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Database: UniProt
Entry: A0A2S1Z5G5_9ACTN
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ID   A0A2S1Z5G5_9ACTN        Unreviewed;       705 AA.
AC   A0A2S1Z5G5;
DT   18-JUL-2018, integrated into UniProtKB/TrEMBL.
DT   18-JUL-2018, sequence version 1.
DT   27-MAR-2024, entry version 37.
DE   RecName: Full=DNA topoisomerase (ATP-hydrolyzing) {ECO:0000256|ARBA:ARBA00012895};
DE            EC=5.6.2.2 {ECO:0000256|ARBA:ARBA00012895};
GN   ORFNames=DDQ41_24530 {ECO:0000313|EMBL:AWK11552.1}, SSP531S_00670
GN   {ECO:0000313|EMBL:GBP98675.1};
OS   Streptomyces spongiicola.
OC   Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC   Streptomycetaceae; Streptomyces.
OX   NCBI_TaxID=1690221 {ECO:0000313|EMBL:AWK11552.1, ECO:0000313|Proteomes:UP000245051};
RN   [1] {ECO:0000313|EMBL:AWK11552.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=HNM0071 {ECO:0000313|EMBL:AWK11552.1};
RA   Zhou S., Huang X.;
RT   "Complete genome sequence of the Type Strain of Streptomyces spongiicola
RT   HNM0071, the producer of staurosporine.";
RL   Submitted (MAY-2018) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:GBP98675.1, ECO:0000313|Proteomes:UP000265354}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=531S {ECO:0000313|EMBL:GBP98675.1,
RC   ECO:0000313|Proteomes:UP000265354};
RA   Dohra H., Kodani S.;
RT   "Whole Genome Shotgun Sequence of Streptomyces spongiicola strain 531S.";
RL   Submitted (JUL-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}.
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DR   EMBL; CP029254; AWK11552.1; -; Genomic_DNA.
DR   EMBL; BGZL01000001; GBP98675.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A2S1Z5G5; -.
DR   KEGG; sspo:DDQ41_24530; -.
DR   OrthoDB; 9802808at2; -.
DR   Proteomes; UP000245051; Chromosome.
DR   Proteomes; UP000265354; 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:AWK11552.1};
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          478..592
FT                   /note="Toprim"
FT                   /evidence="ECO:0000259|PROSITE:PS50880"
SQ   SEQUENCE   705 AA;  77046 MW;  A25A83905286F2CA CRC64;
     MTAETSVPSS ALLTADRDGS NYTARHLLVL EGLEAVRKRP GMYIGSTDSR GLMHCLWEII
     DNSVDEALGG HCDHIEVILH DDGSVEVRDN GRGIPVDVEP KTGLSGVEVV MTKLHAGGKF
     GGGSYAASGG LHGVGASVVN ALSARLDVEV DRGGATHSIS FRRGVPGIFT ESGPDAPFDP
     AGGLIKGRRV PRTRTGTRVR YWADRQIFLK DARLQLETLH QRARQTAFLV PGLTIVVRDE
     RDLEGEGKSQ EIFRFDGGIS EFCEFLAQDK AVCDVLRLSG HGTFKETVPV LDERGHMTPT
     EVTRELGVDI ALRWGTGYDT AVRSFVNIIA TPKGGTHVTG FERSVTKTVN EVLRSAKLLR
     VAEDDIVKDD ALEGLTAVVT VRLAEPQFEG QTKEVLGTSA ANRIVANVVA KELKAFLTST
     KRDAKAQARA VLEKAVAAAR TRIAARQHKE AQRRKTALES SSLPAKLADC RSDDVERSEL
     FIVEGDSALG TAKLARNSEF QALLPIRGKI LNVQKSSVSD MLKNAECGSI IQVIGAGSGR
     TFDIDAARYG KIVLLVDADV DGAHIRCLLL TLFQRYMRPM VEAGRVFAAV PPLHRIELVQ
     PRKGQDKYVY TYSDNELRST LLEFQRKGVR FKDSIQRYKG LGEMDADQLA ETTMDPRHRT
     LRRINIGDLE AAEQIFDLLM GNEVAPRKEF ITSSAATLDR SRIDA
//
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