ID E4MZE6_KITSK Unreviewed; 663 AA.
AC E4MZE6;
DT 08-FEB-2011, integrated into UniProtKB/TrEMBL.
DT 08-FEB-2011, sequence version 1.
DT 01-MAY-2013, entry version 16.
DE RecName: Full=DNA gyrase subunit B;
DE EC=5.99.1.3;
GN Name=gyrB; OrderedLocusNames=KSE_39240;
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;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 33774 / DSM 43861 / JCM 3304 / KCC A-0304 / NBRC 14216 /
RC KM-6054;
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 (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; 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 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: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 441 555 Toprim (By similarity).
FT METAL 447 447 Magnesium 1; catalytic (By similarity).
FT METAL 520 520 Magnesium 1; catalytic (By similarity).
FT METAL 520 520 Magnesium 2 (By similarity).
FT METAL 522 522 Magnesium 2 (By similarity).
FT SITE 472 472 Interaction with DNA (By similarity).
FT SITE 475 475 Interaction with DNA (By similarity).
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
//
