ID D8J639_HALJB Unreviewed; 635 AA.
AC D8J639;
DT 05-OCT-2010, integrated into UniProtKB/TrEMBL.
DT 05-OCT-2010, sequence version 1.
DT 29-MAY-2013, entry version 23.
DE RecName: Full=DNA gyrase subunit B;
DE EC=5.99.1.3;
GN Name=gyrB; OrderedLocusNames=HacjB3_11870; ORFNames=C497_10758;
OS Halalkalicoccus jeotgali (strain DSM 18796 / CECT 7217 / JCM 14584 /
OS KCTC 4019 / B3).
OC Archaea; Euryarchaeota; Halobacteria; Halobacteriales;
OC Halobacteriaceae; Halalkalicoccus.
OX NCBI_TaxID=795797;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=B3, and DSM 18796 / CECT 7217 / JCM 14584 / KCTC 4019 / B3;
RX PubMed=20601480; DOI=10.1128/JB.00663-10;
RA Roh S.W., Nam Y.D., Nam S.H., Choi S.H., Park H.S., Bae J.W.;
RT "Complete genome sequence of Halalkalicoccus jeotgali B3(T), an
RT extremely halophilic archaeon.";
RL J. Bacteriol. 192:4528-4529(2010).
RN [2]
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=B3;
RA Becker E.A., Seitzer P., Tritt A., Larsen D., Yao A., Wu D.,
RA Darling A., Eisen J.A., Facciotti M.T.;
RL Submitted (NOV-2012) 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 -----------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution-NoDerivs License
CC -----------------------------------------------------------------------
DR EMBL; CP002062; ADJ15757.1; -; Genomic_DNA.
DR EMBL; AOHV01000027; ELY37219.1; -; Genomic_DNA.
DR RefSeq; YP_003737549.1; NC_014297.1.
DR ProteinModelPortal; D8J639; -.
DR EnsemblBacteria; ADJ15757; ADJ15757; HacjB3_11870.
DR GeneID; 9420188; -.
DR KEGG; hje:HacjB3_11870; -.
DR HOGENOM; HOG000075154; -.
DR KO; K02470; -.
DR OMA; IFETTEF; -.
DR BioCyc; HJEO795797:GKCD-2403-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 421 535 Toprim (By similarity).
FT METAL 427 427 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 452 452 Interaction with DNA (By similarity).
FT SITE 455 455 Interaction with DNA (By similarity).
SQ SEQUENCE 635 AA; 70752 MW; DF5504DA7649F834 CRC64;
MSEQSEYGAG QIQVLEGLEA VRTRPAMYIG STDSRGLHHL VYEVVDNAID EALAGYCDTI
GVTIHEDGSV SVADDGRGIP VDTHAEYDRP AVEVIMTVLH AGGKFDSKSY QVSGGLHGVG
VSVVNALSER LEVEIRRDGA VWHHRFDHGA PEGDIERVRD LEAEEETGTT VRFWPDDGIF
EDREFVVSTL ENRIRELAFL NPGVEITLAD ERDETESTFQ YDGGIREFVE YLNETRTPLH
EDVLYLDDEE RNIQVEVAMQ ATDELQGSIH AFANNINTRE GGTHLTGFKT ALTRVVNDYA
NGEGLLDEID ENLRGEDIRE GLTAVISIKH PDPQFEGQTK TKLGNSEVRG IVESAVHEGL
GTYFEEHPDT AQAVVRKAVE AAKARKAAKQ AEELTRRKSA LESTALPGKL ADCQTRDPNE
AELFVVEGDS AGGSAKQGRN RKFQAILPLK GKILNVEKHR LDRILENNEI RDLITAVGAG
VGEEFDIDEA RYKRIVIMTD ADVDGAHIRT LLLTLFYRHM RPLIEAGYVY AAQPPLYRLR
YGGETREAMA EAEREAIIDE YGAPDRIQRF KGLGEMNPDQ LWETTMNPDN RVLKRVTVED
AAAADRMFSV LMGDAVEPRK QFIQEHAKEA EWVDI
//
