ID NTPA_CAMJE Reviewed; 200 AA. AC Q9PMS6; Q0P8N5; Q9ZF65; DT 30-AUG-2002, integrated into UniProtKB/Swiss-Prot. DT 01-OCT-2000, sequence version 1. DT 04-NOV-2008, entry version 44. DE RecName: Full=Nucleoside-triphosphatase; DE EC=3.6.1.15; DE AltName: Full=Nucleoside triphosphate phosphohydrolase; DE Short=NTPase; GN OrderedLocusNames=Cj1374c; OS Campylobacter jejuni. OC Bacteria; Proteobacteria; Epsilonproteobacteria; Campylobacterales; OC Campylobacteraceae; Campylobacter. OX NCBI_TaxID=197; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RC STRAIN=OH4384 / Serotype O:19; RA Gilbert M., Michniewicz J., Wakarchuk W.W.; RT "Cloning of a multidrug-efflux transporter homolog from Campylobacter RT jejuni."; RL Submitted (DEC-1998) to the EMBL/GenBank/DDBJ databases. RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=NCTC 11168 / Serotype O:2; RX MEDLINE=20150912; PubMed=10688204; DOI=10.1038/35001088; RA Parkhill J., Wren B.W., Mungall K.L., Ketley J.M., Churcher C.M., RA Basham D., Chillingworth T., Davies R.M., Feltwell T., Holroyd S., RA Jagels K., Karlyshev A.V., Moule S., Pallen M.J., Penn C.W., RA Quail M.A., Rajandream M.A., Rutherford K.M., van Vliet A.H.M., RA Whitehead S., Barrell B.G.; RT "The genome sequence of the food-borne pathogen Campylobacter jejuni RT reveals hypervariable sequences."; RL Nature 403:665-668(2000). CC -!- FUNCTION: Hydrolyzes non-standard nucleotides such as XTP and CC dITP/ITP. Might exclude non-standard purines from DNA precursor CC pool, preventing thus incorporation into DNA and avoiding CC chromosomal lesions (By similarity). CC -!- CATALYTIC ACTIVITY: NTP + H(2)O = NDP + phosphate. CC -!- COFACTOR: Divalent cations (By similarity). CC -!- SUBUNIT: Homodimer (By similarity). CC -!- SIMILARITY: Belongs to the HAM1 NTPase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AF113952; AAD10059.1; -; Genomic_DNA. DR EMBL; AL111168; CAL35486.1; -; Genomic_DNA. DR PIR; C81282; C81282. DR HSSP; Q57679; 1B78. DR IntAct; Q9PMS6; -. DR GenomeReviews; AL111168_GR; Cj1374c. DR KEGG; cje:Cj1374c; -. DR BioCyc; CJEJ192222:CJ1374C-MON; -. DR GO; GO:0017111; F:nucleoside-triphosphatase activity; IEA:HAMAP. DR HAMAP; MF_01405; -; 1. DR InterPro; IPR002637; Ham1p_like. DR PANTHER; PTHR11067; Ham1p_like; 1. DR Pfam; PF01725; Ham1p_like; 1. DR TIGRFAMs; TIGR00042; Ham1p_like; 1. PE 3: Inferred from homology; KW Complete proteome; Hydrolase. FT CHAIN 1 200 Nucleoside-triphosphatase. FT /FTId=PRO_0000178145. FT CONFLICT 120 120 Y -> H (in Ref. 1; AAD10059). SQ SEQUENCE 200 AA; 22375 MW; 02F29AF6FEB0FBA1 CRC64; MKIILATSNK HKVLELKEIL KDFEIYAFDE VLMPFEIEEN GKTFKENALI KARAVFNALD EKQKKDFIAL SDDSGICVDV LEGNPGIYSA RFSGKGDDKS NRDKLVNEMI KKGFKQSKAY YVAAIAMVGL MGEFSTHGTM HGKVIDTEKG ENGFGYDSLF IPKGFDKTLA QLSVDEKNNI SHRFKALELA KIILKILNKG //