ID   GPPA_ECOUT              Reviewed;         494 AA.
AC   Q1R4G0;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   15-JAN-2008, sequence version 2.
DT   22-JUL-2008, entry version 15.
DE   RecName: Full=Guanosine-5'-triphosphate,3'-diphosphate pyrophosphatase;
DE            EC=3.6.1.40;
DE   AltName: Full=Guanosine pentaphosphate phosphohydrolase;
DE   AltName: Full=pppGpp-5'-phosphohydrolase;
GN   Name=gppA; OrderedLocusNames=UTI89_C4333;
OS   Escherichia coli (strain UTI89 / UPEC).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=364106;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=16585510; DOI=10.1073/pnas.0600938103;
RA   Chen S.L., Hung C.-S., Xu J., Reigstad C.S., Magrini V., Sabo A.,
RA   Blasiar D., Bieri T., Meyer R.R., Ozersky P., Armstrong J.R.,
RA   Fulton R.S., Latreille J.P., Spieth J., Hooton T.M., Mardis E.R.,
RA   Hultgren S.J., Gordon J.I.;
RT   "Identification of genes subject to positive selection in
RT   uropathogenic strains of Escherichia coli: a comparative genomics
RT   approach.";
RL   Proc. Natl. Acad. Sci. U.S.A. 103:5977-5982(2006).
CC   -!- FUNCTION: Conversion of pppGpp to ppGpp. Guanosine pentaphosphate
CC       (pppGpp) is a cytoplasmic signaling molecule which together with
CC       ppGpp controls the "stringent response", an adaptive process that
CC       allows bacteria to respond to amino acid starvation, resulting in
CC       the coordinated regulation of numerous cellular activities (By
CC       similarity).
CC   -!- CATALYTIC ACTIVITY: Guanosine 5'-triphosphate,3'-diphosphate +
CC       H(2)O = guanosine 5'-diphosphate,3'-diphosphate + phosphate.
CC   -!- PATHWAY: Purine metabolism; ppGpp biosynthesis; ppGpp from GTP:
CC       step 1/2.
CC   -!- SIMILARITY: Belongs to the gppA/ppx family. GppA subfamily.
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DR   EMBL; CP000243; ABE09754.1; ALT_INIT; Genomic_DNA.
DR   RefSeq; YP_543285.1; -.
DR   GeneID; 3993312; -.
DR   GenomeReviews; CP000243_GR; UTI89_C4333.
DR   KEGG; eci:UTI89_C4333; -.
DR   HOGENOM; Q1R4G0; -.
DR   BioCyc; ECOL364106:UTI89_C4333-MON; -.
DR   GO; GO:0008894; F:guanosine-5'-triphosphate,3'-diphosphate di...; IEA:HAMAP.
DR   HAMAP; MF_01550; -; 1.
DR   InterPro; IPR003695; Ppx_GppA.
DR   Pfam; PF02541; Ppx-GppA; 1.
PE   3: Inferred from homology;
KW   Complete proteome; Hydrolase.
FT   CHAIN         1    494       Guanosine-5'-triphosphate,3'-diphosphate
FT                                pyrophosphatase.
FT                                /FTId=PRO_0000314494.
SQ   SEQUENCE   494 AA;  54945 MW;  9F175CC8F942B980 CRC64;
     MGSTSSLYAA IDLGSNSFHM LVVREVAGSI QTLTRIKRKV RLAAGLNSEN ALSNEAMERG
     WQCLRLFAER LQDIPPSQIR VVATATLRLA VNAGDFIAKA QEILGCPVQV ISGEEEARLI
     YQGVAHTTGG ADQRLVVDIG GASTELVTGT GAQTTSLFSL SMGCVTWLER YFADRNLGQE
     NFDAAEKAAR EVLRPVADEL RYHGWKVCVG ASGTVQALQE IMMAQGMDER ITLEKLQQLK
     QRAIHCGRLE ELEIDGLTLE RALVFPSGLA ILIAIFTELN IQCMTLAGGA LREGLVYGML
     HLTVEQDIRS RTLRNIQRRF MIDIDQAQRV AKVAANFFDQ VENEWHLEAI SRDLLISACQ
     LHEIGLSVDF KQAPQHAAYL VRNLDLPGFT PAQKKLLATL LLNQTNPVDL SSLHQQNAVP
     PRVAEQLCRL LRLAIIFASR RRDDLVPEMT LQANHELLTL TLPQGWLTQH PLGKEIIDQE
     SQWQSYVHWP LEVH
//