ID   GPPA_CROS8              Reviewed;         494 AA.
AC   A7MQI3;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   02-OCT-2007, sequence version 1.
DT   03-AUG-2022, entry version 72.
DE   RecName: Full=Guanosine-5'-triphosphate,3'-diphosphate pyrophosphatase {ECO:0000255|HAMAP-Rule:MF_01550};
DE            EC=3.6.1.40 {ECO:0000255|HAMAP-Rule:MF_01550};
DE   AltName: Full=Guanosine pentaphosphate phosphohydrolase {ECO:0000255|HAMAP-Rule:MF_01550};
DE   AltName: Full=pppGpp-5'-phosphohydrolase {ECO:0000255|HAMAP-Rule:MF_01550};
GN   Name=gppA {ECO:0000255|HAMAP-Rule:MF_01550}; OrderedLocusNames=ESA_03778;
OS   Cronobacter sakazakii (strain ATCC BAA-894) (Enterobacter sakazakii).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Cronobacter.
OX   NCBI_TaxID=290339;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-894;
RX   PubMed=20221447; DOI=10.1371/journal.pone.0009556;
RA   Kucerova E., Clifton S.W., Xia X.Q., Long F., Porwollik S., Fulton L.,
RA   Fronick C., Minx P., Kyung K., Warren W., Fulton R., Feng D., Wollam A.,
RA   Shah N., Bhonagiri V., Nash W.E., Hallsworth-Pepin K., Wilson R.K.,
RA   McClelland M., Forsythe S.J.;
RT   "Genome sequence of Cronobacter sakazakii BAA-894 and comparative genomic
RT   hybridization analysis with other Cronobacter species.";
RL   PLoS ONE 5:E9556-E9556(2010).
CC   -!- FUNCTION: Catalyzes the conversion of pppGpp to ppGpp. Guanosine
CC       pentaphosphate (pppGpp) is a cytoplasmic signaling molecule which
CC       together with ppGpp controls the 'stringent response', an adaptive
CC       process that allows bacteria to respond to amino acid starvation,
CC       resulting in the coordinated regulation of numerous cellular
CC       activities. {ECO:0000255|HAMAP-Rule:MF_01550}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=guanosine 3'-diphosphate 5'-triphosphate + H2O = guanosine
CC         3',5'-bis(diphosphate) + H(+) + phosphate; Xref=Rhea:RHEA:13073,
CC         ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:43474,
CC         ChEBI:CHEBI:77828, ChEBI:CHEBI:142410; EC=3.6.1.40;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_01550};
CC   -!- PATHWAY: Purine metabolism; ppGpp biosynthesis; ppGpp from GTP: step
CC       2/2. {ECO:0000255|HAMAP-Rule:MF_01550}.
CC   -!- SIMILARITY: Belongs to the GppA/Ppx family. GppA subfamily.
CC       {ECO:0000255|HAMAP-Rule:MF_01550}.
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DR   EMBL; CP000783; ABU78970.1; -; Genomic_DNA.
DR   RefSeq; WP_012126057.1; NC_009778.1.
DR   AlphaFoldDB; A7MQI3; -.
DR   SMR; A7MQI3; -.
DR   EnsemblBacteria; ABU78970; ABU78970; ESA_03778.
DR   KEGG; esa:ESA_03778; -.
DR   PATRIC; fig|290339.8.peg.3359; -.
DR   HOGENOM; CLU_025908_4_0_6; -.
DR   OMA; WQICVGA; -.
DR   OrthoDB; 1862004at2; -.
DR   UniPathway; UPA00908; UER00885.
DR   Proteomes; UP000000260; Chromosome.
DR   GO; GO:0008894; F:guanosine-5'-triphosphate,3'-diphosphate diphosphatase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0015974; P:guanosine pentaphosphate catabolic process; IEA:UniProtKB-UniRule.
DR   GO; GO:0015970; P:guanosine tetraphosphate biosynthetic process; IEA:UniProtKB-UniPathway.
DR   HAMAP; MF_01550; GppA; 1.
DR   InterPro; IPR043129; ATPase_NBD.
DR   InterPro; IPR023709; Guo-5TP_3DP_PyrP.
DR   InterPro; IPR003695; Ppx_GppA.
DR   InterPro; IPR030673; PyroPPase_GppA_Ppx.
DR   Pfam; PF02541; Ppx-GppA; 1.
DR   PIRSF; PIRSF001267; Pyrophosphatase_GppA_Ppx; 1.
DR   SUPFAM; SSF53067; SSF53067; 2.
PE   3: Inferred from homology;
KW   Hydrolase.
FT   CHAIN           1..494
FT                   /note="Guanosine-5'-triphosphate,3'-diphosphate
FT                   pyrophosphatase"
FT                   /id="PRO_0000314493"
SQ   SEQUENCE   494 AA;  54237 MW;  93EB6216DE0729E1 CRC64;
     MPGTPSLYAA IDLGSNSFHM LVVREVAGSI QTLTRVKRKV RLAAGLGADN ALSADAMERG
     WQCLRLFAER LQDIPPSQIR VVATATLRLA TNADVFVARA QEILGCPVQV IAGEEEARLI
     YQGVAHTTGG ADRRLVVDIG GASTELVTGT GARATSLFSL PMGCVTFLER FFTDRSLTQE
     HFASAEQAAR DILQPVIAQL RGQGWKICVG ASGTVQALQE IMMAQGMDER ITLAKLQQLK
     ARAIHCGRLE ELEIEGLTLE RALVFPSGLA ILIAIFSELE IECMTLAGGA LREGLVYGML
     HLAVDQDIRN RTLKNIQRRF MVDIAQAGRV AQLAERFAVS VEREWALDDL SRALLHSASL
     LHEVGLAVDF KRAPQHAAYL VNNLDLPGFT PAQKKLLATL LLNQTGTVDL PALQQQNAVP
     LRVAERLCRL LRLAIIFASR RRDDMLPDVT LTAHDDTLTA SLPQDWLSVH PLGAEMLEQE
     QLWQSYVHWQ LDVK