ID A0A1T4SMH5_9ACTN Unreviewed; 701 AA.
AC A0A1T4SMH5;
DT 10-MAY-2017, integrated into UniProtKB/TrEMBL.
DT 10-MAY-2017, sequence version 1.
DT 27-MAR-2024, entry version 31.
DE RecName: Full=DNA topoisomerase (ATP-hydrolyzing) {ECO:0000256|ARBA:ARBA00012895};
DE EC=5.6.2.2 {ECO:0000256|ARBA:ARBA00012895};
GN ORFNames=SAMN02745673_03712 {ECO:0000313|EMBL:SKA29429.1};
OS Marinactinospora thermotolerans DSM 45154.
OC Bacteria; Actinomycetota; Actinomycetes; Streptosporangiales;
OC Nocardiopsaceae; Marinactinospora.
OX NCBI_TaxID=1122192 {ECO:0000313|EMBL:SKA29429.1, ECO:0000313|Proteomes:UP000190637};
RN [1] {ECO:0000313|EMBL:SKA29429.1, ECO:0000313|Proteomes:UP000190637}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 45154 {ECO:0000313|EMBL:SKA29429.1,
RC ECO:0000313|Proteomes:UP000190637};
RA Peterson S.W.;
RL Submitted (FEB-2017) 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; FUWS01000010; SKA29429.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1T4SMH5; -.
DR STRING; 1122192.SAMN02745673_03712; -.
DR OrthoDB; 9802808at2; -.
DR Proteomes; UP000190637; 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:SKA29429.1};
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:UP000190637};
KW Topoisomerase {ECO:0000256|ARBA:ARBA00023029}.
FT DOMAIN 469..583
FT /note="Toprim"
FT /evidence="ECO:0000259|PROSITE:PS50880"
SQ SEQUENCE 701 AA; 77213 MW; 21435AF6ABB0225D CRC64;
MTALTAAVHD PEDYSARHLS VLEGLEAVRK RPGMYIGSTD SRGLTHCMWE IIDNAVDEAL
GGFCTRIDVV LHADGSVEVR DNGRGIPVDV EPKSGLSGVE LVMTKLHAGG KFGTGSYTAS
GGLHGVGASV VNALSARLDV EVDREGHTNA ISFRRGIPGR FDAAGPDAGF TPESGLVRTR
RVARKVTGTR VRFWADRQIF LKDADIAREA LLERARQTAF LIPGLTISVR DERTEGEEPY
EEEFRFDGGI GEFCTFLAPD EPVSDVLRIQ GTGQFKETVP VLDENGHMTP TEVERQLEVD
VALRWGTGYD TTVRSFVNVI ATPKGGTHLA GFDRALVRVI NDQLRSTKLL KASDDPVVKE
DVLEGLTAVV TVRLPEPQFE GQTKEILGTS AASRIVSQVV GKELRHFLTS TKRAEKQQAR
AVLEKVANAA KARLAARQQR ETQRRKNALE NSALPAKLVD CRSEGLERSE LFIVEGDSAL
GTAKLARDSE FQALLPIRGK ILNVQKSSVA DMLKNAECAA IIQVIGAGSG RTFDVEAARY
GRVILMADAD VDGAHIRCLL LTLFYRYMRP MLEAGRVYAA VPPLHRIELT NVRKKRGARP
EDKYIYTYSD AELHRTLAEL EKKGKTWKEP VQRYKGLGEM DADQLAETTM DPRYRTLRRI
RVEQAEEAAA VFSLLMGNEV APRREFIAKG ARELDLSRID A
//
