ID A0A2V2PZU2_9ACTN Unreviewed; 708 AA.
AC A0A2V2PZU2;
DT 12-SEP-2018, integrated into UniProtKB/TrEMBL.
DT 12-SEP-2018, sequence version 1.
DT 27-MAR-2024, entry version 27.
DE RecName: Full=DNA topoisomerase (ATP-hydrolyzing) {ECO:0000256|ARBA:ARBA00012895};
DE EC=5.6.2.2 {ECO:0000256|ARBA:ARBA00012895};
GN ORFNames=DKT74_28405 {ECO:0000313|EMBL:PWS41281.1};
OS Streptomyces sp. ZEA17I.
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces.
OX NCBI_TaxID=2202516 {ECO:0000313|EMBL:PWS41281.1, ECO:0000313|Proteomes:UP000245984};
RN [1] {ECO:0000313|EMBL:PWS41281.1, ECO:0000313|Proteomes:UP000245984}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ZEA17I {ECO:0000313|EMBL:PWS41281.1,
RC ECO:0000313|Proteomes:UP000245984};
RA Chen X., Qin K., Li H., Cortesi P., Saracchi M., Sang W., Yang M.;
RT "Genome sequencing and identification of chitinase family genes of
RT Streptomyces sp. ZEA17I, a biocontrol agent against plant pathogens.";
RL Submitted (MAY-2018) to the EMBL/GenBank/DDBJ databases.
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}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:PWS41281.1}.
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DR EMBL; QGMS01001480; PWS41281.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2V2PZU2; -.
DR Proteomes; UP000245984; Unassembled WGS sequence.
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:PWS41281.1};
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 481..595
FT /note="Toprim"
FT /evidence="ECO:0000259|PROSITE:PS50880"
FT REGION 173..193
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 708 AA; 77402 MW; CEBDF93E37536A8A CRC64;
MTAETSVPST AMLAAAGGDR DSSNYTARHL LVLEGLEAVR KRPGMYIGST DSRGLMHCLW
EIIDNSVDEA LGGHCDLIEV ILHDDASVEV RDNGRGIPVD VEPKTGLSGV EVVMTKLHAG
GKFGGGSYAA SGGLHGVGAS VVNALSARLD VEVDRNSATH SISFRRGVPG LFTEQGPDSP
FDPANGLRKG KRVPKTRTGT RVRYWADRQI FLKDARLNLE TLHQRARQTA FLVPGLTLVV
RDERGIDGEG KTEETFRFDG GISEFCEYLA QDKAVCDVQR LTGTGTFKET VPVLDDRGHM
TATEVTRELG VDIALRWGTG YDTTIRSFVN IIATPKGGTH VTGFERSLTK TVNEALRSAK
LLRVAEDDVV KDDALEGLTA VVTVRLAEPQ FEGQTKEVLG TSAANRIVAA VVARELKAFL
TSTKRDAKAQ ARAVLEKAVA AARTRIAARQ HKDAQRRKTA LESSSLPAKL ADCRSDDVER
SELFIVEGDS ALGTAKLARN SEFQALLPIR GKILNVQKSS VSDMLKNAEC GAIIQVIGAG
SGRTFDIDAA RYGKVIMMTD ADVDGSHIRT LLLTLFQRYM RPMVEAGRVF AAVPPLHRIE
LVQPKKGQDK YVYTYSDNEL RQTLLEFQRK NIRIKESIQR YKGLGEMDAD QLAETTMDPR
HRTLRRINIG DLDSAEQVFD LLMGNEVAPR KEFITSSAAT LDRSRIDA
//
