ID Q83VW6_STRRC Unreviewed; 702 AA.
AC Q83VW6;
DT 01-JUN-2003, integrated into UniProtKB/TrEMBL.
DT 01-JUN-2003, sequence version 1.
DT 27-MAR-2024, entry version 109.
DE RecName: Full=DNA topoisomerase (ATP-hydrolyzing) {ECO:0000256|ARBA:ARBA00012895};
DE EC=5.6.2.2 {ECO:0000256|ARBA:ARBA00012895};
GN Name=parYR {ECO:0000313|EMBL:AAN75469.1};
OS Streptomyces roseochromogenus subsp. oscitans.
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces.
OX NCBI_TaxID=149682 {ECO:0000313|EMBL:AAN75469.1};
RN [1] {ECO:0000313|EMBL:AAN75469.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=DS 12.976 {ECO:0000313|EMBL:AAN75469.1};
RX PubMed=12604514; DOI=10.1128/AAC.47.3.869-877.2003;
RA Schmutz E., Muhlenweg A., Li S.M., Heide L.;
RT "Resistance genes of aminocoumarin producers: two type II topoisomerase
RT genes confer resistance against coumermycin A1 and clorobiocin.";
RL Antimicrob. Agents Chemother. 47:869-877(2003).
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP-dependent breakage, passage and rejoining of double-
CC stranded DNA.; EC=5.6.2.2; Evidence={ECO:0000256|ARBA:ARBA00000185};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000256|ARBA:ARBA00001946};
CC -!- SIMILARITY: Belongs to the type II topoisomerase GyrB family.
CC {ECO:0000256|ARBA:ARBA00010708}.
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DR EMBL; AY136281; AAN75469.1; -; Genomic_DNA.
DR AlphaFoldDB; Q83VW6; -.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR GO; GO:0034335; F:DNA negative supercoiling activity; IEA:UniProt.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0006265; P:DNA topological change; IEA:InterPro.
DR CDD; cd16928; HATPase_GyrB-like; 1.
DR CDD; cd00822; TopoII_Trans_DNA_gyrase; 1.
DR Gene3D; 3.30.230.10; -; 1.
DR Gene3D; 3.40.50.670; -; 1.
DR Gene3D; 3.30.565.10; Histidine kinase-like ATPase, C-terminal domain; 1.
DR InterPro; IPR002288; DNA_gyrase_B_C.
DR InterPro; IPR003594; HATPase_C.
DR InterPro; IPR036890; HATPase_C_sf.
DR InterPro; IPR020568; Ribosomal_Su5_D2-typ_SF.
DR InterPro; IPR014721; Ribsml_uS5_D2-typ_fold_subgr.
DR InterPro; IPR001241; Topo_IIA.
DR InterPro; IPR013760; Topo_IIA-like_dom_sf.
DR InterPro; IPR000565; Topo_IIA_B.
DR InterPro; IPR013759; Topo_IIA_B_C.
DR InterPro; IPR013506; Topo_IIA_bsu_dom2.
DR InterPro; IPR018522; TopoIIA_CS.
DR InterPro; IPR006171; TOPRIM_domain.
DR PANTHER; PTHR45866:SF1; DNA GYRASE SUBUNIT B, MITOCHONDRIAL; 1.
DR PANTHER; PTHR45866; DNA GYRASE/TOPOISOMERASE SUBUNIT B; 1.
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; PR01159; DNAGYRASEB.
DR PRINTS; PR00418; TPI2FAMILY.
DR SMART; SM00387; HATPase_c; 1.
DR SMART; SM00433; TOP2c; 1.
DR SUPFAM; SSF55874; ATPase domain of HSP90 chaperone/DNA topoisomerase II/histidine kinase; 1.
DR SUPFAM; SSF54211; Ribosomal protein S5 domain 2-like; 1.
DR SUPFAM; SSF56719; Type II DNA topoisomerase; 1.
DR PROSITE; PS00177; TOPOISOMERASE_II; 1.
DR PROSITE; PS50880; TOPRIM; 1.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW DNA-binding {ECO:0000256|ARBA:ARBA00023125};
KW Isomerase {ECO:0000256|ARBA:ARBA00023235, ECO:0000313|EMBL:AAN75469.1};
KW Magnesium {ECO:0000256|ARBA:ARBA00022842};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Topoisomerase {ECO:0000256|ARBA:ARBA00023029}.
FT DOMAIN 475..589
FT /note="Toprim"
FT /evidence="ECO:0000259|PROSITE:PS50880"
SQ SEQUENCE 702 AA; 76722 MW; FA13366DA62D51E3 CRC64;
MSTLPAPAAG SRPQDGSDYT ARHLMVLEGL EAVRKRPGMY IGSSDSRGLM HCLWEIIDNA
VDEALAGACD YIEVILHDDG SVEVTDNGRG IPVDTEPRTG LSGVEIAYTK LHAGGKFGGG
SYAASGGLHG VGASVVNALS ARLDVEVDRH GRTHAISFRR GTPGTYTGPG PDAPFTPAQG
LRQTTKIPKS RTGTRVRYWA DRQSFLKDAK LSLENLHQRA RQTAFLVPGL TIVVRDEFGL
GEGGSKGEES FRFDGGISEF CEFLASDTPV CDILRFSGQG TFKETVPVLD EHGQMTPTEV
TRELGVDVAL RWGTGYDTTV RSFVNIIATP KGGTHVAGFE QAVGKTLNEV LRAKKLLRVA
EDDIAKDDAL EGLTAVVTVR LAEPQFEGQT KEVLGTSAAR RIVNNVISKE LKAFLTSTKR
DAAQQARVVM EKAVAAARTR IAARQHKDAQ RKSALESSSL PAKLADCRSD DVDRSELFIV
EGDSALGTAK LARNSEFQAL LPIRGKILNV QRSSVSDMLK NAECGAIIQV IGAGSGRTFD
IDTARYRKII MMTDADVDGS HIRTLLLTLF HRYMRPMVEA GRVFAAVPPL HRIELVQPRK
GQERYVYTYS DRELRDKLME FQSKGIRYKD SVQRYKGLGE MDADQLAETT MDPRHRTLRR
INLTDLEAAE GVFDLLMGND VAPRKEFITS SAATLDRSRI DV
//
