ID   GPPA_PECCP              Reviewed;         498 AA.
AC   C6DHF6;
DT   22-SEP-2009, integrated into UniProtKB/Swiss-Prot.
DT   01-SEP-2009, sequence version 1.
DT   25-MAY-2022, entry version 64.
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=PC1_4014;
OS   Pectobacterium carotovorum subsp. carotovorum (strain PC1).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Pectobacteriaceae; Pectobacterium.
OX   NCBI_TaxID=561230;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=PC1;
RG   US DOE Joint Genome Institute;
RA   Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Tice H., Bruce D.,
RA   Goodwin L., Pitluck S., Munk A.C., Brettin T., Detter J.C., Han C.,
RA   Tapia R., Larimer F., Land M., Hauser L., Kyrpides N., Mikhailova N.,
RA   Balakrishnan V., Glasner J., Perna N.T.;
RT   "Complete sequence of Pectobacterium carotovorum subsp. carotovorum PC1.";
RL   Submitted (JUL-2009) 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; CP001657; ACT15029.1; -; Genomic_DNA.
DR   RefSeq; WP_015842108.1; NC_012917.1.
DR   AlphaFoldDB; C6DHF6; -.
DR   SMR; C6DHF6; -.
DR   STRING; 561230.PC1_4014; -.
DR   EnsemblBacteria; ACT15029; ACT15029; PC1_4014.
DR   KEGG; pct:PC1_4014; -.
DR   eggNOG; COG0248; Bacteria.
DR   HOGENOM; CLU_025908_4_0_6; -.
DR   OMA; WQICVGA; -.
DR   OrthoDB; 1862004at2; -.
DR   UniPathway; UPA00908; UER00885.
DR   Proteomes; UP000002736; 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   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_1000215466"
SQ   SEQUENCE   498 AA;  55777 MW;  4B1670C7F306E724 CRC64;
     MLSSSSLYAA IDLGSNSFHM LVARETAGSI QTLAKIKRKV RLAAGLDKQN RLSQDAMQRG
     WQCLQLFSER LQDIPQDQVR VVATATLRLA TNADEFLQRA QEILGLPIQV ISGEEEARLI
     YQGVAHTTGG PDARLVVDIG GGSTELATGV GAKTTQLISL PMGCVTWLDR YFSDRNLEAG
     NFERAEQAAR EMLRPVAASL REQGWQICVG ASGTVQALQE IMVAQGMDEY ITLPKLRQLK
     EHAIQCDKLE ELEIEGLTLE RALVFPSGLA ILLAIFQELD IKTMTLAGGA LREGLVYGML
     HLPVDQDIRH RTLATLQRRY LLDVEQAKRV STLADNFLQQ VARDWQLDNR CRELLRSACL
     VHEIGLSIDF RQSPQHAAYL IRHSDLPGFT PAQKKLLATL LQNQINPVDL MPLSQQNALP
     VNQAQRLCRL LRLAIIFASR RRDDTLPAVR LRVEGETLRL ILPAGWLSQH PLRAEMLEQE
     SRWQSYVHWP LMLEETPA