(data stored in ACNUC10043 zone)

SWISSPROT: D1YWG1_METPS

ID   D1YWG1_METPS            Unreviewed;       812 AA.
AC   D1YWG1;
DT   09-FEB-2010, integrated into UniProtKB/TrEMBL.
DT   09-FEB-2010, sequence version 1.
DT   11-DEC-2019, entry version 64.
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   ECO:0000313|EMBL:BAI60783.1};
GN   OrderedLocusNames=MCP_0711 {ECO:0000313|EMBL:BAI60783.1};
OS   Methanocella paludicola (strain DSM 17711 / JCM 13418 / NBRC 101707 /
OS   SANAE).
OC   Archaea; Euryarchaeota; Stenosarchaea group; Methanomicrobia;
OC   Methanocellales; Methanocellaceae; Methanocella.
OX   NCBI_TaxID=304371 {ECO:0000313|EMBL:BAI60783.1, ECO:0000313|Proteomes:UP000001882};
RN   [1] {ECO:0000313|Proteomes:UP000001882}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 17711 / JCM 13418 / NBRC 101707 / SANAE
RC   {ECO:0000313|Proteomes:UP000001882};
RX   PubMed=21829548; DOI=10.1371/journal.pone.0022898;
RA   Sakai S., Takaki Y., Shimamura S., Sekine M., Tajima T., Kosugi H.,
RA   Ichikawa N., Tasumi E., Hiraki A.T., Shimizu A., Kato Y., Nishiko R.,
RA   Mori K., Fujita N., Imachi H., Takai K.;
RT   "Genome sequence of a mesophilic hydrogenotrophic methanogen Methanocella
RT   paludicola, the first cultivated representative of the order
RT   Methanocellales.";
RL   PLoS ONE 6:E22898-E22898(2011).
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|HAMAP-
CC         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 topoisomerase GyrA/ParC subunit family.
CC       {ECO:0000256|HAMAP-Rule:MF_01897}.
CC   -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC       feature annotation. {ECO:0000256|HAMAP-Rule:MF_01897}.
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DR   EMBL; AP011532; BAI60783.1; -; Genomic_DNA.
DR   STRING; 304371.MCP_0711; -.
DR   EnsemblBacteria; BAI60783; BAI60783; MCP_0711.
DR   KEGG; mpd:MCP_0711; -.
DR   PATRIC; fig|304371.9.peg.736; -.
DR   eggNOG; arCOG04367; Archaea.
DR   eggNOG; COG0188; LUCA.
DR   HOGENOM; HOG000076278; -.
DR   KO; K02469; -.
DR   OMA; THHWLLF; -.
DR   Proteomes; UP000001882; 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 (double strand cut, 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   CDD; cd00187; TOP4c; 1.
DR   Gene3D; 1.10.268.10; -; 1.
DR   Gene3D; 2.120.10.90; -; 1.
DR   Gene3D; 3.90.199.10; -; 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; IPR002205; Topo_IIA_A/C.
DR   InterPro; IPR013758; Topo_IIA_A/C_ab.
DR   InterPro; IPR013757; Topo_IIA_A_a_sf.
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;
DR   PRODOM; D1YWG1.
DR   SWISS-2DPAGE; D1YWG1.
KW   ATP-binding {ECO:0000256|HAMAP-Rule:MF_01897};
KW   Coiled coil {ECO:0000256|SAM:Coils};
KW   Cytoplasm {ECO:0000256|HAMAP-Rule:MF_01897};
KW   DNA-binding {ECO:0000256|HAMAP-Rule:MF_01897};
KW   Isomerase {ECO:0000256|HAMAP-Rule:MF_01897};
KW   Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_01897};
KW   Reference proteome {ECO:0000313|Proteomes:UP000001882};
KW   Topoisomerase {ECO:0000256|HAMAP-Rule:MF_01897}.
FT   DOMAIN          10..462
FT                   /note="TOP4c"
FT                   /evidence="ECO:0000259|SMART:SM00434"
FT   COILED          434..454
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   ACT_SITE        121
FT                   /note="O-(5'-phospho-DNA)-tyrosine intermediate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01897"
SQ   SEQUENCE   812 AA;  90467 MW;  A349EFBB9080B41F CRC64;
     MATQETVLPV KIEEEMRKSY IDYAMSVIVG RALPDVRDGL KPVHRRVLYG MYELGNTYDK
     PYKKSARVVG DVMGKYHPHG DMAIYDTIVR MVQDFSLRYP LIDGQGNFGS VDGDSAAAMR
     YTEVRMAKIA DEMLDDLDKE TVNFVPNFDE SLKEPSVLPA KLPNLLINGS SGIAVGMATN
     IPPHNISEVI DGTVALINDP AIEPLELLKL ITGPDFPTGA YIYGREGIKD AYLTGRGSIK
     IRAKAEITEE GGRNVILVTE IPYMVNKAKL IENIADLVRD KKLEGISDLR DESDRDGMRI
     VIELKKGANA NVLLNQLYRH TQMETTFGVN NLALVDNQPR TLSLKETLEY YLKHRQEVVT
     RRSQFELKKA QAREHILAGL LVALDNIDDF VNILRRSASA DDAKAVFMSK YGLSEEQSKA
     ILDMRLRGLT GLERRKIEDE RAELIKLIAH LKEVLASPQM VLDIIKNELL ELRAKYGDGR
     RTIIKESDGE IVDEDLIPVE NVVVTISNTG YIKRQPVDTY RTQRRGGMGI MGMETKEEDF
     VVDVFTASTH DHLLFFTNKG RVYVLKVYEI PEASRQSRGK AIVNLLTLMP NESVNAMIPI
     KEFDEKHYLI MCTREGTIKK TALSSFQNIR RTGIIAIGLD EGDELISVKL TNGGQEVLIA
     TRNGKANRFS ESEVRPMGRQ AGGVIGIRLT EKDKVIGMEV VSESASILTV CENGFGKRTA
     ISEYTPHHRG GQGMINIKTT LRNGGVVAIA SVTDDDQLLV VTRDGIMMRI NVKDISEISR
     NTQGVKIITL KSENDAVVGV AKLVSEKKEE EI
//

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