
KW   Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_01897,
KW   ECO:0000256|SAAS:SAAS00846452};
KW   Reference proteome {ECO:0000313|Proteomes:UP000029079};
KW   Topoisomerase {ECO:0000256|HAMAP-Rule:MF_01897,
KW   ECO:0000256|SAAS:SAAS00846490}.
FT   DOMAIN       14    467       TOP4c. {ECO:0000259|SMART:SM00434}.
FT   MOTIF       529    535       GyrA-box. {ECO:0000256|HAMAP-Rule:
FT                                MF_01897}.
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
//