ID E0TXL5_BACPZ Unreviewed; 638 AA.
AC E0TXL5;
DT 02-NOV-2010, integrated into UniProtKB/TrEMBL.
DT 02-NOV-2010, sequence version 1.
DT 01-MAY-2013, entry version 22.
DE RecName: Full=DNA gyrase subunit B;
DE EC=5.99.1.3;
GN Name=gyrB; OrderedLocusNames=BSUW23_00035;
OS Bacillus subtilis subsp. spizizenii (strain ATCC 23059 / NRRL B-14472
OS / W23).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX NCBI_TaxID=655816;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 23059 / NRRL B-14472 / W23;
RA Zeigler D.R.;
RT "Complete genome sequence of Bacillus subtilis subsp. spizizenii str.
RT W23.";
RL Submitted (AUG-2010) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=W23;
RA Zeigler D.R.;
RL Submitted (AUG-2010) to the EMBL/GenBank/DDBJ databases.
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 (By similarity).
CC -!- SIMILARITY: Belongs to the type II topoisomerase family.
CC -!- SIMILARITY: Contains 1 Toprim domain.
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DR EMBL; CP002183; ADM36065.1; -; Genomic_DNA.
DR RefSeq; YP_003864375.1; NC_014479.1.
DR ProteinModelPortal; E0TXL5; -.
DR EnsemblBacteria; ADM36065; ADM36065; BSUW23_00035.
DR GeneID; 9720936; -.
DR KEGG; bss:BSUW23_00035; -.
DR PATRIC; 42185934; VBIBacSub57968_0006.
DR HOGENOM; HOG000075156; -.
DR KO; K02470; -.
DR OMA; MDRILAN; -.
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.
PE 3: Inferred from homology;
KW ATP-binding; Complete proteome; Cytoplasm; DNA-binding; Isomerase;
KW Magnesium; Metal-binding; Nucleotide-binding; Topoisomerase.
FT DOMAIN 422 536 Toprim (By similarity).
FT METAL 428 428 Magnesium 1; catalytic (By similarity).
FT METAL 501 501 Magnesium 1; catalytic (By similarity).
FT METAL 501 501 Magnesium 2 (By similarity).
FT METAL 503 503 Magnesium 2 (By similarity).
FT SITE 453 453 Interaction with DNA (By similarity).
FT SITE 456 456 Interaction with DNA (By similarity).
SQ SEQUENCE 638 AA; 71410 MW; F1C63CC931AB1F2F CRC64;
MEQQQNSYDE NQIQVLEGLE AVRKRPGMYI GSTNSKGLHH LVWEIVDNSI DEALAGYCTD
INIQIEKDNS ITVIDNGRGI PVGIHEKMGR PAVEVIMTVL HAGGKFDGSG YKVSGGLHGV
GASVVNALST ELVVTVHRDG KIHRQTYKRG VPVSDLEIIG ETDHTGTTTH FVPDPEIFTE
TTVYDYDLLA NRVRELAFLT KGVNITIEDK REGQERKNEY HYEGGIKSYV EYLNRSKEVV
HEEPIYIEGE KDGITVEVAL QYNDSYTSNI YSFTNNINTY EGGTHEAGFK TGLTRVINDY
ARKKGLIKEN DPNLSGDDVR EGLTAIISIK HPDPQFEGQT KTKLGNSEAR TITDTLFSAA
LETFMLENPD AAKKIVDKGL MAARARMAAK KARELTRRKS ALEISNLPGK LADCSSKDPS
ISELYIVEGD SAGGSAKQGR DRHFQAILPL RGKILNVEKA RLDKILSNNE VRSMITALGT
GIGEDFNLEK ARYHKVVIMT DADVDGAHIR TLLLTFFYRY MRQIIENGYV YIAQPPLYKV
QQGKRVEYAY NDKELEDLLK TLPQTPKPGL QRYKGLGEMN ATQLWETTMD PSSRTLLQVT
LEDAMDADET FEMLMGDKVE PRRNFIEANA RYVKNLDI
//
