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Database: UniProt/TrEMBL
Entry: A8LVH4_SALAI
LinkDB: A8LVH4_SALAI
Original site: A8LVH4_SALAI 
ID   A8LVH4_SALAI            Unreviewed;       648 AA.
AC   A8LVH4;
DT   04-DEC-2007, integrated into UniProtKB/TrEMBL.
DT   04-DEC-2007, sequence version 1.
DT   19-FEB-2014, entry version 52.
DE   RecName: Full=DNA gyrase subunit B;
DE            EC=5.99.1.3;
GN   Name=gyrB; OrderedLocusNames=Sare_0007;
OS   Salinispora arenicola (strain CNS-205).
OC   Bacteria; Actinobacteria; Actinobacteridae; Actinomycetales;
OC   Micromonosporineae; Micromonosporaceae; Salinispora.
OX   NCBI_TaxID=391037;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CNS-205;
RG   US DOE Joint Genome Institute;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Glavina del Rio T.,
RA   Dalin E., Tice H., Pitluck S., Foster B., Schmutz J., Larimer F.,
RA   Land M., Hauser L., Kyrpides N., Ivanova N., Jensen P.R., Moore B.S.,
RA   Penn K., Jenkins C., Udwary D., Xiang L., Gontang E., Richardson P.;
RT   "Complete sequence of Salinispora arenicola CNS-205.";
RL   Submitted (OCT-2007) 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; CP000850; ABV95943.1; -; Genomic_DNA.
DR   RefSeq; YP_001534934.1; NC_009953.1.
DR   ProteinModelPortal; A8LVH4; -.
DR   STRING; 391037.Sare_0007; -.
DR   EnsemblBacteria; ABV95943; ABV95943; Sare_0007.
DR   GeneID; 5707580; -.
DR   KEGG; saq:Sare_0007; -.
DR   PATRIC; 23428419; VBISalAre38676_0007.
DR   eggNOG; COG0187; -.
DR   HOGENOM; HOG000075154; -.
DR   KO; K02470; -.
DR   OMA; NINTREG; -.
DR   OrthoDB; EOG6P334W; -.
DR   ProtClustDB; PRK05644; -.
DR   BioCyc; SARE391037:GH66-7-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      425    539       Toprim (By similarity).
FT   METAL       431    431       Magnesium 1; catalytic (By similarity).
FT   METAL       504    504       Magnesium 1; catalytic (By similarity).
FT   METAL       504    504       Magnesium 2 (By similarity).
FT   METAL       506    506       Magnesium 2 (By similarity).
FT   SITE        456    456       Interaction with DNA (By similarity).
FT   SITE        459    459       Interaction with DNA (By similarity).
SQ   SEQUENCE   648 AA;  72001 MW;  8775535031C910BD CRC64;
     MAAQDKQEYG AESITVLEGL EAVRKRPGMY IGSTGERGLH HLVWEVVDNA VDEALAGYCD
     TIDVVLLADG GVRVTDNGRG FPVDPHPKLK KPGVEVALTV LHAGGKFDGK AYAVSGGLHG
     VGVSVVNALS TRMAVEIQKD GYFWRQSYTD SKPSPLEKGE PTDATGSAVS FWPDPAVFET
     VDFDFQTIYR RLQEMAFLNR GLTIHFLDER VAADEDGKMR EVTFCYKGGI ADFVRHLNAS
     KTPIHKSVVE FGTEEDGMSV EIAMQWNESY GESVYTFANN INTHEGGTHE EGFRAALTSV
     INRYGADKRL LKSDEKLSGE DIREGLAAII SVKLTNPQFE GQTKTKLGNT PVKSFVQRVC
     NEWLVDWLDR NPAEAKVIIT KASQAARARV AAQQARKLAR RKSLLESGSM PGKLADCQST
     DPRECEVFIV EGDSAGGSAK QGRDPRTQAI LPIRGKILNV EKARIDRVLK NNEVQALITA
     LGTGIHDDFD IEKLRYHKIV LMADADVDGQ HIQTLLLTLL FRFMRPLVEL GHVYLAAPPL
     YKIKWNRKGD DAQYAYSDRE RDGLIALRQQ KKPNAKPDDI QRFKGLGEMN YPELWETTMN
     PATRTLRQVT LDDAATADEL FSVLMGEDVE ARRSFIQRNA KDVRFLDI
//
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