ID NTPA_BACHK Reviewed; 205 AA. AC Q6HD43; DT 26-APR-2005, integrated into UniProtKB/Swiss-Prot. DT 19-JUL-2004, sequence version 1. DT 16-JUN-2009, entry version 29. DE RecName: Full=Nucleoside-triphosphatase; DE EC=3.6.1.15; DE AltName: Full=Nucleoside triphosphate phosphohydrolase; DE Short=NTPase; GN OrderedLocusNames=BT9727_4217; OS Bacillus thuringiensis subsp. konkukian. OC Bacteria; Firmicutes; Bacillales; Bacillaceae; Bacillus; OC Bacillus cereus group. OX NCBI_TaxID=180856; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=97-27; RX PubMed=16621833; DOI=10.1128/JB.188.9.3382-3390.2006; RA Han C.S., Xie G., Challacombe J.F., Altherr M.R., Bhotika S.S., RA Bruce D., Campbell C.S., Campbell M.L., Chen J., Chertkov O., RA Cleland C., Dimitrijevic M., Doggett N.A., Fawcett J.J., Glavina T., RA Goodwin L.A., Hill K.K., Hitchcock P., Jackson P.J., Keim P., RA Kewalramani A.R., Longmire J., Lucas S., Malfatti S., McMurry K., RA Meincke L.J., Misra M., Moseman B.L., Mundt M., Munk A.C., RA Okinaka R.T., Parson-Quintana B., Reilly L.P., Richardson P., RA Robinson D.L., Rubin E., Saunders E., Tapia R., Tesmer J.G., RA Thayer N., Thompson L.S., Tice H., Ticknor L.O., Wills P.L., RA Brettin T.S., Gilna P.; RT "Pathogenomic sequence analysis of Bacillus cereus and Bacillus RT thuringiensis isolates closely related to Bacillus anthracis."; RL J. Bacteriol. 188:3382-3390(2006). 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; AE017355; AAT63711.1; -; Genomic_DNA. DR RefSeq; YP_038533.1; -. DR GeneID; 2855522; -. DR GenomeReviews; AE017355_GR; BT9727_4217. DR KEGG; btk:BT9727_4217; -. DR HOGENOM; Q6HD43; -. DR OMA; Q6HD43; NACLKAS. DR BioCyc; BTHU281309:BT9727_4217-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 1 205 Nucleoside-triphosphatase. FT /FTId=PRO_0000178126. SQ SEQUENCE 205 AA; 23223 MW; 09C1E0693E774682 CRC64; MENMKQVVVA TKNMGKVREF AELFERFDLE VKSLHDFPHI EEVEETGETF EENAILKADS LSRQLNAIVI ADDSGLIVDA LNGKPGVYSA RFAGEPKDDQ ANIDKVLQEL NEVAFEKRKA RFYCALAVAF PEGDKKPVIV NGTCEGFILE QRRGENGFGY DPIFYVEEYK KAMAELSSDE KNAISHRGRA LRKLEEKIPE WFLGE //