ID   PPNK2_BACHK             Reviewed;         267 AA.
AC   Q6HCN5;
DT   04-APR-2006, integrated into UniProtKB/Swiss-Prot.
DT   19-JUL-2004, sequence version 1.
DT   16-JUN-2009, entry version 30.
DE   RecName: Full=Probable inorganic polyphosphate/ATP-NAD kinase 2;
DE            Short=Poly(P)/ATP NAD kinase 2;
DE            EC=2.7.1.23;
GN   Name=ppnK2; OrderedLocusNames=BT9727_4376;
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: Catalyzes the phosphorylation of NAD to NADP. Utilizes
CC       ATP and other nucleoside triphosphates as well as inorganic
CC       polyphosphate as a source of phosphorus (By similarity).
CC   -!- CATALYTIC ACTIVITY: ATP + NAD(+) = ADP + NADP(+).
CC   -!- COFACTOR: Divalent metal ions (By similarity).
CC   -!- SUBCELLULAR LOCATION: Cytoplasm (By similarity).
CC   -!- SIMILARITY: Belongs to the NAD kinase family.
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DR   EMBL; AE017355; AAT63589.1; -; Genomic_DNA.
DR   RefSeq; YP_038691.1; -.
DR   GeneID; 2856194; -.
DR   GenomeReviews; AE017355_GR; BT9727_4376.
DR   KEGG; btk:BT9727_4376; -.
DR   HOGENOM; Q6HCN5; -.
DR   OMA; Q6HCN5; NEVSIRS.
DR   BioCyc; BTHU281309:BT9727_4376-MON; -.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0046872; F:metal ion binding; IEA:HAMAP.
DR   GO; GO:0003951; F:NAD+ kinase activity; IEA:HAMAP.
DR   GO; GO:0008152; P:metabolic process; IEA:InterPro.
DR   HAMAP; MF_00361; -; 1.
DR   InterPro; IPR017437; ATP-NAD_kinase_PpnK-typ_all-b.
DR   InterPro; IPR002504; ATP_NADK.
DR   Gene3D; G3DSA:2.60.200.30; ATP-NAD_kinase_PpnK-typ; 1.
DR   PANTHER; PTHR20275; ATP_NADK; 1.
DR   Pfam; PF01513; NAD_kinase; 1.
PE   3: Inferred from homology;
KW   ATP-binding; Complete proteome; Cytoplasm; Kinase; NAD; NADP;
KW   Nucleotide-binding; Transferase.
FT   CHAIN         1    267       Probable inorganic polyphosphate/ATP-NAD
FT                                kinase 2.
FT                                /FTId=PRO_0000229607.
SQ   SEQUENCE   267 AA;  30365 MW;  22C017138F19C795 CRC64;
     MADRRNLFFF YGDDKAKLVE KMKPIYRILE ENGFTILDHP KNANAIVSVG DDATFLQAVR
     KTGFREDCLY AGISTKDEIS FYCDFHIDHV DTALQEITKN EIEVRKYPTI EVDVDGSTSF
     HCLNEFSLRS SIIKTFVVDV HVDDLYFETF RGDGLVVSTP TGSTAYNKSL RGAVVDPLIP
     CFQVSELASL NNNTYRTLGS PFILNHERTL TLKLRPDGND YPVIGMDNEA LSIKQVEKAV
     VRLSDKQIKT VKLKNNSFWE KVQRTFL
//