ID A5D6E8_PELTS Unreviewed; 643 AA.
AC A5D6E8;
DT 12-JUN-2007, integrated into UniProtKB/TrEMBL.
DT 12-JUN-2007, sequence version 1.
DT 01-MAY-2013, entry version 48.
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.
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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; IFETTEF; -.
DR ProtClustDB; PRK05644; -.
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 428 542 Toprim (By similarity).
FT METAL 434 434 Magnesium 1; catalytic (By similarity).
FT METAL 507 507 Magnesium 1; catalytic (By similarity).
FT METAL 507 507 Magnesium 2 (By similarity).
FT METAL 509 509 Magnesium 2 (By similarity).
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
//
