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Entry: A5D6E8_PELTS
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ID   A5D6E8_PELTS            Unreviewed;       643 AA.
AC   A5D6E8;
DT   12-JUN-2007, integrated into UniProtKB/TrEMBL.
DT   12-JUN-2007, sequence version 1.
DT   11-JUN-2014, entry version 58.
DE   RecName: Full=DNA gyrase subunit B;
DE            EC=5.99.1.3;
GN   Name=GyrB; Synonyms=gyrB; OrderedLocusNames=PTH_0005;
OS   Pelotomaculum thermopropionicum (strain DSM 13744 / JCM 10971 / SI).
OC   Bacteria; Firmicutes; Clostridia; Clostridiales; Peptococcaceae;
OC   Pelotomaculum.
OX   NCBI_TaxID=370438;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 13744 / JCM 10971 / SI;
RX   PubMed=18218977; DOI=10.1101/gr.7136508;
RA   Kosaka T., Kato S., Shimoyama T., Ishii S., Abe T., Watanabe K.;
RT   "The genome of Pelotomaculum thermopropionicum reveals niche-
RT   associated evolution in anaerobic microbiota.";
RL   Genome Res. 18:442-448(2008).
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; AP009389; BAF58186.1; -; Genomic_DNA.
DR   RefSeq; YP_001210555.1; NC_009454.1.
DR   ProteinModelPortal; A5D6E8; -.
DR   SMR; A5D6E8; 21-401.
DR   STRING; 370438.PTH_0005; -.
DR   EnsemblBacteria; BAF58186; BAF58186; PTH_0005.
DR   GeneID; 5139744; -.
DR   KEGG; pth:PTH_0005; -.
DR   PATRIC; 22906732; VBIPelThe8413_0005.
DR   eggNOG; COG0187; -.
DR   HOGENOM; HOG000075154; -.
DR   KO; K02470; -.
DR   OMA; HIIIMTD; -.
DR   OrthoDB; EOG6P334W; -.
DR   BioCyc; PTHE370438:GCGQ-5-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: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      428    542       Toprim (By similarity).
FT   METAL       434    434       Magnesium 1; catalytic (By
FT                                similarity){EA9}.
FT   METAL       507    507       Magnesium 1; catalytic (By
FT                                similarity){EA9}.
FT   METAL       507    507       Magnesium 2 (By similarity){EA9}.
FT   METAL       509    509       Magnesium 2 (By similarity){EA9}.
FT   SITE        459    459       Interaction with DNA (By similarity).
FT   SITE        462    462       Interaction with DNA (By similarity).
SQ   SEQUENCE   643 AA;  71287 MW;  4FB17740044E4F77 CRC64;
     MYLALTGDTS NNNNSKYGAE EIQILEGLEA VRRRPGMYIG STSARGLHHL VYEVVDNSID
     EAMAGFCDRI EVILNEDGSA TVIDNGRGIP VDIHPKTGRP AVEVVMTMLH AGGKFGGGGY
     KVSGGLHGVG VSVVNALSLW LEVEVKRDGK VYYQRYSRGI PVTGLLVKGK SSATGTKVTF
     MPDPEIFEDL IFNQDILAQR LRELSFLNMG VKIILKDRRS GQETVFQHDG GIMDFVRYLN
     KSKTPLHGKP IYIQKQKDDV LVEVALQYTD TYVESILSYA NNINTIDGGT HEAGFKAALT
     RVINDYGRKY NLLKNGAGNL SGEDIREGLT AVISVKVPEP QFEGQTKTKL GNSEVRSIVD
     SVVGEGLGIF LEENPSIARR ILEKAVTASR AREAARKARE LTRRKSALEG STLPGKLADC
     SERDPSVSEL YLVEGDSAGG SAKQGRDRRF QAILPLRGKI LNVEKARLDK ILANEEIRAM
     ITALGTGIGE EFDVSKARYH KIILMSDADV DGAHIRTLLL TFFYRYMRPL IEKGYVFIAQ
     PPLYRVKKGK LEKYAYSDAE LEKLLDQIGR DGVSIQRYKG LGEMNAEQLW ETTMDPETRT
     VMQVNLEDAI EADAVFSMLM GDRVEPRRDF IQENARLVRN LDI
//
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