ID A0A0D7CGW4_9ACTN Unreviewed; 706 AA.
AC A0A0D7CGW4;
DT 27-MAY-2015, integrated into UniProtKB/TrEMBL.
DT 27-MAY-2015, sequence version 1.
DT 27-MAR-2024, entry version 44.
DE RecName: Full=DNA topoisomerase (ATP-hydrolyzing) {ECO:0000256|ARBA:ARBA00012895};
DE EC=5.6.2.2 {ECO:0000256|ARBA:ARBA00012895};
GN ORFNames=SNA_31700 {ECO:0000313|EMBL:KIZ14662.1};
OS Streptomyces natalensis ATCC 27448.
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces.
OX NCBI_TaxID=1240678 {ECO:0000313|EMBL:KIZ14662.1, ECO:0000313|Proteomes:UP000032458};
RN [1] {ECO:0000313|EMBL:KIZ14662.1, ECO:0000313|Proteomes:UP000032458}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 27448 {ECO:0000313|EMBL:KIZ14662.1,
RC ECO:0000313|Proteomes:UP000032458};
RA Mendes M.V., Beites T., Pires S., Santos C.L., Moradas-Ferreira P.;
RT "Draft genome sequence of Streptomyces natalensis ATCC 27448, producer of
RT the antifungal pimaricin.";
RL Submitted (SEP-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:KIZ14662.1}.
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DR EMBL; JRKI01000056; KIZ14662.1; -; Genomic_DNA.
DR RefSeq; WP_030068920.1; NZ_JRKI01000056.1.
DR AlphaFoldDB; A0A0D7CGW4; -.
DR PATRIC; fig|1240678.4.peg.6780; -.
DR Proteomes; UP000032458; 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:KIZ14662.1};
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 479..593
FT /note="Toprim"
FT /evidence="ECO:0000259|PROSITE:PS50880"
SQ SEQUENCE 706 AA; 77324 MW; DA23D23D287F3490 CRC64;
MTAEMSVPST AVLTGADRDG SNYTARHLLV LEGLEAVRKR PGMYIGSTDS RGLMHCLWEI
IDNSVDEALG GYCDHIEVIL HDDGSVEVRD NGRGIPVDVE PKTGLSGVEV VMTKLHAGGK
FGGGSYAASG GLHGVGASVV NALSARLDVE VDRSSKTHSI SFRRGVPGVF TESGPDAPFD
PGNGLVKGKR IPKTRTGTRV RYWADRQIFL KDAKLSLENL HARARQTAFL VPGLTIVVRD
ERGIDGAGKT EETFRYDGGI SEFCEYLAQD KAVCDVLRLT GQGTFKETVP VLDDRGHMTP
TEVTRELGVD IALRWGTGYD AAVRSFVNII ATPKGGTHVS GFERSVTKTV NEVLRAQKLL
RVAEDDVVKD DAMEGLTAVV TVRLAEPQFE GQTKEVLGTS AASRIVAQVV SRELKAFLTS
TKRDAKQQAR SVLEKVVAAA RTRIAARQHK EAQRRKTALE SSSLPAKLAD CRSDDVDRSE
LFIVEGDSAL GTAKLARSSE FQALLPIRGK ILNVQKASVS DMLKNAECGA IIQVIGAGSG
RTFDIDAARY GKVIFLADAD VDGAHIRILL LTLFQRYMRP MVEQGRVFSA VPPLHRIELI
NPKKGQDKYI YTYSDNELRQ TLLELQRKNV RYKDSIQRYK GLGEMDADQL AETTMDPRHR
TLRRINIGDL EAAEKAFDLL MGNEVAPRKE FITNSASFLD RSRIDT
//
