(data stored in SCRATCH zone)

SWISSPROT: A0A0F6BHG0_GEOS0

ID   A0A0F6BHG0_GEOS0        Unreviewed;       640 AA.
AC   A0A0F6BHG0;
DT   24-JUN-2015, integrated into UniProtKB/TrEMBL.
DT   24-JUN-2015, sequence version 1.
DT   08-MAY-2019, entry version 27.
DE   RecName: Full=DNA gyrase subunit B {ECO:0000256|HAMAP-Rule:MF_01898};
DE            EC=5.6.2.3 {ECO:0000256|HAMAP-Rule:MF_01898};
GN   Name=gyrB {ECO:0000256|HAMAP-Rule:MF_01898};
GN   OrderedLocusNames=GY4MC1_0005 {ECO:0000313|EMBL:ADP72861.1};
OS   Geobacillus sp. (strain Y4.1MC1).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Geobacillus.
OX   NCBI_TaxID=581103 {ECO:0000313|EMBL:ADP72861.1, ECO:0000313|Proteomes:UP000002034};
RN   [1] {ECO:0000313|EMBL:ADP72861.1, ECO:0000313|Proteomes:UP000002034}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Y4.1MC1 {ECO:0000313|EMBL:ADP72861.1,
RC   ECO:0000313|Proteomes:UP000002034};
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.,
RA   Land M., Hauser L., Jeffries C., Kyrpides N., Ivanova N.,
RA   Ovchinnikova G., Brumm P., 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
CC       closed circular double-stranded (ds) DNA in an ATP-dependent
CC       manner to modulate DNA topology and maintain chromosomes in an
CC       underwound state. Negative supercoiling favors strand separation,
CC       and DNA replication, transcription, recombination and repair, all
CC       of which involve strand separation. Also able to catalyze the
CC       interconversion of other topological isomers of dsDNA rings,
CC       including catenanes and knotted rings. Type II topoisomerases
CC       break and join 2 DNA strands simultaneously in an ATP-dependent
CC       manner. {ECO:0000256|HAMAP-Rule:MF_01898}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP-dependent breakage, passage and rejoining of double-
CC         stranded DNA.; EC=5.6.2.3; Evidence={ECO:0000256|HAMAP-
CC         Rule:MF_01898, ECO:0000256|SAAS:SAAS01180974};
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000256|SAAS:SAAS00924966};
CC   -!- COFACTOR:
CC       Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC         Evidence={ECO:0000256|SAAS:SAAS00888357};
CC   -!- SUBUNIT: Heterotetramer, composed of two GyrA and two GyrB chains.
CC       In the heterotetramer, GyrA contains the active site tyrosine that
CC       forms a transient covalent intermediate with DNA, while GyrB binds
CC       cofactors and catalyzes ATP hydrolysis. {ECO:0000256|HAMAP-
CC       Rule:MF_01898}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_01898}.
CC   -!- MISCELLANEOUS: Few gyrases are as efficient as E.coli at forming
CC       negative supercoils. Not all organisms have 2 type II
CC       topoisomerases; in organisms with a single type II topoisomerase
CC       this enzyme also has to decatenate newly replicated chromosomes.
CC       {ECO:0000256|HAMAP-Rule:MF_01898}.
CC   -!- SIMILARITY: Belongs to the type II topoisomerase family.
CC       {ECO:0000256|HAMAP-Rule:MF_01898}.
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DR   EMBL; CP002293; ADP72861.1; -; Genomic_DNA.
DR   RefSeq; WP_003247343.1; NC_014650.1.
DR   EnsemblBacteria; ADP72861; ADP72861; GY4MC1_0005.
DR   GeneID; 29237384; -.
DR   KEGG; gmc:GY4MC1_0005; -.
DR   KO; K02470; -.
DR   OMA; IYIACPP; -.
DR   OrthoDB; 205481at2; -.
DR   BioCyc; GSP581103:G1GOQ-5-MONOMER; -.
DR   Proteomes; UP000002034; 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-KW.
DR   GO; GO:0003918; F:DNA topoisomerase type II (ATP-hydrolyzing) activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
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; cd00075; HATPase_c; 1.
DR   CDD; cd03366; TOPRIM_TopoIIA_GyrB; 1.
DR   Gene3D; 3.30.230.10; -; 1.
DR   Gene3D; 3.30.565.10; -; 1.
DR   Gene3D; 3.40.50.670; -; 1.
DR   HAMAP; MF_01898; GyrB; 1.
DR   InterPro; IPR002288; DNA_gyrase_B_C.
DR   InterPro; IPR011557; GyrB.
DR   InterPro; IPR003594; HATPase_C.
DR   InterPro; IPR036890; HATPase_C_sf.
DR   InterPro; IPR020568; Ribosomal_S5_D2-typ_fold.
DR   InterPro; IPR014721; Ribosomal_S5_D2-typ_fold_subgr.
DR   InterPro; IPR001241; Topo_IIA.
DR   InterPro; IPR013760; Topo_IIA-like_dom_sf.
DR   InterPro; IPR013759; Topo_IIA_B_C.
DR   InterPro; IPR013506; Topo_IIA_bsu_dom2.
DR   InterPro; IPR018522; TopoIIA_CS.
DR   InterPro; IPR006171; TOPRIM_domain.
DR   InterPro; IPR034160; TOPRIM_GyrB.
DR   Pfam; PF00204; DNA_gyraseB; 1.
DR   Pfam; PF00986; DNA_gyraseB_C; 1.
DR   Pfam; PF02518; HATPase_c; 1.
DR   Pfam; PF01751; Toprim; 1.
DR   SMART; SM00387; HATPase_c; 1.
DR   SMART; SM00433; TOP2c; 1.
DR   SUPFAM; SSF54211; SSF54211; 1.
DR   SUPFAM; SSF55874; SSF55874; 1.
DR   SUPFAM; SSF56719; SSF56719; 1.
DR   TIGRFAMs; TIGR01059; gyrB; 1.
DR   PROSITE; PS00177; TOPOISOMERASE_II; 1.
DR   PROSITE; PS50880; TOPRIM; 1.
PE   3: Inferred from homology;
DR   PRODOM; A0A0F6BHG0.
DR   SWISS-2DPAGE; A0A0F6BHG0.
KW   ATP-binding {ECO:0000256|HAMAP-Rule:MF_01898,
KW   ECO:0000256|SAAS:SAAS00924926};
KW   Complete proteome {ECO:0000313|Proteomes:UP000002034};
KW   Cytoplasm {ECO:0000256|HAMAP-Rule:MF_01898};
KW   DNA-binding {ECO:0000256|SAAS:SAAS00888349};
KW   Isomerase {ECO:0000256|HAMAP-Rule:MF_01898,
KW   ECO:0000256|SAAS:SAAS00924998, ECO:0000313|EMBL:ADP72861.1};
KW   Magnesium {ECO:0000256|SAAS:SAAS00906748};
KW   Metal-binding {ECO:0000256|SAAS:SAAS00906804};
KW   Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_01898,
KW   ECO:0000256|SAAS:SAAS00924952};
KW   Topoisomerase {ECO:0000256|HAMAP-Rule:MF_01898,
KW   ECO:0000256|SAAS:SAAS00924964}.
FT   DOMAIN      424    538       Toprim. {ECO:0000259|PROSITE:PS50880}.
SQ   SEQUENCE   640 AA;  72364 MW;  D69A19CBF69A126C CRC64;
     MTMEQKVEHT YDASQIQVLE GLEAVRKRPG MYIGSTGPKG LHHLVWEIVD NSIDEALAGY
     CTEINVTIEK DGSITVTDNG RGIPVDIQEK MGRPAVEVIM TVLHAGGKFG GGGYKVSGGL
     HGVGASVVNA LSEELEVYVH RDGKIHYQKY QRGVPCTDLQ VVGETDRTGT TVHFKPDPEI
     FTETTEFDYE TLATRLRELA FLNRGLKITL EDKRVENRKN EYCYEGGIQS YVKHLNRTRE
     VLHEEPIYII GERDGIYVEI AFQYNDSYSS NIYSFVNNIH THEGGTHESG FKMALTRIIN
     DYARKQQIFK DNDPNLTGED VREGLTAIVS IKHPAPQFEG QTKTKLGNSD ARTVTDAVFS
     EQFETFLLEN PTIARKIVEK GMMAARARLA AKKARELTRR KSALEISNLP GKLADCSSKD
     PSISELYVVE GDSAGGSAKQ GRDRHFQAIL PLRGKIINVE KARLDKILSN NEVRAIITAL
     GTGIGEDFDI TKARYHKIII MTDADVDGAH IRTLLLTFFY RYMREFIERG YVYIAQPPLY
     KIEQDKQVRY AYNDRQLEKI LAELPENPKP TIQRYKGLGE MNPEQLWETT MNPETRTLLQ
     VSLQDAIEAD ETFEILMGDK VEPRRQFIEE NARYVKNLDI
//

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