(data stored in SCRATCH3701 zone)

SWISSPROT: Q0B0Y9_SYNWW

ID   Q0B0Y9_SYNWW            Unreviewed;       812 AA.
AC   Q0B0Y9;
DT   17-OCT-2006, integrated into UniProtKB/TrEMBL.
DT   17-OCT-2006, sequence version 1.
DT   11-DEC-2019, entry version 100.
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   OrderedLocusNames=Swol_0006 {ECO:0000313|EMBL:ABI67365.1};
OS   Syntrophomonas wolfei subsp. wolfei (strain DSM 2245B / Goettingen).
OC   Bacteria; Firmicutes; Clostridia; Clostridiales; Syntrophomonadaceae;
OC   Syntrophomonas.
OX   NCBI_TaxID=335541 {ECO:0000313|EMBL:ABI67365.1, ECO:0000313|Proteomes:UP000001968};
RN   [1] {ECO:0000313|Proteomes:UP000001968}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 2245B / Goettingen {ECO:0000313|Proteomes:UP000001968};
RX   PubMed=21966920; DOI=10.1111/j.1462-2920.2010.02237.x;
RA   Sieber J.R., Sims D.R., Han C., Kim E., Lykidis A., Lapidus A.L.,
RA   McDonnald E., Rohlin L., Culley D.E., Gunsalus R., McInerney M.J.;
RT   "The genome of Syntrophomonas wolfei: new insights into syntrophic
RT   metabolism and biohydrogen production.";
RL   Environ. Microbiol. 12:2289-2301(2010).
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-Rule:MF_01897,
CC         ECO:0000256|SAAS:SAAS01218217};
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   -!- SIMILARITY: Belongs to the type II topoisomerase GyrA/ParC subunit
CC       family. {ECO:0000256|SAAS:SAAS01062860}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; CP000448; ABI67365.1; -; Genomic_DNA.
DR   RefSeq; WP_011639476.1; NC_008346.1.
DR   STRING; 335541.Swol_0006; -.
DR   EnsemblBacteria; ABI67365; ABI67365; Swol_0006.
DR   KEGG; swo:Swol_0006; -.
DR   eggNOG; ENOG4105C24; Bacteria.
DR   eggNOG; COG0188; LUCA.
DR   HOGENOM; HOG000076278; -.
DR   KO; K02469; -.
DR   OMA; THHWLLF; -.
DR   OrthoDB; 217468at2; -.
DR   BioCyc; SWOL335541:G1G78-6-MONOMER; -.
DR   Proteomes; UP000001968; 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; Q0B0Y9.
DR   SWISS-2DPAGE; Q0B0Y9.
KW   ATP-binding {ECO:0000256|HAMAP-Rule:MF_01897,
KW   ECO:0000256|SAAS:SAAS01062880}; Coiled coil {ECO:0000256|SAM:Coils};
KW   Cytoplasm {ECO:0000256|HAMAP-Rule:MF_01897};
KW   DNA-binding {ECO:0000256|HAMAP-Rule:MF_01897,
KW   ECO:0000256|SAAS:SAAS01062879};
KW   Isomerase {ECO:0000256|HAMAP-Rule:MF_01897, ECO:0000256|SAAS:SAAS00972514,
KW   ECO:0000313|EMBL:ABI67365.1};
KW   Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_01897,
KW   ECO:0000256|SAAS:SAAS01062871};
KW   Reference proteome {ECO:0000313|Proteomes:UP000001968};
KW   Topoisomerase {ECO:0000256|HAMAP-Rule:MF_01897,
KW   ECO:0000256|SAAS:SAAS00974554}.
FT   DOMAIN          13..465
FT                   /note="TOP4c"
FT                   /evidence="ECO:0000259|SMART:SM00434"
FT   COILED          437..457
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   MOTIF           526..532
FT                   /note="GyrA-box"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01897"
FT   ACT_SITE        124
FT                   /note="O-(5'-phospho-DNA)-tyrosine intermediate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01897"
SQ   SEQUENCE   812 AA;  92430 MW;  85F354629D2FAD6C CRC64;
     MAQDSLFEKV IPIDIEKEVK KSFLEYSMSV IVSRALPDVR DGLKPVHRRI LYALHEQGMT
     HDKPHKKSAN IVGEVMGKYH PHGDAAIYQT MVKLAQEFAM RYPLVDGHGN FGSIDGDAAA
     AMRYTESRMS RIAAELLKDI DKDTVDWRPN YDESREEPQV LPARIPNLLL NGSAGIAVGM
     ATNIPPHNLR EIVKGIKEYI DNPDITIEEL MQSIPGPDFP TGGILEARGI RQAYETGRGT
     IRTRARYEIE EKKGGKFSIV VTEIPYQVNK ARLVEKIAEL VRDKKVEGIV DLRDESDRKG
     IRIVIELRKD VNVNVILNKL FRHTQMEDSF GIIMLSLVNG EPRILNLKEM IQYYVEHRQE
     VINRRTTYEL NLAKNRKHIL EGLKIALDNL DEIINLIRNS RDRENARGEL QSRFNLSEIQ
     ANAILDMRLV QLTGLERSKV ENEYEEVLLR IADYEDILAR PERVLSMIKE DLDDIEKRYG
     DNRRTEISQE ESSYEEEDFI DDHEVVITLS NRGYVKRQPL DTYRSQKRGG KGVSATTIRA
     EDFAHDVLVT SALATLLFFT NQGRVFTTRA FQIPESSRQA KGMPLVNFLE LRPGEKVTTI
     VGAREFNREH HLLMVTKKGI IKKTALKAFQ NVRKSGLIAV NLREDDELVG VIRVKTGSKV
     MIANSRGISI MFDEKQVRSM GRTAAGVKAI NLSKDDYVVG LDRYREGADV LLVTEKGYGK
     RTALSEFKLQ NRGGKGLKAI EITRRNGKLV AFQIVSKEDE LVILTSEGNI IRLEVEDISQ
     QKRYSRGVLL MRLPEEDRIV GVARFKIEKE ED
//

If you have problems or comments...

PBIL Back to PBIL home page