ID   GPPA_YERPS              Reviewed;         498 AA.
AC   Q66G20;
DT   20-DEC-2005, integrated into UniProtKB/Swiss-Prot.
DT   11-OCT-2004, sequence version 1.
DT   27-MAR-2024, entry version 86.
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};
GN   OrderedLocusNames=YPTB0164;
OS   Yersinia pseudotuberculosis serotype I (strain IP32953).
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC   Yersiniaceae; Yersinia.
OX   NCBI_TaxID=273123;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=IP32953;
RX   PubMed=15358858; DOI=10.1073/pnas.0404012101;
RA   Chain P.S.G., Carniel E., Larimer F.W., Lamerdin J., Stoutland P.O.,
RA   Regala W.M., Georgescu A.M., Vergez L.M., Land M.L., Motin V.L.,
RA   Brubaker R.R., Fowler J., Hinnebusch J., Marceau M., Medigue C.,
RA   Simonet M., Chenal-Francisque V., Souza B., Dacheux D., Elliott J.M.,
RA   Derbise A., Hauser L.J., Garcia E.;
RT   "Insights into the evolution of Yersinia pestis through whole-genome
RT   comparison with Yersinia pseudotuberculosis.";
RL   Proc. Natl. Acad. Sci. U.S.A. 101:13826-13831(2004).
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; BX936398; CAH19404.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q66G20; -.
DR   SMR; Q66G20; -.
DR   KEGG; yps:YPTB0164; -.
DR   UniPathway; UPA00908; UER00885.
DR   Proteomes; UP000001011; Chromosome.
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   Gene3D; 3.30.420.40; -; 1.
DR   Gene3D; 3.30.420.150; Exopolyphosphatase. Domain 2; 1.
DR   Gene3D; 1.10.3210.10; Hypothetical protein af1432; 1.
DR   HAMAP; MF_01550; GppA; 1.
DR   InterPro; IPR043129; ATPase_NBD.
DR   InterPro; IPR022371; Exopolyphosphatase.
DR   InterPro; IPR023709; Guo-5TP_3DP_PyrP.
DR   InterPro; IPR048950; Ppx_GppA_C.
DR   InterPro; IPR003695; Ppx_GppA_N.
DR   InterPro; IPR030673; PyroPPase_GppA_Ppx.
DR   NCBIfam; TIGR03706; exo_poly_only; 1.
DR   PANTHER; PTHR30005; EXOPOLYPHOSPHATASE; 1.
DR   PANTHER; PTHR30005:SF0; RETROGRADE REGULATION PROTEIN 2; 1.
DR   Pfam; PF02541; Ppx-GppA; 1.
DR   Pfam; PF21447; Ppx-GppA_III; 1.
DR   PIRSF; PIRSF001267; Pyrophosphatase_GppA_Ppx; 1.
DR   SUPFAM; SSF53067; Actin-like ATPase domain; 2.
DR   SUPFAM; SSF109604; HD-domain/PDEase-like; 1.
PE   3: Inferred from homology;
KW   Hydrolase.
FT   CHAIN           1..498
FT                   /note="Guanosine-5'-triphosphate,3'-diphosphate
FT                   pyrophosphatase"
FT                   /id="PRO_0000194298"
SQ   SEQUENCE   498 AA;  55926 MW;  583A72F958AFFEB5 CRC64;
     MMLSSTSLYA AIDLGSNSFH MLVVREVAGS IQTLARIKRK VRLAAGLDNQ NHLSQEAMER
     GWQCLKLFSE RLQDIPLDQI RVVATATLRL ASNADEFLRT ATEILGCPIQ VISGEEEARL
     IYHGVAHTTG GPEQRLVVDI GGGSTELVTG NGAQANILVS LSMGCVTWLE RYFGDRHLAK
     ENFERAELAA HEMIKPVAQR FREHGWQVCV GASGTVQALQ EIMVAQGMDE LITLAKLQQL
     KQRAIQCGKL EELEIPGLTL ERALVFPSGL SILIAIFQEL SIESMTLAGG ALREGLVYGM
     LHLPVEQDIR RRTLRNLQRR YLLDTEQAKR VSCLADNFFL QVEKEWHLDG RCREFLQNAC
     LIHEIGLSVD FKHAPQHAAY LIRNLDLPGF TPAQKLLLSA LLQNQSDTID LSLLNQQNAL
     PADMAQHLCR LLRLAIIFSS RRRDDTLPAV RLRADNNALY VLVPQGWLEQ HPYRAEALEQ
     ESHWQSYVQW PLLLEELS
//