NTPTH_THEMA
ID NTPTH_THEMA Reviewed; 174 AA.
AC Q9WXP3;
DT 11-OCT-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1999, sequence version 1.
DT 03-AUG-2022, entry version 116.
DE RecName: Full=Nucleoside-triphosphatase THEP1 {ECO:0000255|HAMAP-Rule:MF_00796};
DE Short=NTPase THEP1 {ECO:0000255|HAMAP-Rule:MF_00796};
DE EC=3.6.1.15 {ECO:0000255|HAMAP-Rule:MF_00796};
DE AltName: Full=Nucleoside triphosphate phosphohydrolase {ECO:0000255|HAMAP-Rule:MF_00796};
GN OrderedLocusNames=TM_0036;
OS Thermotoga maritima (strain ATCC 43589 / DSM 3109 / JCM 10099 / NBRC 100826
OS / MSB8).
OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga.
OX NCBI_TaxID=243274;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 43589 / DSM 3109 / JCM 10099 / NBRC 100826 / MSB8;
RX PubMed=10360571; DOI=10.1038/20601;
RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., Haft D.H.,
RA Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., McDonald L.A.,
RA Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., Stewart A.M.,
RA Cotton M.D., Pratt M.S., Phillips C.A., Richardson D.L., Heidelberg J.F.,
RA Sutton G.G., Fleischmann R.D., Eisen J.A., White O., Salzberg S.L.,
RA Smith H.O., Venter J.C., Fraser C.M.;
RT "Evidence for lateral gene transfer between Archaea and Bacteria from
RT genome sequence of Thermotoga maritima.";
RL Nature 399:323-329(1999).
CC -!- FUNCTION: Has nucleotide phosphatase activity towards ATP, GTP, CTP,
CC TTP and UTP. May hydrolyze nucleoside diphosphates with lower
CC efficiency. {ECO:0000255|HAMAP-Rule:MF_00796}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a ribonucleoside 5'-triphosphate + H2O = a ribonucleoside 5'-
CC diphosphate + H(+) + phosphate; Xref=Rhea:RHEA:23680,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:43474,
CC ChEBI:CHEBI:57930, ChEBI:CHEBI:61557; EC=3.6.1.15;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_00796};
CC -!- SIMILARITY: Belongs to the THEP1 NTPase family. {ECO:0000255|HAMAP-
CC Rule:MF_00796}.
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DR EMBL; AE000512; AAD35130.1; -; Genomic_DNA.
DR PIR; A72425; A72425.
DR RefSeq; NP_227852.1; NC_000853.1.
DR RefSeq; WP_004082498.1; NZ_CP011107.1.
DR AlphaFoldDB; Q9WXP3; -.
DR SMR; Q9WXP3; -.
DR STRING; 243274.THEMA_04620; -.
DR EnsemblBacteria; AAD35130; AAD35130; TM_0036.
DR KEGG; tma:TM0036; -.
DR eggNOG; COG1618; Bacteria.
DR InParanoid; Q9WXP3; -.
DR OMA; GAMEFKC; -.
DR OrthoDB; 1935037at2; -.
DR Proteomes; UP000008183; Chromosome.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0017111; F:nucleoside-triphosphatase activity; IEA:UniProtKB-UniRule.
DR Gene3D; 3.40.50.300; -; 1.
DR HAMAP; MF_00796; NTPase_1; 1.
DR InterPro; IPR003593; AAA+_ATPase.
DR InterPro; IPR004948; Nuc-triphosphatase_THEP1.
DR InterPro; IPR027417; P-loop_NTPase.
DR PANTHER; PTHR43146; PTHR43146; 1.
DR Pfam; PF03266; NTPase_1; 1.
DR SMART; SM00382; AAA; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
PE 3: Inferred from homology;
KW ATP-binding; Hydrolase; Nucleotide-binding; Reference proteome.
FT CHAIN 1..174
FT /note="Nucleoside-triphosphatase THEP1"
FT /id="PRO_0000146710"
FT BINDING 7..14
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00796"
FT BINDING 94..101
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00796"
SQ SEQUENCE 174 AA; 20034 MW; A739CCA34DF59B52 CRC64;
MKILITGRPG VGKTTLIKKL SRLLQNAGGF YTEEMREGEK RIGFKIITLD GEEGILARTD
LPSPYRVGKY YVNLKDLEEI GVRSLERAFQ EKDLIIVDEI GKMELLSRKF REVVEKIFDS
EKDVIATIKK SSDPFVEKIK NRNDVVIFEL NEKNRNSLLN EILSVLKFNR GEKQ
