ID A8LVH4_SALAI Unreviewed; 648 AA.
AC A8LVH4;
DT 04-DEC-2007, integrated into UniProtKB/TrEMBL.
DT 04-DEC-2007, sequence version 1.
DT 29-MAY-2013, entry version 46.
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.
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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; IFETTEF; -.
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: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 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
//
