ID A0A1H5RG63_9PSEU Unreviewed; 683 AA.
AC A0A1H5RG63;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, 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=SAMN05421837_110246 {ECO:0000313|EMBL:SEF36491.1};
OS Amycolatopsis pretoriensis.
OC Bacteria; Actinomycetota; Actinomycetes; Pseudonocardiales;
OC Pseudonocardiaceae; Amycolatopsis.
OX NCBI_TaxID=218821 {ECO:0000313|EMBL:SEF36491.1, ECO:0000313|Proteomes:UP000198878};
RN [1] {ECO:0000313|EMBL:SEF36491.1, ECO:0000313|Proteomes:UP000198878}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 44654 {ECO:0000313|EMBL:SEF36491.1,
RC ECO:0000313|Proteomes:UP000198878};
RA de Groot N.N.;
RL Submitted (OCT-2016) 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; FNUJ01000010; SEF36491.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1H5RG63; -.
DR STRING; 218821.SAMN05421837_110246; -.
DR Proteomes; UP000198878; 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};
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 459..573
FT /note="Toprim"
FT /evidence="ECO:0000259|PROSITE:PS50880"
SQ SEQUENCE 683 AA; 74575 MW; 575343C3935C62DC CRC64;
MTAETLYGAD DLTHLEGLEA VRKRPGMYIG STDSRGINHL FSEVVDNSTD EGVAGHATKI
VVTLHADGSV QVDDDGRGIP TGTHAKSGLS GVELVLTRLH AGGKFGGSGY KTSGGLHGVG
ASAVNALSHR FDVTVKQEGK VHQMSFKHGI PGTFDAPGPK AKFTRRSGLN LVGKMKRGER
SGTSIRYWYD ARYFESGAAL DVEGVRAKLR NTAFLVPGVT YVLRTAIEDT INEETFHFPH
GLADMVDFLT PSGDKPVCGT LLITGEGTYK ENAADAAGVM QSNVERHAEV EVALRWGTGY
ERTVECFTNT IRNVHGGTHR RGFDRAVTKA LQEAISKTRG LLKPKEDMPT IEDVLEGMTA
VVHVRLPEPQ FTSQTKDELS TAGITRVLQG IVDKHVKAWT EDRKTKSEAK VVLQKVVDAA
RVRLTQKQQK DAARRKTALE GAAMPPKLVD CRTTGVSRSE LFLVEGDSAL GSARMARVSE
YQALLPLRGK ILNVQKASLG DTLKNAEIAS IVQVLGAGTG RTFDLTTMRY GRVILMADAD
VDGSHIRTLL ITLFAKYMRP VIEDGRLYAA MPPLHKLVTK GRNPETHFTY TQQEMETKFA
ELEKAGKNIV TPVPRFKGLG EMDADELWET TMNPATRSVR RITMDDVEAA EGALELLMGE
KVEPRRNWLV ASSDRIDREA IDA
//
