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Database: UniProt
Entry: A0A0G0XTJ1_9BACT
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ID   A0A0G0XTJ1_9BACT        Unreviewed;       822 AA.
AC   A0A0G0XTJ1;
DT   22-JUL-2015, integrated into UniProtKB/TrEMBL.
DT   22-JUL-2015, sequence version 1.
DT   27-MAR-2024, entry version 38.
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=UU88_C0003G0045 {ECO:0000313|EMBL:KKS27717.1};
OS   Parcubacteria group bacterium GW2011_GWC1_42_11.
OC   Bacteria.
OX   NCBI_TaxID=1618905 {ECO:0000313|EMBL:KKS27717.1, ECO:0000313|Proteomes:UP000034518};
RN   [1] {ECO:0000313|EMBL:KKS27717.1, ECO:0000313|Proteomes:UP000034518}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Brown C.T., Hug L.A., Thomas B.C., Sharon I., Castelle C.J., Singh A.,
RA   Wilkins M.J., Williams K.H., Banfield J.F.;
RT   "rRNA introns, odd ribosomes, and small enigmatic genomes across a large
RT   radiation of phyla.";
RL   Nature 0:0-0(2015).
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}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:KKS27717.1}.
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DR   EMBL; LCCI01000003; KKS27717.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0G0XTJ1; -.
DR   PATRIC; fig|1618905.3.peg.245; -.
DR   Proteomes; UP000034518; Unassembled WGS sequence.
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: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   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   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};
KW   Topoisomerase {ECO:0000256|ARBA:ARBA00023029, ECO:0000256|HAMAP-
KW   Rule:MF_01897}.
FT   DOMAIN          24..475
FT                   /note="DNA topoisomerase type IIA"
FT                   /evidence="ECO:0000259|SMART:SM00434"
FT   MOTIF           537..543
FT                   /note="GyrA-box"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01897"
FT   ACT_SITE        135
FT                   /note="O-(5'-phospho-DNA)-tyrosine intermediate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01897"
SQ   SEQUENCE   822 AA;  90873 MW;  2413CB68F747F30C CRC64;
     MARKKEEKDE SAVVPPERVN VVPQDISSEM RASFIDYAMS VITDRALPDV RDGLKPVHRR
     ILFSMYEKGL TASAKFRKSA TVVGDVLGSY HPHGDSSVYE AMVKMAQEFS FRYPLVIGQG
     NFGSIDGDAA AAYRYTEAKM SRISGELLND IDRETVDFKP NYDGTKKEPT VLPSSLPNLL
     LNGTLGIAVG MATNFPPHNL GELVDATNHL IDEPDATSDD LVKFVKGPDF PIGGIVFGEK
     DIKHAYSSGR GGVVCRGEAE IIEDKNLNQI IITSLPFRVN KANLIVKIAD LVREKKLEGI
     RGLRDESTKD IRVVIDLKNG AYPQVVLNYL YKHTELESTF HYNMVALVDG VPQTLSLKGV
     LSNFIGHRQV VVKRRTEYDL RKAEEREHIL LGLKKALDHI DRVITIIRAS KDTATAHANL
     IKEFKFSDLQ ATAILEMKLQ KLAGLERKNV ELELKEKQDF IKECKDLLAS PKKILAVVKK
     ELGEMKEKYG DARRTKVVKH AAGSISLEDM IPDEESMLVY TKGGYIKRTN PGEYRQQNRG
     GVGVVDLDTK EEDFITLFMS ATTHSDMLFF SDKGKAYQIK MYDIPEGKRA TRGKSIMNFI
     ALSGEEKVTS ILSMPKSLKD SNLSLFMVTK HGTIKKCGAE SFKDVRRNGI ISIKLDAGDE
     LIAALFTEKG DDIILTTAKG QAIRFKESDA REMGRAAAGV RGMKLGKGDF IIGADVIQKG
     AEKPELLVMS ENGYGKKTAI KEYKVQKRGG SGIKTAKVTA KIGQLMVAKV VTPAFSELVA
     ISKNSQVIRI TMKDVPTLGR DTQGVRIMKL REGDSIASLS CL
//
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