ID   NTPA_BORBU              Reviewed;         201 AA.
AC   O51263;
DT   30-AUG-2002, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-1998, sequence version 1.
DT   22-JUL-2008, entry version 50.
DE   RecName: Full=Nucleoside-triphosphatase;
DE            EC=3.6.1.15;
DE   AltName: Full=Nucleoside triphosphate phosphohydrolase;
DE            Short=NTPase;
GN   OrderedLocusNames=BB_0247;
OS   Borrelia burgdorferi (Lyme disease spirochete).
OC   Bacteria; Spirochaetes; Spirochaetales; Spirochaetaceae; Borrelia;
OC   Borrelia burgdorferi group.
OX   NCBI_TaxID=139;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 35210 / B31 / CIP 102532 / DSM 4680;
RX   MEDLINE=98065943; PubMed=9403685; DOI=10.1038/37551;
RA   Fraser C.M., Casjens S., Huang W.M., Sutton G.G., Clayton R.A.,
RA   Lathigra R., White O., Ketchum K.A., Dodson R.J., Hickey E.K.,
RA   Gwinn M.L., Dougherty B.A., Tomb J.-F., Fleischmann R.D.,
RA   Richardson D.L., Peterson J.D., Kerlavage A.R., Quackenbush J.,
RA   Salzberg S.L., Hanson M., van Vugt R., Palmer N., Adams M.D.,
RA   Gocayne J.D., Weidman J.F., Utterback T.R., Watthey L., McDonald L.A.,
RA   Artiach P., Bowman C., Garland S.A., Fujii C., Cotton M.D., Horst K.,
RA   Roberts K.M., Hatch B., Smith H.O., Venter J.C.;
RT   "Genomic sequence of a Lyme disease spirochaete, Borrelia
RT   burgdorferi.";
RL   Nature 390:580-586(1997).
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; AE000783; AAB91499.1; -; Genomic_DNA.
DR   PIR; G70130; G70130.
DR   RefSeq; NP_212381.1; -.
DR   HSSP; Q57679; 1B78.
DR   GeneID; 1195084; -.
DR   GenomeReviews; AE000783_GR; BB_0247.
DR   KEGG; bbu:BB0247; -.
DR   NMPDR; fig|224326.1.peg.631; -.
DR   TIGR; BB_0247; -.
DR   HOGENOM; O51263; -.
DR   BioCyc; BBUR224326:BB_0247-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    201       Nucleoside-triphosphatase.
FT                                /FTId=PRO_0000178136.
SQ   SEQUENCE   201 AA;  23138 MW;  199E43E0704B4575 CRC64;
     MKTLFFATTN ENKINEVKNI LDIPNLNLIV PQNFNIKETG KTFKENSLLK AKALFEILNN
     NQNVFGEDSG LCIEALNLEP GIYSKRYDTY KLCKKLSTNE KNQLILDLMK NEKNRKAYFI
     CNISYISKNG QILNFEGIIK GKIALSLNDK KNYGFGYDSI FLTKNNKKLS DLTLEEKNKI
     SHRGIAFLKF KKFLLKSLFN S
//