ID F4AH44_GLAS4 Unreviewed; 806 AA.
AC F4AH44;
DT 28-JUN-2011, integrated into UniProtKB/TrEMBL.
DT 28-JUN-2011, sequence version 1.
DT 01-MAY-2013, entry version 17.
DE RecName: Full=DNA gyrase subunit B;
DE EC=5.99.1.3;
GN Name=gyrB; OrderedLocusNames=Glaag_0004;
OS Glaciecola sp. (strain 4H-3-7+YE-5).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Alteromonadales;
OC Alteromonadaceae; Glaciecola.
OX NCBI_TaxID=983545;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=4H-3-7+YE-5;
RX PubMed=21705587; DOI=10.1128/JB.05468-11;
RG US DOE Joint Genome Institute;
RA Klippel B., Lochner A., Bruce D.C., Walston Davenport K., Detter C.,
RA Goodwin L.A., Han J., Han S., Land M.L., Mikhailova N., Nolan M.,
RA Pennacchio L., Pitluck S., Tapia R., Woyke T., Wiebusch S., Basner A.,
RA Abe F., Horikoshi K., Keller M., Antranikian G.;
RT "Complete genome sequence of the marine cellulose- and xylan-degrading
RT bacterium Glaciecola sp. strain 4H-3-7+YE-5.";
RL J. Bacteriol. 193:4547-4548(2011).
RN [2]
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=4H-3-7+YE-5;
RG US DOE Joint Genome Institute;
RA Lucas S., Copeland A., Lapidus A., Cheng J.-F., Goodwin L.,
RA Pitluck S., Davenport K., Detter J.C., Han C., Tapia R., Land M.,
RA Hauser L., Kyrpides N., Ivanova N., Mikhailova N., Pagani I.,
RA Piela B., Lochner A., Antranikian F.I., Woyke T.;
RT "Complete sequence of chromosome of Glaciecola sp. 4H-3-7+YE-5.";
RL Submitted (FEB-2011) 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; CP002526; AEE20973.1; -; Genomic_DNA.
DR RefSeq; YP_004432241.1; NC_015497.1.
DR EnsemblBacteria; AEE20973; AEE20973; Glaag_0004.
DR GeneID; 10570095; -.
DR KEGG; gag:Glaag_0004; -.
DR PATRIC; 54573303; VBIGlaSp182133_0004.
DR KO; K02470; -.
DR BioCyc; GSP983545:GH3Q-336-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; -; 2.
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 420 535 Toprim (By similarity).
FT METAL 426 426 Magnesium 1; catalytic (By similarity).
FT METAL 500 500 Magnesium 1; catalytic (By similarity).
FT METAL 500 500 Magnesium 2 (By similarity).
FT METAL 502 502 Magnesium 2 (By similarity).
FT SITE 451 451 Interaction with DNA (By similarity).
FT SITE 454 454 Interaction with DNA (By similarity).
SQ SEQUENCE 806 AA; 90321 MW; EBC16E10AD08E638 CRC64;
MAEENKYDSS SIKVLKGLDA VRKRPGMYIG DTDDGTGLHH MVFEVVDNSI DEALAGHCTN
INVKIHTDGS VSVKDDGRGI PTEIHEEEGV SAAEVIMTVL HAGGKFDDNS YKVSGGLHGV
GVSVVNALSR RLQILIRRAG KVHEQEYQHG VPQKPLEVIG ESDTSGTSIR FWPSEETFTG
IEFHYDILAK RLRELSFLNS GVSIILEDER DGKRDHFMYE GGIQAFVEYL NQNKTPVHQQ
VFHFNSERDD GISVEVALQW NDSFQENVFC FTNNIPQRDG GSHLAGFRGA LTRTLNAFME
KEGHNKKNKT SASGDDAREG LTAVVSVKVP DPKFSSQTKD KLVSSEVRPA VETVMGEKLN
EFLLENPSAS KIIINKIIDA ARAREAARKA RDMTRRKGAL DLAGLPGKLA DCQEKDPSLS
ELYIVEGDSA GGSAKQGRNR KNQAILPLKG KILNVEKARF DKMLSSQEVA TLITALGCGI
GRDEYDPEKL RYHRIIIMTD ADVDGSHIRT LLLTFFYRQM PEIIERGYIY IAQPPLYKTK
KGKQEQYLKD DDSLTKYLTA IALDNASIHV NEEAPGLSGP SLEKLVNQYQ NAMKMIKRVS
RVMPEVILTS LVYSKVISLQ DLQDEASLNV VAKSFTDSLT RNEVDGATYR YEVRVNSERN
NYYIALIIRL HGIDTEYKID QEFIESIEYT RLRELNEAIN GLIEEGGYVK RNDKVKPIFS
FAEGLDWLMA ESKKGQYIQR YKGLGEMNPE QLWETTMDPG SRRMLQVKVE DAIAADQLFT
TLMGDHVEPR RAFIEDNALR VANLDV
//
