ID GYRB_STAAM Reviewed; 644 AA.
AC P66936; Q99XG6;
DT 11-OCT-2004, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 2.
DT 01-MAY-2013, entry version 61.
DE RecName: Full=DNA gyrase subunit B;
DE EC=5.99.1.3;
GN Name=gyrB; OrderedLocusNames=SAV0005;
OS Staphylococcus aureus (strain Mu50 / ATCC 700699).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcus.
OX NCBI_TaxID=158878;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Mu50 / ATCC 700699;
RX PubMed=11418146; DOI=10.1016/S0140-6736(00)04403-2;
RA Kuroda M., Ohta T., Uchiyama I., Baba T., Yuzawa H., Kobayashi I.,
RA Cui L., Oguchi A., Aoki K., Nagai Y., Lian J.-Q., Ito T., Kanamori M.,
RA Matsumaru H., Maruyama A., Murakami H., Hosoyama A., Mizutani-Ui Y.,
RA Takahashi N.K., Sawano T., Inoue R., Kaito C., Sekimizu K.,
RA Hirakawa H., Kuhara S., Goto S., Yabuzaki J., Kanehisa M.,
RA Yamashita A., Oshima K., Furuya K., Yoshino C., Shiba T., Hattori M.,
RA Ogasawara N., Hayashi H., Hiramatsu K.;
RT "Whole genome sequencing of meticillin-resistant Staphylococcus
RT aureus.";
RL Lancet 357:1225-1240(2001).
CC -!- FUNCTION: DNA gyrase negatively supercoils closed circular double-
CC stranded DNA in an ATP-dependent manner and also catalyzes the
CC interconversion of other topological isomers of double-stranded
CC DNA rings, including catenanes and knotted rings (By similarity).
CC -!- CATALYTIC ACTIVITY: ATP-dependent breakage, passage and rejoining
CC of double-stranded DNA.
CC -!- COFACTOR: Magnesium. Binds two Mg(2+) per subunit. The magnesium
CC ions form salt bridges with both the protein and the DNA. Can also
CC accept other divalent metal cations, such as Mn(2+) and Ca(2+) (By
CC similarity).
CC -!- SUBUNIT: Heterotetramer, composed of two GyrA and two GyrB chains.
CC Within the heterotetramer, GyrA contains the active site tyrosine
CC that forms a covalent intermediate with the DNA, while GyrB
CC contributes the cofactor binding sites and catalyzes ATP
CC hydrolysis (By similarity).
CC -!- SUBCELLULAR LOCATION: Cytoplasm (Potential).
CC -!- SIMILARITY: Belongs to the type II topoisomerase family.
CC -!- SIMILARITY: Contains 1 Toprim domain.
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DR EMBL; BA000017; BAB56167.1; -; Genomic_DNA.
DR RefSeq; NP_370529.1; NC_002758.2.
DR ProteinModelPortal; P66936; -.
DR SMR; P66936; 14-387, 416-644.
DR STRING; 158878.SAV0005; -.
DR World-2DPAGE; 0002:P66936; -.
DR PRIDE; P66936; -.
DR EnsemblBacteria; BAB56167; BAB56167; SAV0005.
DR GeneID; 1119965; -.
DR KEGG; sav:SAV0005; -.
DR PATRIC; 19560611; VBIStaAur52173_0005.
DR eggNOG; COG0187; -.
DR HOGENOM; HOG000075154; -.
DR KO; K02470; -.
DR OMA; IFETTEF; -.
DR ProtClustDB; PRK05644; -.
DR BioCyc; SAUR158878:GJJ5-5-MONOMER; -.
DR ChEMBL; CHEMBL2589; -.
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:HAMAP.
DR GO; GO:0003918; F:DNA topoisomerase type II (ATP-hydrolyzing) activity; IEA:HAMAP.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0006265; P:DNA topological change; IEA:InterPro.
DR GO; GO:0006261; P:DNA-dependent DNA replication; IEA:HAMAP.
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_ATP-bd.
DR InterPro; IPR020568; Ribosomal_S5_D2-typ_fold.
DR InterPro; IPR014721; Ribosomal_S5_D2-typ_fold_subgr.
DR InterPro; IPR001241; Topo_IIA.
DR InterPro; IPR013506; Topo_IIA_bsu_dom2.
DR InterPro; IPR013759; Topo_IIA_cen_dom.
DR InterPro; IPR013760; Topo_IIA_like_dom.
DR InterPro; IPR018522; TopoIIA_CS.
DR InterPro; IPR006171; Toprim_domain.
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 PRINTS; PR00418; TPI2FAMILY.
DR SMART; SM00387; HATPase_c; 1.
DR SMART; SM00433; TOP2c; 1.
DR SUPFAM; SSF55874; ATP_bd_ATPase; 1.
DR SUPFAM; SSF54211; Ribosomal_S5_D2-typ_fold; 1.
DR SUPFAM; SSF56719; Topo_IIA_cen; 1.
DR TIGRFAMs; TIGR01059; gyrB; 1.
DR PROSITE; PS00177; TOPOISOMERASE_II; 1.
DR PROSITE; PS50880; TOPRIM; 1.
PE 1: Evidence at protein level;
KW ATP-binding; Complete proteome; Cytoplasm; DNA-binding; Isomerase;
KW Magnesium; Metal-binding; Nucleotide-binding; Topoisomerase.
FT INIT_MET 1 1 Removed (By similarity).
FT CHAIN 2 644 DNA gyrase subunit B.
FT /FTId=PRO_0000145338.
FT DOMAIN 429 543 Toprim.
FT METAL 435 435 Magnesium 1; catalytic (By similarity).
FT METAL 508 508 Magnesium 1; catalytic (By similarity).
FT METAL 508 508 Magnesium 2 (By similarity).
FT METAL 510 510 Magnesium 2 (By similarity).
FT SITE 460 460 Interaction with DNA (By similarity).
FT SITE 463 463 Interaction with DNA (By similarity).
SQ SEQUENCE 644 AA; 72540 MW; D4E02886B97DFBC5 CRC64;
MVTALSDVNN TDNYGAGQIQ VLEGLEAVRK RPGMYIGSTS ERGLHHLVWE IVDNSIDEAL
AGYANKIEVV IEKDNWIKVT DNGRGIPVDI QEKMGRPAVE VILTVLHAGG KFGGGGYKVS
GGLHGVGSSV VNALSQDLEV YVHRNETIYH QAYKKGVPQF DLKEVGTTDK TGTVIRFKAD
GEIFTETTVY NYETLQQRIR ELAFLNKGIQ ITLRDERDEE NVREDSYHYE GGIKSYVELL
NENKEPIHDE PIYIHQSKDD IEVEIAIQYN SGYATNLLTY ANNIHTYEGG THEDGFKRAL
TRVLNSYGLS SKIMKEEKDR LSGEDTREGM TAIISIKHGD PQFEGQTKTK LGNSEVRQVV
DKLFSEHFER FLYENPQVAR TVVEKGIMAA RARVAAKKAR EVTRRKSALD VASLPGKLAD
CSSKSPEECE IFLVEGDSAG GSTKSGRDSR TQAILPLRGK ILNVEKARLD RILNNNEIRQ
MITAFGTGIG GDFDLAKARY HKIVIMTDAD VDGAHIRTLL LTFFYRFMRP LIEAGYVYIA
QPPLYKLTQG KQKYYVYNDR ELDKLKSELN PTPKWSIARY KGLGEMNADQ LWETTMNPEH
RALLQVKLED AIEADQTFEM LMGDVVENRR QFIEDNAVYA NLDF
//
