ID   A0A075U492_9LACO        Unreviewed;       846 AA.
AC   A0A075U492;
DT   29-OCT-2014, integrated into UniProtKB/TrEMBL.
DT   29-OCT-2014, sequence version 1.
DT   27-NOV-2024, entry version 54.
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   ORFNames=WS74_0007 {ECO:0000313|EMBL:AIM62259.1};
OS   Weissella ceti.
OC   Bacteria; Bacillota; Bacilli; Lactobacillales; Lactobacillaceae; Weissella.
OX   NCBI_TaxID=759620 {ECO:0000313|EMBL:AIM62259.1, ECO:0000313|Proteomes:UP000029079};
RN   [1] {ECO:0000313|EMBL:AIM62259.1, ECO:0000313|Proteomes:UP000029079}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=WS74 {ECO:0000313|EMBL:AIM62259.1,
RC   ECO:0000313|Proteomes:UP000029079};
RX   PubMed=25323710;
RA   Figueiredo H.C., Leal C.A., Dorella F.A., Carvalho A.F., Soares S.C.,
RA   Pereira F.L., Azevedo V.A.;
RT   "Complete Genome Sequences of Fish Pathogenic Weissella ceti Strains WS74
RT   and WS105.";
RL   Genome Announc. 2:0-0(2014).
RN   [2] {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., Dorella F.A.,
RA   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 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|ARBA:ARBA00000185,
CC         ECO:0000256|HAMAP-Rule:MF_01897};
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 type II topoisomerase GyrA/ParC subunit
CC       family. {ECO:0000256|ARBA:ARBA00008263, ECO:0000256|HAMAP-
CC       Rule:MF_01897}.
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DR   EMBL; CP009223; AIM62259.1; -; Genomic_DNA.
DR   RefSeq; WP_009765218.1; NZ_CP009224.1.
DR   AlphaFoldDB; A0A075U492; -.
DR   STRING; 759620.WS105_0007; -.
DR   KEGG; wce:WS08_0008; -.
DR   KEGG; wci:WS105_0007; -.
DR   KEGG; wct:WS74_0007; -.
DR   PATRIC; fig|759620.7.peg.7; -.
DR   OrthoDB; 9806486at2; -.
DR   Proteomes; UP000029079; Chromosome.
DR   GO; GO:0005694; C:chromosome; IEA:InterPro.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0009330; C:DNA topoisomerase type II (double strand cut, ATP-hydrolyzing) complex; IEA:TreeGrafter.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0003677; F:DNA binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0034335; F:DNA negative supercoiling activity; IEA:UniProt.
DR   GO; GO:0006265; P:DNA topological change; IEA:UniProtKB-UniRule.
DR   GO; GO:0006261; P:DNA-templated DNA replication; IEA:UniProtKB-UniRule.
DR   CDD; cd00187; TOP4c; 1.
DR   FunFam; 1.10.268.10:FF:000001; DNA gyrase subunit A; 1.
DR   FunFam; 2.120.10.90:FF:000004; DNA gyrase subunit A; 1.
DR   FunFam; 3.30.1360.40:FF:000002; DNA gyrase subunit A; 1.
DR   FunFam; 3.90.199.10:FF:000001; DNA gyrase subunit A; 1.
DR   Gene3D; 3.30.1360.40; -; 1.
DR   Gene3D; 2.120.10.90; DNA gyrase/topoisomerase IV, subunit A, C-terminal; 1.
DR   Gene3D; 3.90.199.10; Topoisomerase II, domain 5; 1.
DR   Gene3D; 1.10.268.10; Topoisomerase, domain 3; 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; IPR013758; Topo_IIA_A/C_ab.
DR   InterPro; IPR013757; Topo_IIA_A_a_sf.
DR   InterPro; IPR002205; Topo_IIA_dom_A.
DR   InterPro; IPR050220; Type_II_DNA_Topoisomerases.
DR   NCBIfam; TIGR01063; gyrA; 1.
DR   PANTHER; PTHR43493:SF5; DNA GYRASE SUBUNIT A, CHLOROPLASTIC_MITOCHONDRIAL; 1.
DR   PANTHER; PTHR43493; DNA GYRASE/TOPOISOMERASE SUBUNIT A; 1.
DR   Pfam; PF03989; DNA_gyraseA_C; 6.
DR   Pfam; PF00521; DNA_topoisoIV; 1.
DR   SMART; SM00434; TOP4c; 1.
DR   SUPFAM; SSF101904; GyrA/ParC C-terminal domain-like; 1.
DR   SUPFAM; SSF56719; Type II DNA topoisomerase; 1.
PE   3: Inferred from homology;
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|HAMAP-
KW   Rule:MF_01897}; Cytoplasm {ECO:0000256|HAMAP-Rule:MF_01897};
KW   DNA-binding {ECO:0000256|ARBA:ARBA00023125, ECO:0000256|HAMAP-
KW   Rule:MF_01897};
KW   Isomerase {ECO:0000256|ARBA:ARBA00023235, ECO:0000256|HAMAP-Rule:MF_01897};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|HAMAP-
KW   Rule:MF_01897}; Reference proteome {ECO:0000313|Proteomes:UP000029079};
KW   Topoisomerase {ECO:0000256|ARBA:ARBA00023029, ECO:0000256|HAMAP-
KW   Rule:MF_01897}.
FT   DOMAIN          14..467
FT                   /note="DNA topoisomerase type IIA"
FT                   /evidence="ECO:0000259|SMART:SM00434"
FT   MOTIF           529..535
FT                   /note="GyrA-box"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01897"
FT   ACT_SITE        125
FT                   /note="O-(5'-phospho-DNA)-tyrosine intermediate"
FT                   /evidence="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
//