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Database: UniProt/TrEMBL
Entry: E4MZE6_KITSK
LinkDB: E4MZE6_KITSK
Original site: E4MZE6_KITSK 
ID   E4MZE6_KITSK            Unreviewed;       663 AA.
AC   E4MZE6;
DT   08-FEB-2011, integrated into UniProtKB/TrEMBL.
DT   08-FEB-2011, sequence version 1.
DT   26-NOV-2014, entry version 29.
DE   RecName: Full=DNA gyrase subunit B {ECO:0000256|HAMAP-Rule:MF_01898, ECO:0000256|RuleBase:RU003363};
DE            EC=5.99.1.3 {ECO:0000256|HAMAP-Rule:MF_01898, ECO:0000256|RuleBase:RU003363};
GN   Name=gyrB {ECO:0000256|HAMAP-Rule:MF_01898,
GN   ECO:0000313|EMBL:BAJ29720.1};
GN   OrderedLocusNames=KSE_39240 {ECO:0000313|EMBL:BAJ29720.1};
OS   Kitasatospora setae (strain ATCC 33774 / DSM 43861 / JCM 3304 / KCC
OS   A-0304 / NBRC 14216 / KM-6054) (Streptomyces setae).
OC   Bacteria; Actinobacteria; Actinobacteridae; Actinomycetales;
OC   Streptomycineae; Streptomycetaceae; Kitasatospora.
OX   NCBI_TaxID=452652 {ECO:0000313|EMBL:BAJ29720.1, ECO:0000313|Proteomes:UP000007076};
RN   [1] {ECO:0000313|EMBL:BAJ29720.1, ECO:0000313|Proteomes:UP000007076}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 33774 / DSM 43861 / JCM 3304 / KCC A-0304 / NBRC 14216 /
RC   KM-6054 {ECO:0000313|Proteomes:UP000007076};
RX   PubMed=21059706; DOI=10.1093/dnares/dsq026;
RA   Ichikawa N., Oguchi A., Ikeda H., Ishikawa J., Kitani S., Watanabe Y.,
RA   Nakamura S., Katano Y., Kishi E., Sasagawa M., Ankai A., Fukui S.,
RA   Hashimoto Y., Kamata S., Otoguro M., Tanikawa S., Nihira T.,
RA   Horinouchi S., Ohnishi Y., Hayakawa M., Kuzuyama T., Arisawa A.,
RA   Nomoto F., Miura H., Takahashi Y., Fujita N.;
RT   "Genome sequence of Kitasatospora setae NBRC 14216T: an evolutionary
RT   snapshot of the family Streptomycetaceae.";
RL   DNA Res. 17:393-406(2010).
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.
CC       {ECO:0000256|HAMAP-Rule:MF_01898, ECO:0000256|RuleBase:RU003363}.
CC   -!- CATALYTIC ACTIVITY: ATP-dependent breakage, passage and rejoining
CC       of double-stranded DNA. {ECO:0000256|HAMAP-Rule:MF_01898,
CC       ECO:0000256|SAAS:SAAS00030552}.
CC   -!- COFACTOR:
CC       Note=Magnesium. Binds two Mg(2+) per subunit. The magnesium ions
CC       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+).
CC       {ECO:0000256|HAMAP-Rule:MF_01898};
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. {ECO:0000256|HAMAP-Rule:MF_01898}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_01898}.
CC   -!- SIMILARITY: Belongs to the type II topoisomerase family.
CC       {ECO:0000256|HAMAP-Rule:MF_01898, ECO:0000256|RuleBase:RU000380}.
CC   -!- SIMILARITY: Contains 1 Toprim domain. {ECO:0000256|HAMAP-
CC       Rule:MF_01898}.
CC   -!- SIMILARITY: Contains Toprim domain.
CC       {ECO:0000256|SAAS:SAAS00106838}.
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DR   EMBL; AP010968; BAJ29720.1; -; Genomic_DNA.
DR   RefSeq; YP_004905676.1; NC_016109.1.
DR   EnsemblBacteria; BAJ29720; BAJ29720; KSE_39240.
DR   GeneID; 11348518; -.
DR   KEGG; ksk:KSE_39240; -.
DR   KO; K02470; -.
DR   OMA; HIIIMTD; -.
DR   BioCyc; KSET452652:GJFD-3923-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_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; 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 {ECO:0000256|HAMAP-Rule:MF_01898,
KW   ECO:0000256|RuleBase:RU000380};
KW   Complete proteome {ECO:0000313|Proteomes:UP000007076};
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|RuleBase:RU000380};
KW   Magnesium {ECO:0000256|HAMAP-Rule:MF_01898};
KW   Metal-binding {ECO:0000256|HAMAP-Rule:MF_01898};
KW   Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_01898,
KW   ECO:0000256|RuleBase:RU000380};
KW   Reference proteome {ECO:0000313|Proteomes:UP000007076};
KW   Topoisomerase {ECO:0000256|HAMAP-Rule:MF_01898,
KW   ECO:0000256|RuleBase:RU000380}.
FT   DOMAIN      441    555       Toprim. {ECO:0000256|HAMAP-Rule:
FT                                MF_01898}.
FT   METAL       447    447       Magnesium 1; catalytic.
FT                                {ECO:0000256|HAMAP-Rule:MF_01898}.
FT   METAL       520    520       Magnesium 1; catalytic.
FT                                {ECO:0000256|HAMAP-Rule:MF_01898}.
FT   METAL       520    520       Magnesium 2. {ECO:0000256|HAMAP-Rule:
FT                                MF_01898}.
FT   METAL       522    522       Magnesium 2. {ECO:0000256|HAMAP-Rule:
FT                                MF_01898}.
FT   SITE        472    472       Interaction with DNA. {ECO:0000256|HAMAP-
FT                                Rule:MF_01898}.
FT   SITE        475    475       Interaction with DNA. {ECO:0000256|HAMAP-
FT                                Rule:MF_01898}.
SQ   SEQUENCE   663 AA;  72570 MW;  67B5D2258DCD564D CRC64;
     MADSGNPSQT PDPSDQKAYD ASAIQVLEGL DAVRKRPGMY IGSTGERGLH HLVYEIVDNS
     VDEALAGHAD TIGVTILADG GVRVVDNGRG IPVGIMPGQD RPAVEVVLTV LHAGGKFGGG
     GYAVSGGLHG VGISVVNALS TRLAVDISTD GARWTQEYKS GAPTAPLARH EETGETGTTV
     TFWADPDIFE TTVYSFETLS RRFQEMAFLN KGLTIALTDE RPEHVDDEGK PLSVTYRYDG
     GIADFVAHLN SRKGEVIHPS VIDFEAEDKD KTISAEIAMQ WNSSYTEGVY SFANTIHTHG
     GGTHEEGFRA ALTGLMNRYA RDKKLLREKD DNLSGEDIRE GLTAIISVKL GEPQFEGQTK
     DKLGNTEAKT FVQKVVNEHL ADWLDRNPAE AADIIRKSIQ AASARVAARK ARDLTRRKGL
     LESASLPGKL SDCQSKDPAE CEIFIVEGDS AGGSAKQGRD PRTQAILPIR GKILNVEKAR
     IDKVLQNTEV QALISAFGCG IQEDYDAAKL RYHKIVLMAD ADVDGQHIRT LLLTLLFRFM
     RPLVEAGYVY LAMPPLYKIK WGRDEFEYAY SDRERDALIA AGVEAGRRLP KDDAIQRFKG
     LGEMNAEELR VTTMDAAHRL LLQVTLEDAA RADDLFSVLM GEDVEARRSF IQRNAKDVRF
     LDV
//
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