ID   GPPA_ERWT9              Reviewed;         494 AA.
AC   B2VG72;
DT   14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT   01-JUL-2008, sequence version 1.
DT   25-MAY-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=ETA_01930;
OS   Erwinia tasmaniensis (strain DSM 17950 / CFBP 7177 / CIP 109463 / NCPPB
OS   4357 / Et1/99).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Erwiniaceae; Erwinia.
OX   NCBI_TaxID=465817;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 17950 / CFBP 7177 / CIP 109463 / NCPPB 4357 / Et1/99;
RX   PubMed=18462403; DOI=10.1111/j.1462-2920.2008.01639.x;
RA   Kube M., Migdoll A.M., Mueller I., Kuhl H., Beck A., Reinhardt R.,
RA   Geider K.;
RT   "The genome of Erwinia tasmaniensis strain Et1/99, a non-pathogenic
RT   bacterium in the genus Erwinia.";
RL   Environ. Microbiol. 10:2211-2222(2008).
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; CU468135; CAO95239.1; -; Genomic_DNA.
DR   RefSeq; WP_012439959.1; NC_010694.1.
DR   AlphaFoldDB; B2VG72; -.
DR   SMR; B2VG72; -.
DR   STRING; 465817.ETA_01930; -.
DR   EnsemblBacteria; CAO95239; CAO95239; ETA_01930.
DR   KEGG; eta:ETA_01930; -.
DR   eggNOG; COG0248; Bacteria.
DR   HOGENOM; CLU_025908_4_0_6; -.
DR   OMA; WQICVGA; -.
DR   OrthoDB; 1862004at2; -.
DR   UniPathway; UPA00908; UER00885.
DR   Proteomes; UP000001726; 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; Reference proteome.
FT   CHAIN           1..494
FT                   /note="Guanosine-5'-triphosphate,3'-diphosphate
FT                   pyrophosphatase"
FT                   /id="PRO_1000146872"
SQ   SEQUENCE   494 AA;  54728 MW;  164A4574EE6E56D0 CRC64;
     MRSASSLYAA IDLGSNSFHM LVVREVAGSI QTIARIKRKV RLAAGLDADN NLSAEAMDRG
     WQCLRLFSEQ LQDIPPEQIR VVATATLRIA ANAGSFLAQA QKLLGCPVNV ISGEEEARLI
     YQGVSHTTGG SDKRLVVDIG GGSTELVTGR GSQPTTLYSL SMGCVTWLER YFSDRQLGKV
     NFEQAEQAAR AMIRPIADSL KAQGWQVCVG ASGTVQALQE IMMAQGMDER ITLNKLQQLK
     QRAIECGKLE ELEIEGLTLE RALVFPSGLS ILIAIFSELN ISSMTLAGGA LREGLLYGML
     PLPVDRDIRS RTLHDVQRRF SVDPEQAERV RQLADSFARQ VSLQWKLDDR SRELLGSACL
     LHEIGLSVDF RQAPQHAAYL VRYLDLPGFT PAQKKLLATL LQNQVGNIDL PLLSQQNALL
     PRIAERLSRL LRLAIIFASR RRDDRLPAVR LQADDDNLTV TLPSGWLEAH PLRAELLEQE
     ARWQGYVHWP LIIA