ID A0A0L0K457_9ACTN Unreviewed; 707 AA.
AC A0A0L0K457;
DT 11-NOV-2015, integrated into UniProtKB/TrEMBL.
DT 11-NOV-2015, sequence version 1.
DT 27-MAR-2024, entry version 38.
DE RecName: Full=DNA topoisomerase (ATP-hydrolyzing) {ECO:0000256|ARBA:ARBA00012895};
DE EC=5.6.2.2 {ECO:0000256|ARBA:ARBA00012895};
GN ORFNames=IQ63_22370 {ECO:0000313|EMBL:KND32892.1};
OS Streptomyces acidiscabies.
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces.
OX NCBI_TaxID=42234 {ECO:0000313|EMBL:KND32892.1, ECO:0000313|Proteomes:UP000037151};
RN [1] {ECO:0000313|Proteomes:UP000037151}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NCPPB 4445 {ECO:0000313|Proteomes:UP000037151};
RA Harrison J., Sapp M., Thwaites R., Studholme D.J.;
RT "Genome sequencing of plant-pathogenic Streptomyces species.";
RL Submitted (JUL-2014) 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:KND32892.1}.
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DR EMBL; JPPY01000132; KND32892.1; -; Genomic_DNA.
DR RefSeq; WP_050372216.1; NZ_KQ257822.1.
DR AlphaFoldDB; A0A0L0K457; -.
DR PATRIC; fig|42234.21.peg.4625; -.
DR OrthoDB; 9802808at2; -.
DR Proteomes; UP000037151; 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:KND32892.1};
KW Magnesium {ECO:0000256|ARBA:ARBA00022842};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Reference proteome {ECO:0000313|Proteomes:UP000037151};
KW Topoisomerase {ECO:0000256|ARBA:ARBA00023029}.
FT DOMAIN 480..594
FT /note="Toprim"
FT /evidence="ECO:0000259|PROSITE:PS50880"
SQ SEQUENCE 707 AA; 77026 MW; EC8C379183423252 CRC64;
MTADTSVPST ALLAGADRDG SNYTARHLLV LEGLEAVRKR PGMYIGSTDS RGLMHCLWEI
IDNSVDEALG GYCDHIDVVL HDDGSVEVRD NGRGIPVDVE PKTGLSGVEV VMTKLHAGGK
FGGGSYAASG GLHGVGASVV NALSARLDVE VDRNGSTHAI SFRRGVPGAF AAAGPDAGFE
SQSGLRKTKR VAKARTGTRV RYWADRQIFL KDAKLSLEHL HQRARQTAFL VPGLTIVVRD
ELGLGEGGSK GEESFRFDGG ISEFCEYLAG DKPVCDILRF TGQGTFRETV PVLDEHGQMT
PTQVTRELGV DVAMRWGTGY DTTLKSFVNI IATPKGGTHV AGFEQAIVTT MNEVLRAKKL
LRVAEDGVLK DDALEGLTAV VTVRLAEPQF EGQTKEVLGT SAARRIVTQV ISKELKAFLT
STKRDAGAQA RVVMEKVVAA ARTRVAARQH KDAQRRKTAL ESSSLPAKLA DCRSDDVDRS
ELFIVEGDSA LGTAKLARNS EFQALLPIRG KILNVQKSSV TDMLKNAECG AIIQVIGAGS
GRTFDLETAR YGKIIMMTDA DVDGSHIRCL LLTLFQRYMR PMVEAGRVFA AVPPLHRIEL
VQPKKGQDKY VYTYSDRELR DKLMEFQTKG VRYKDSIQRY KGLGEMDADQ LAETTMDPRH
RTLRRINLSD LEAAEQVFDL LMGNDVAPRK EFISSSAATL DRSRIDA
//
