GPPA_ECOLI
ID GPPA_ECOLI Reviewed; 494 AA.
AC P25552; Q2M887; Q6BF04;
DT 01-MAY-1992, integrated into UniProtKB/Swiss-Prot.
DT 11-OCT-2004, sequence version 3.
DT 03-AUG-2022, entry version 146.
DE RecName: Full=Guanosine-5'-triphosphate,3'-diphosphate pyrophosphatase {ECO:0000255|HAMAP-Rule:MF_01550, ECO:0000305};
DE EC=3.6.1.40 {ECO:0000255|HAMAP-Rule:MF_01550, ECO:0000269|PubMed:6130093, ECO:0000269|PubMed:8394006};
DE AltName: Full=Guanosine pentaphosphate phosphohydrolase {ECO:0000255|HAMAP-Rule:MF_01550, ECO:0000303|PubMed:8394006};
DE AltName: Full=pppGpp-5'-phosphohydrolase {ECO:0000255|HAMAP-Rule:MF_01550};
GN Name=gppA {ECO:0000255|HAMAP-Rule:MF_01550};
GN Synonyms=gpp {ECO:0000303|PubMed:6130093}; OrderedLocusNames=b3779, JW5603;
OS Escherichia coli (strain K12).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=83333;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=K12;
RX PubMed=1931833;
RA Kalman M., Murphy H., Cashel M.;
RT "rhlB, a new Escherichia coli K-12 gene with an RNA helicase-like protein
RT sequence motif, one of at least five such possible genes in a prokaryote.";
RL New Biol. 3:886-895(1991).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=1379743; DOI=10.1126/science.1379743;
RA Daniels D.L., Plunkett G. III, Burland V.D., Blattner F.R.;
RT "Analysis of the Escherichia coli genome: DNA sequence of the region from
RT 84.5 to 86.5 minutes.";
RL Science 257:771-778(1992).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=9278503; DOI=10.1126/science.277.5331.1453;
RA Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V.,
RA Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F.,
RA Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B.,
RA Shao Y.;
RT "The complete genome sequence of Escherichia coli K-12.";
RL Science 277:1453-1462(1997).
RN [4]
RP SEQUENCE REVISION TO 86 AND 423.
RX PubMed=16397293; DOI=10.1093/nar/gkj405;
RA Riley M., Abe T., Arnaud M.B., Berlyn M.K.B., Blattner F.R.,
RA Chaudhuri R.R., Glasner J.D., Horiuchi T., Keseler I.M., Kosuge T.,
RA Mori H., Perna N.T., Plunkett G. III, Rudd K.E., Serres M.H., Thomas G.H.,
RA Thomson N.R., Wishart D., Wanner B.L.;
RT "Escherichia coli K-12: a cooperatively developed annotation snapshot
RT -- 2005.";
RL Nucleic Acids Res. 34:1-9(2006).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=16738553; DOI=10.1038/msb4100049;
RA Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S.,
RA Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.;
RT "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655
RT and W3110.";
RL Mol. Syst. Biol. 2:E1-E5(2006).
RN [6]
RP FUNCTION, CATALYTIC ACTIVITY, ACTIVITY REGULATION, BIOPHYSICOCHEMICAL
RP PROPERTIES, AND PATHWAY.
RX PubMed=6130093; DOI=10.1016/s0021-9258(18)33039-4;
RA Hara A., Sy J.;
RT "Guanosine 5'-triphosphate, 3'-diphosphate 5'-phosphohydrolase.
RT Purification and substrate specificity.";
RL J. Biol. Chem. 258:1678-1683(1983).
RN [7]
RP SIMILARITY TO PPX.
RX PubMed=8212131; DOI=10.1016/0968-0004(93)90172-j;
RA Reizer J., Reizer A., Saier M.H. Jr., Bork B., Sander C.;
RT "Exopolyphosphate phosphatase and guanosine pentaphosphate phosphatase
RT belong to the sugar kinase/actin/hsp 70 superfamily.";
RL Trends Biochem. Sci. 18:247-248(1993).
RN [8]
RP FUNCTION, CATALYTIC ACTIVITY, ACTIVITY REGULATION, AND BIOPHYSICOCHEMICAL
RP PROPERTIES.
RX PubMed=8394006; DOI=10.1073/pnas.90.15.7029;
RA Keasling J.D., Bertsch L., Kornberg A.;
RT "Guanosine pentaphosphate phosphohydrolase of Escherichia coli is a long-
RT chain exopolyphosphatase.";
RL Proc. Natl. Acad. Sci. U.S.A. 90:7029-7033(1993).
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 activities
CC (PubMed:6130093, PubMed:8394006). In vitro, can hydrolyze pppGp
CC (PubMed:6130093). Also has exopolyphosphatase activity, catalyzing the
CC release of orthophosphate by processive hydrolysis of the
CC phosphoanyhydride bonds of polyphosphate chains (1000 residues)
CC (PubMed:8394006). {ECO:0000269|PubMed:6130093,
CC ECO:0000269|PubMed:8394006}.
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 ECO:0000269|PubMed:6130093, ECO:0000269|PubMed:8394006};
CC -!- ACTIVITY REGULATION: Requires Mg(2+) and a monovalent cation, with
CC NH(4) preferred over K(+) (PubMed:6130093). KCl, NaCl and NaF salts
CC inhibit the exopolyphosphatase activity (PubMed:8394006).
CC {ECO:0000269|PubMed:6130093, ECO:0000269|PubMed:8394006}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=0.11 mM for pppGpp {ECO:0000269|PubMed:6130093};
CC KM=0.13 mM for pppGpp {ECO:0000269|PubMed:8394006};
CC KM=0.13 mM for pppGp {ECO:0000269|PubMed:6130093};
CC KM=0.5 nM for long-chain poly(P) {ECO:0000269|PubMed:8394006};
CC Note=kcat is 0.023 sec(-1) for pppGpp hydrolase activity. kcat is 1.1
CC sec(-1) for the exopolyphosphatase activity.
CC {ECO:0000269|PubMed:8394006};
CC pH dependence:
CC Optimum pH is 9. {ECO:0000269|PubMed:6130093};
CC -!- PATHWAY: Purine metabolism; ppGpp biosynthesis; ppGpp from GTP: step
CC 2/2. {ECO:0000255|HAMAP-Rule:MF_01550, ECO:0000305|PubMed:6130093}.
CC -!- SIMILARITY: Belongs to the GppA/Ppx family. GppA subfamily.
CC {ECO:0000255|HAMAP-Rule:MF_01550, ECO:0000305}.
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DR EMBL; M83316; AAB59049.1; -; Genomic_DNA.
DR EMBL; M87049; AAA67580.1; -; Genomic_DNA.
DR EMBL; U00096; AAT48210.1; -; Genomic_DNA.
DR EMBL; AP009048; BAE77519.1; -; Genomic_DNA.
DR PIR; A48285; A48285.
DR RefSeq; WP_001295254.1; NZ_SSZK01000025.1.
DR RefSeq; YP_026252.1; NC_000913.3.
DR PDB; 6PBZ; X-ray; 2.48 A; A/B/C/D=1-494.
DR PDBsum; 6PBZ; -.
DR AlphaFoldDB; P25552; -.
DR SMR; P25552; -.
DR BioGRID; 4263319; 6.
DR STRING; 511145.b3779; -.
DR jPOST; P25552; -.
DR PaxDb; P25552; -.
DR PRIDE; P25552; -.
DR EnsemblBacteria; AAT48210; AAT48210; b3779.
DR EnsemblBacteria; BAE77519; BAE77519; BAE77519.
DR GeneID; 948291; -.
DR KEGG; ecj:JW5603; -.
DR KEGG; eco:b3779; -.
DR PATRIC; fig|511145.12.peg.3894; -.
DR EchoBASE; EB0408; -.
DR eggNOG; COG0248; Bacteria.
DR HOGENOM; CLU_025908_4_0_6; -.
DR InParanoid; P25552; -.
DR OMA; WQICVGA; -.
DR PhylomeDB; P25552; -.
DR BioCyc; EcoCyc:PPPGPPHYDRO-MON; -.
DR BioCyc; MetaCyc:PPPGPPHYDRO-MON; -.
DR BRENDA; 3.6.1.40; 2026.
DR UniPathway; UPA00908; UER00885.
DR PRO; PR:P25552; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; Chromosome.
DR GO; GO:0008894; F:guanosine-5'-triphosphate,3'-diphosphate diphosphatase activity; IDA:EcoCyc.
DR GO; GO:0016462; F:pyrophosphatase activity; IBA:GO_Central.
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 GO; GO:0015949; P:nucleobase-containing small molecule interconversion; IMP:EcoCyc.
DR GO; GO:0006793; P:phosphorus metabolic process; IMP:EcoCyc.
DR GO; GO:0042594; P:response to starvation; IMP:EcoCyc.
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 1: Evidence at protein level;
KW 3D-structure; Hydrolase; Reference proteome.
FT CHAIN 1..494
FT /note="Guanosine-5'-triphosphate,3'-diphosphate
FT pyrophosphatase"
FT /id="PRO_0000194280"
FT CONFLICT 86
FT /note="T -> R (in Ref. 2; AAA67580)"
FT /evidence="ECO:0000305"
FT CONFLICT 423
FT /note="V -> L (in Ref. 2; AAA67580)"
FT /evidence="ECO:0000305"
FT CONFLICT 437..494
FT /note="FASRRRDDLVPEMTLQANHELLTLTLPQGWLTQHPLGKEIIAQESQWQSYVH
FT WPLEVH -> VGQPSP (in Ref. 1; AAB59049)"
FT /evidence="ECO:0000305"
FT STRAND 7..13
FT /evidence="ECO:0007829|PDB:6PBZ"
FT STRAND 15..26
FT /evidence="ECO:0007829|PDB:6PBZ"
FT STRAND 29..39
FT /evidence="ECO:0007829|PDB:6PBZ"
FT HELIX 43..45
FT /evidence="ECO:0007829|PDB:6PBZ"
FT HELIX 54..71
FT /evidence="ECO:0007829|PDB:6PBZ"
FT HELIX 76..78
FT /evidence="ECO:0007829|PDB:6PBZ"
FT STRAND 79..83
FT /evidence="ECO:0007829|PDB:6PBZ"
FT TURN 85..89
FT /evidence="ECO:0007829|PDB:6PBZ"
FT HELIX 93..103
FT /evidence="ECO:0007829|PDB:6PBZ"
FT STRAND 104..106
FT /evidence="ECO:0007829|PDB:6PBZ"
FT STRAND 108..110
FT /evidence="ECO:0007829|PDB:6PBZ"
FT HELIX 113..127
FT /evidence="ECO:0007829|PDB:6PBZ"
FT STRAND 132..139
FT /evidence="ECO:0007829|PDB:6PBZ"
FT STRAND 144..150
FT /evidence="ECO:0007829|PDB:6PBZ"
FT STRAND 153..161
FT /evidence="ECO:0007829|PDB:6PBZ"
FT HELIX 164..171
FT /evidence="ECO:0007829|PDB:6PBZ"
FT TURN 172..174
FT /evidence="ECO:0007829|PDB:6PBZ"
FT HELIX 179..203
FT /evidence="ECO:0007829|PDB:6PBZ"
FT STRAND 206..210
FT /evidence="ECO:0007829|PDB:6PBZ"
FT HELIX 213..225
FT /evidence="ECO:0007829|PDB:6PBZ"
FT HELIX 233..246
FT /evidence="ECO:0007829|PDB:6PBZ"
FT HELIX 249..251
FT /evidence="ECO:0007829|PDB:6PBZ"
FT HELIX 259..263
FT /evidence="ECO:0007829|PDB:6PBZ"
FT HELIX 265..278
FT /evidence="ECO:0007829|PDB:6PBZ"
FT STRAND 284..286
FT /evidence="ECO:0007829|PDB:6PBZ"
FT HELIX 291..300
FT /evidence="ECO:0007829|PDB:6PBZ"
FT HELIX 308..319
FT /evidence="ECO:0007829|PDB:6PBZ"
FT HELIX 324..345
FT /evidence="ECO:0007829|PDB:6PBZ"
FT HELIX 349..361
FT /evidence="ECO:0007829|PDB:6PBZ"
FT HELIX 362..367
FT /evidence="ECO:0007829|PDB:6PBZ"
FT HELIX 373..383
FT /evidence="ECO:0007829|PDB:6PBZ"
FT HELIX 391..402
FT /evidence="ECO:0007829|PDB:6PBZ"
FT STRAND 404..407
FT /evidence="ECO:0007829|PDB:6PBZ"
FT HELIX 410..413
FT /evidence="ECO:0007829|PDB:6PBZ"
FT HELIX 421..436
FT /evidence="ECO:0007829|PDB:6PBZ"
FT TURN 437..440
FT /evidence="ECO:0007829|PDB:6PBZ"
FT HELIX 443..445
FT /evidence="ECO:0007829|PDB:6PBZ"
FT STRAND 450..454
FT /evidence="ECO:0007829|PDB:6PBZ"
FT STRAND 457..461
FT /evidence="ECO:0007829|PDB:6PBZ"
FT HELIX 466..469
FT /evidence="ECO:0007829|PDB:6PBZ"
FT HELIX 471..486
FT /evidence="ECO:0007829|PDB:6PBZ"
FT STRAND 491..494
FT /evidence="ECO:0007829|PDB:6PBZ"
SQ SEQUENCE 494 AA; 54871 MW; C4DD8DC59432A5F9 CRC64;
MGSTSSLYAA IDLGSNSFHM LVVREVAGSI QTLTRIKRKV RLAAGLNSEN ALSNEAMERG
WQCLRLFAER LQDIPPSQIR VVATATLRLA VNAGDFIAKA QEILGCPVQV ISGEEEARLI
YQGVAHTTGG ADQRLVVDIG GASTELVTGT GAQTTSLFSL SMGCVTWLER YFADRNLGQE
NFDAAEKAAR EVLRPVADEL RYHGWKVCVG ASGTVQALQE IMMAQGMDER ITLEKLQQLK
QRAIHCGRLE ELEIDGLTLE RALVFPSGLA ILIAIFTELN IQCMTLAGGA LREGLVYGML
HLAVEQDIRS RTLRNIQRRF MIDIDQAQRV AKVAANFFDQ VENEWHLEAI SRDLLISACQ
LHEIGLSVDF KQAPQHAAYL VRNLDLPGFT PAQKKLLATL LLNQTNPVDL SSLHQQNAVP
PRVAEQLCRL LRLAIIFASR RRDDLVPEMT LQANHELLTL TLPQGWLTQH PLGKEIIAQE
SQWQSYVHWP LEVH
