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Database: UniProt/TrEMBL
Entry: E0TXL5_BACPZ
LinkDB: E0TXL5_BACPZ
Original site: E0TXL5_BACPZ 
ID   E0TXL5_BACPZ            Unreviewed;       638 AA.
AC   E0TXL5;
DT   02-NOV-2010, integrated into UniProtKB/TrEMBL.
DT   02-NOV-2010, sequence version 1.
DT   19-FEB-2014, entry version 28.
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.
CC   -!- SIMILARITY: Contains 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; NINTREG; -.
DR   BioCyc; BSUB655816:GCOR-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-HAMAP.
DR   GO; GO:0003677; F:DNA binding; IEA:UniProtKB-HAMAP.
DR   GO; GO:0003918; F:DNA topoisomerase type II (ATP-hydrolyzing) activity; IEA:UniProtKB-HAMAP.
DR   GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP.
DR   GO; GO:0006200; P:ATP catabolic process; IEA:GOC.
DR   GO; GO:0006265; P:DNA topological change; IEA:InterPro.
DR   GO; GO:0006261; P:DNA-dependent DNA replication; IEA:UniProtKB-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; 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;
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
//
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