ID   GPPA_SERP5              Reviewed;         498 AA.
AC   A8G827;
DT   05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT   13-NOV-2007, sequence version 1.
DT   25-MAY-2022, entry version 70.
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=Spro_0157;
OS   Serratia proteamaculans (strain 568).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Yersiniaceae; Serratia.
OX   NCBI_TaxID=399741;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=568;
RG   US DOE Joint Genome Institute;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Glavina del Rio T., Dalin E.,
RA   Tice H., Pitluck S., Chain P., Malfatti S., Shin M., Vergez L., Schmutz J.,
RA   Larimer F., Land M., Hauser L., Kyrpides N., Kim E., Taghavi S., Newman L.,
RA   Vangronsveld J., van der Lelie D., Richardson P.;
RT   "Complete sequence of chromosome of Serratia proteamaculans 568.";
RL   Submitted (SEP-2007) to the EMBL/GenBank/DDBJ databases.
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; CP000826; ABV39267.1; -; Genomic_DNA.
DR   RefSeq; WP_012004629.1; NC_009832.1.
DR   AlphaFoldDB; A8G827; -.
DR   SMR; A8G827; -.
DR   STRING; 399741.Spro_0157; -.
DR   EnsemblBacteria; ABV39267; ABV39267; Spro_0157.
DR   KEGG; spe:Spro_0157; -.
DR   eggNOG; COG0248; Bacteria.
DR   HOGENOM; CLU_025908_4_0_6; -.
DR   OMA; WQICVGA; -.
DR   OrthoDB; 1862004at2; -.
DR   UniPathway; UPA00908; UER00885.
DR   GO; GO:0004309; F:exopolyphosphatase activity; IEA:InterPro.
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; IPR022371; Exopolyphosphatase.
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.
DR   TIGRFAMs; TIGR03706; exo_poly_only; 1.
PE   3: Inferred from homology;
KW   Hydrolase.
FT   CHAIN           1..498
FT                   /note="Guanosine-5'-triphosphate,3'-diphosphate
FT                   pyrophosphatase"
FT                   /id="PRO_1000068824"
SQ   SEQUENCE   498 AA;  55773 MW;  0AD1CDF3CD2DE489 CRC64;
     MLSSSALYAA IDLGSNSFHM LVVREVAGSI QTLARIKRKV RLAAGLDQNN LLSHEAMQRG
     WQCLKLFSER LQDIPRAQIR VVATATLRLA SNADEFLQTA EQILGCPIQV ISGEEEARLI
     YHGVAHTTGG PDQRLVVDIG GGSTELVTGT GAQAAQLYSL SMGCVTWLER FFSDRNLGQE
     NFERAEQAAR EMVRPIAPQL RQHGWQVCVG ASGTVQALQE IMVAQGMDER ITLSKLRQLK
     QRAIQCGKLE ELEIEGLTLE RALVFPSGLS ILLAIFQELG IESMMLAGGA LREGLVYGML
     HLPVEQDIRS RTIRNLQRRY LLDTEQAERV SQLAANFSQQ VSNEWQLDAR CRELLHSACL
     IHEIGLSVDF KQAPQHAAYL IRHLDLPGFT PAQKKLLATL LQNQSNTIDL PLLSQQNALP
     PRTAQRLCRI LRLAIIFASR RRDDTLPAVR LRANNDDELT VILPPGWLEQ HPLRAEALDQ
     ESHWQSYVHW PLILEEQR