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Database: UniProt/TrEMBL
Entry: A5D6E8_PELTS
LinkDB: A5D6E8_PELTS
Original site: A5D6E8_PELTS 
ID   A5D6E8_PELTS            Unreviewed;       643 AA.
AC   A5D6E8;
DT   12-JUN-2007, integrated into UniProtKB/TrEMBL.
DT   12-JUN-2007, sequence version 1.
DT   07-SEP-2016, entry version 76.
DE   RecName: Full=DNA gyrase subunit B {ECO:0000256|HAMAP-Rule:MF_01898, ECO:0000256|SAAS:SAAS00555050};
DE            EC=5.99.1.3 {ECO:0000256|HAMAP-Rule:MF_01898, ECO:0000256|SAAS:SAAS00470646};
GN   Name=GyrB {ECO:0000313|EMBL:BAF58186.1};
GN   Synonyms=gyrB {ECO:0000256|HAMAP-Rule:MF_01898};
GN   OrderedLocusNames=PTH_0005 {ECO:0000313|EMBL:BAF58186.1};
OS   Pelotomaculum thermopropionicum (strain DSM 13744 / JCM 10971 / SI).
OC   Bacteria; Firmicutes; Clostridia; Clostridiales; Peptococcaceae;
OC   Pelotomaculum.
OX   NCBI_TaxID=370438 {ECO:0000313|EMBL:BAF58186.1, ECO:0000313|Proteomes:UP000006556};
RN   [1] {ECO:0000313|Proteomes:UP000006556}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 13744 / JCM 10971 / SI {ECO:0000313|Proteomes:UP000006556};
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: A type II topoisomerase that negatively supercoils
CC       closed circular double-stranded (ds) DNA in an ATP-dependent
CC       manner to modulate DNA topology and maintain chromosomes in an
CC       underwound state. Negative supercoiling favors strand separation,
CC       and DNA replication, transcription, recombination and repair, all
CC       of which involve strand separation. Also able to catalyze the
CC       interconversion of other topological isomers of dsDNA rings,
CC       including catenanes and knotted rings. Type II topoisomerases
CC       break and join 2 DNA strands simultaneously in an ATP-dependent
CC       manner. {ECO:0000256|HAMAP-Rule:MF_01898}.
CC   -!- CATALYTIC ACTIVITY: ATP-dependent breakage, passage and rejoining
CC       of double-stranded DNA. {ECO:0000256|HAMAP-Rule:MF_01898,
CC       ECO:0000256|SAAS:SAAS00470725}.
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000256|HAMAP-
CC         Rule:MF_01898};
CC       Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000256|HAMAP-
CC         Rule:MF_01898};
CC       Name=Ca(2+); Xref=ChEBI:CHEBI:29108; Evidence={ECO:0000256|HAMAP-
CC         Rule:MF_01898};
CC       Note=Binds two Mg(2+) per subunit. The magnesium ions form salt
CC       bridges with both the protein and the DNA. Can also accept other
CC       divalent metal cations, such as Mn(2+) or Ca(2+).
CC       {ECO:0000256|HAMAP-Rule:MF_01898};
CC   -!- SUBUNIT: Heterotetramer, composed of two GyrA and two GyrB chains.
CC       In the heterotetramer, GyrA contains the active site tyrosine that
CC       forms a transient covalent intermediate with DNA, while GyrB binds
CC       cofactors and catalyzes ATP hydrolysis. {ECO:0000256|HAMAP-
CC       Rule:MF_01898}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_01898}.
CC   -!- MISCELLANEOUS: Few gyrases are as efficient as E.coli at forming
CC       negative supercoils. Not all organisms have 2 type II
CC       topoisomerases; in organisms with a single type II topoisomerase
CC       this enzyme also has to decatenate newly replicated chromosomes.
CC       {ECO:0000256|HAMAP-Rule:MF_01898}.
CC   -!- SIMILARITY: Belongs to the type II topoisomerase family.
CC       {ECO:0000256|HAMAP-Rule:MF_01898}.
CC   -!- SIMILARITY: Contains 1 Toprim domain. {ECO:0000256|HAMAP-
CC       Rule:MF_01898}.
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DR   EMBL; AP009389; BAF58186.1; -; Genomic_DNA.
DR   RefSeq; WP_011928085.1; NC_009454.1.
DR   ProteinModelPortal; A5D6E8; -.
DR   SMR; A5D6E8; 21-401.
DR   STRING; 370438.PTH_0005; -.
DR   EnsemblBacteria; BAF58186; BAF58186; PTH_0005.
DR   KEGG; pth:PTH_0005; -.
DR   PATRIC; 22906732; VBIPelThe8413_0005.
DR   eggNOG; ENOG4105C7D; Bacteria.
DR   eggNOG; COG0187; LUCA.
DR   HOGENOM; HOG000075154; -.
DR   KO; K02470; -.
DR   OMA; IKNMITA; -.
DR   OrthoDB; POG091H01XP; -.
DR   BioCyc; PTHE370438:GCGQ-5-MONOMER; -.
DR   Proteomes; UP000006556; Chromosome.
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:UniProtKB-HAMAP.
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_C.
DR   InterPro; IPR020568; Ribosomal_S5_D2-typ_fold.
DR   InterPro; IPR014721; Ribosomal_S5_D2-typ_fold_subgr.
DR   InterPro; IPR001241; Topo_IIA.
DR   InterPro; IPR013760; Topo_IIA-like_dom.
DR   InterPro; IPR013506; Topo_IIA_bsu_dom2.
DR   InterPro; IPR013759; Topo_IIA_cen_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 {ECO:0000256|HAMAP-Rule:MF_01898,
KW   ECO:0000256|SAAS:SAAS00528655};
KW   Complete proteome {ECO:0000313|Proteomes:UP000006556};
KW   Cytoplasm {ECO:0000256|HAMAP-Rule:MF_01898};
KW   DNA-binding {ECO:0000256|HAMAP-Rule:MF_01898};
KW   Isomerase {ECO:0000256|HAMAP-Rule:MF_01898,
KW   ECO:0000256|SAAS:SAAS00470744, ECO:0000313|EMBL:BAF58186.1};
KW   Magnesium {ECO:0000256|HAMAP-Rule:MF_01898,
KW   ECO:0000256|SAAS:SAAS00445358};
KW   Metal-binding {ECO:0000256|HAMAP-Rule:MF_01898,
KW   ECO:0000256|SAAS:SAAS00445373};
KW   Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_01898,
KW   ECO:0000256|SAAS:SAAS00528653};
KW   Reference proteome {ECO:0000313|Proteomes:UP000006556};
KW   Topoisomerase {ECO:0000256|HAMAP-Rule:MF_01898,
KW   ECO:0000256|SAAS:SAAS00528650}.
FT   DOMAIN      428    542       Toprim. {ECO:0000259|PROSITE:PS50880}.
FT   METAL       434    434       Magnesium 1; catalytic.
FT                                {ECO:0000256|HAMAP-Rule:MF_01898}.
FT   METAL       507    507       Magnesium 1; catalytic.
FT                                {ECO:0000256|HAMAP-Rule:MF_01898}.
FT   METAL       507    507       Magnesium 2. {ECO:0000256|HAMAP-Rule:
FT                                MF_01898}.
FT   METAL       509    509       Magnesium 2. {ECO:0000256|HAMAP-Rule:
FT                                MF_01898}.
FT   SITE        459    459       Interaction with DNA. {ECO:0000256|HAMAP-
FT                                Rule:MF_01898}.
FT   SITE        462    462       Interaction with DNA. {ECO:0000256|HAMAP-
FT                                Rule:MF_01898}.
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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