(data stored in SCRATCH zone)

SWISSPROT: A0A0F6BHG1_GEOS0

ID   A0A0F6BHG1_GEOS0        Unreviewed;       824 AA.
AC   A0A0F6BHG1;
DT   24-JUN-2015, integrated into UniProtKB/TrEMBL.
DT   24-JUN-2015, sequence version 1.
DT   11-DEC-2019, entry version 34.
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=GY4MC1_0006 {ECO:0000313|EMBL:ADP72862.1};
OS   Geobacillus sp. (strain Y4.1MC1).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Geobacillus;
OC   unclassified Geobacillus.
OX   NCBI_TaxID=581103 {ECO:0000313|EMBL:ADP72862.1};
RN   [1] {ECO:0000313|EMBL:ADP72862.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Y4.1MC1 {ECO:0000313|EMBL:ADP72862.1};
RG   US DOE Joint Genome Institute;
RA   Lucas S., Copeland A., Lapidus A., Cheng J.-F., Bruce D., Goodwin L.,
RA   Pitluck S., Chertkov O., Zhang X., Detter J.C., Han C., Tapia R., Land M.,
RA   Hauser L., Jeffries C., Kyrpides N., Ivanova N., Ovchinnikova G., Brumm P.,
RA   Mead D., Woyke T.;
RT   "Complete sequence of chromosome of Geobacillus sp. Y4.1MC1.";
RL   Submitted (OCT-2010) 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|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}.
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DR   EMBL; CP002293; ADP72862.1; -; Genomic_DNA.
DR   RefSeq; WP_013399790.1; NC_014650.1.
DR   EnsemblBacteria; ADP72862; ADP72862; GY4MC1_0006.
DR   KEGG; gmc:GY4MC1_0006; -.
DR   KO; K02469; -.
DR   OMA; THHWLLF; -.
DR   OrthoDB; 217468at2; -.
DR   BioCyc; GSP581103:G1GOQ-6-MONOMER; -.
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; A0A0F6BHG1.
DR   SWISS-2DPAGE; A0A0F6BHG1.
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:ADP72862.1};
KW   Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_01897,
KW   ECO:0000256|SAAS:SAAS01062871};
KW   Topoisomerase {ECO:0000256|HAMAP-Rule:MF_01897,
KW   ECO:0000256|SAAS:SAAS00974554}.
FT   DOMAIN          12..465
FT                   /note="TOP4c"
FT                   /evidence="ECO:0000259|SMART:SM00434"
FT   COILED          437..485
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   MOTIF           527..533
FT                   /note="GyrA-box"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01897"
FT   ACT_SITE        123
FT                   /note="O-(5'-phospho-DNA)-tyrosine intermediate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01897"
SQ   SEQUENCE   824 AA;  92782 MW;  10932BCF95379ED5 CRC64;
     MSENQHPRIR EVNISQEMRS SFLDYAMSVI VSRALPDVRD GLKPVHRRIL YAMHDLGMTA
     DKPYKKSARI VGEVIGKYHP HGDAAVYDTM VRMAQDFNYR YMLVDGHGNF GSIDGDAAAA
     MRYTEARMSK IAMEMLRDIN KDTIDYQDNY DGSEKEPVVL PSRFPNLLVN GSSGIAVGMA
     TNIPPHQLGE VIDAILALSK NPDMTVADLM EHIPGPDFPT AGQIIGRSGI RKAYETGRGS
     ITLRAKAEIE QQPNGKEMII VRELPYQVNK AKLIERIAEL VREKKIDGIT DLRDESDRSG
     MRIVIEVRKD ANAKVILNNL YKHTAMQTSF GINMLALVDG QPKVLNLKEC LQHYLDHQKT
     VIRRRTAYEL KKAEARAHIL EGLRIALDYL DEVINLIRSS KTTEIAREGL MQQFSLSERQ
     AQAILDMRLQ RLTGLEREKI EQEYQELIRL IAELKAILAD EEKVLQIIRD ELTEIKERFN
     DERRTEIVAG GAEEFEDEDL IPRENIVITL THKGYIKRLP VSTYKSQKRG GRGVQGMHTN
     EDDFVEHLLI TSTHDTVLFF TNKGKVYRAK GYEIPEFGRT AKGIPLINLL ELDKDEWINT
     IIPIDNEFDD NLYLFFTTKQ GIAKRSPLSS FAHIRNNGLI AIHLREGDEL ISAKLTDGSK
     HIIVGTKNGM LIRFPETDVR AMGRSATGVK AITLEDGDEV VGMEILEDGC DVLVVTKNGY
     GKRTPASEYR IQSRGGKGIK TCNITEKNGP IVAVKTVTGE EDLMLITASG ILIRIAVSDI
     SRMGRNTQGV KLIRLSDDNE HEYVATVAKV PKEEKENEAE EEEH
//

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