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UniProtKB/Swiss-Prot entry P25552


[Entry info] [Name and origin] [References] [Comments] [Cross-references] [Keywords] [Features] [Sequence] [Tools]

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Entry information
Entry name GPPA_ECOLI
Primary accession number P25552
Secondary accession numbers Q2M887 Q6BF04
Integrated into Swiss-Prot on May 1, 1992
Sequence was last modified on October 11, 2004 (Sequence version 3)
Annotations were last modified on    September 2, 2008 (Entry version 59)
Name and origin of the protein
Protein name Guanosine-5'-triphosphate,3'-diphosphate pyrophosphatase
Synonyms EC 3.6.1.40
Guanosine pentaphosphate phosphohydrolase
pppGpp-5'-phosphohydrolase
Gene name
Name: gppA
Synonyms: gpp
OrderedLocusNames: b3779, JW5603
From
Escherichia coli (strain K12) [TaxID: 83333] [HAMAP proteome]
Taxonomy Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales; Enterobacteriaceae; Escherichia.
Protein existence 1: Evidence at protein level;
References
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
STRAIN=K12;
PubMed=1931833 [NCBI, ExPASy, EBI, Israel, Japan]
Kalman M., Murphy H., Cashel M.;
"rhlB, a new Escherichia coli K-12 gene with an RNA helicase-like protein sequence motif, one of at least five such possible genes in a prokaryote.";
New Biol. 3:886-895(1991).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=K12 / MG1655 / ATCC 47076;
PubMed=1379743 [NCBI, ExPASy, EBI, Israel, Japan]
Daniels D.L., Plunkett G. III, Burland V.D., Blattner F.R.;
"Analysis of the Escherichia coli genome: DNA sequence of the region from 84.5 to 86.5 minutes.";
Science 257:771-778(1992).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=K12 / MG1655 / ATCC 47076;
DOI=10.1126/science.277.5331.1453; PubMed=9278503 [NCBI, ExPASy, EBI, Israel, Japan]
Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V., Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F., Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B., Shao Y.;
"The complete genome sequence of Escherichia coli K-12.";
Science 277:1453-1474(1997).
[4]
SEQUENCE REVISION TO 86 AND 423.
DOI=10.1093/nar/gkj405; PubMed=16397293 [NCBI, ExPASy, EBI, Israel, Japan]
Riley M., Abe T., Arnaud M.B., Berlyn M.K.B., Blattner F.R., Chaudhuri R.R., Glasner J.D., Horiuchi T., Keseler I.M., Kosuge T., Mori H., Perna N.T., Plunkett G. III, Rudd K.E., Serres M.H., Thomas G.H., Thomson N.R., Wishart D., Wanner B.L.;
"Escherichia coli K-12: a cooperatively developed annotation snapshot -- 2005.";
Nucleic Acids Res. 34:1-9(2006).
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
DOI=10.1038/msb4100049; PubMed=16738553 [NCBI, ExPASy, EBI, Israel, Japan]
Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S., Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.;
"Highly accurate genome sequences of Escherichia coli K-12 strains MG1655 and W3110.";
Mol. Syst. Biol. 2:E1-E5(2006).
[6]
SIMILARITY TO PPX.
DOI=10.1016/0968-0004(93)90172-J; PubMed=8212131 [NCBI, ExPASy, EBI, Israel, Japan]
Reizer J., Reizer A., Saier M.H. Jr., Bork B., Sander C.;
"Exopolyphosphate phosphatase and guanosine pentaphosphate phosphatase belong to the sugar kinase/actin/hsp 70 superfamily.";
Trends Biochem. Sci. 18:247-248(1993).
[7]
CHARACTERIZATION.
PubMed=8394006 [NCBI, ExPASy, EBI, Israel, Japan]
Keasling J.D., Bertsch L., Kornberg A.;
"Guanosine pentaphosphate phosphohydrolase of Escherichia coli is a long-chain exopolyphosphatase.";
Proc. Natl. Acad. Sci. U.S.A. 90:7029-7033(1993).
Comments
Copyright
Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.
Cross-references
Sequence databases
EMBL
M83316; AAB59049.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
M87049; AAA67580.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
U00096; AAT48210.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AP009048; BAE77519.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
PIR A48285; A48285.
RefSeq AP_004018.1; -.
YP_026252.1; -.
3D structure databases
ModBase P25552.
Enzyme and pathway databases
BioCyc EcoCyc:PPPGPPHYDRO-MON; -.
MetaCyc:PPPGPPHYDRO-MON; -.
Organism-specific databases
EchoBASE EB0408; -.
EcoGene EG10413; gpp.
Ontologies
GO
GO:0008894; Molecular function: guanosine-5'-triphosphate,3'-diphosphate diphosphatase activity (inferred from electronic annotation from HAMAP).
QuickGo view.
Family and domain databases
HAMAP MF_01550; -; 1.
PBIL [Tree]
InterPro IPR003695; Ppx_GppA.
Graphical view of domain structure.
Pfam PF02541; Ppx-GppA; 1.
Pfam graphical view of domain structure.
BLOCKS P25552.
ProtoNet P25552.
Genome annotation databases
GeneID 948291; -.
GenomeReviews U00096_GR; b3779.
AP009048_GR; JW5603.
KEGG ecj:JW5603; -.
eco:b3779; -.
Phylogenomic databases
HOGENOM P25552; -.
Genome annotation databases
CMR P25552; b3779.
Other
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
Complete proteome; Hydrolase.
Features
SEVIEWER logo Feature table viewer
KeyFrom   To Length Description FTId
CHAIN   1   494  494     Guanosine-5'-triphosphate,3'-diphosphate pyrophosphatase. PRO_0000194280
CONFLICT   86    86        T -> R (in Ref. 2; AAA67580). 
CONFLICT   423   423        V -> L (in Ref. 2; AAA67580). 
CONFLICT   437   494        FASRRRDDLVPEMTLQANHELLTLTLPQGWLTQHPLGKEI IAQESQWQSYVHWPLEVH -> VGQPSP (in Ref. 1; AAB59049). 
Sequence information
Length: 494 AA [This is the length of the unprocessed precursor] Molecular weight: 54871 Da [This is the MW of the unprocessed precursor] CRC64: C4DD8DC59432A5F9 [This is a checksum on the sequence]
        10         20         30         40         50         60 
MGSTSSLYAA IDLGSNSFHM LVVREVAGSI QTLTRIKRKV RLAAGLNSEN ALSNEAMERG 

        70         80         90        100        110        120 
WQCLRLFAER LQDIPPSQIR VVATATLRLA VNAGDFIAKA QEILGCPVQV ISGEEEARLI 

       130        140        150        160        170        180 
YQGVAHTTGG ADQRLVVDIG GASTELVTGT GAQTTSLFSL SMGCVTWLER YFADRNLGQE 

       190        200        210        220        230        240 
NFDAAEKAAR EVLRPVADEL RYHGWKVCVG ASGTVQALQE IMMAQGMDER ITLEKLQQLK 

       250        260        270        280        290        300 
QRAIHCGRLE ELEIDGLTLE RALVFPSGLA ILIAIFTELN IQCMTLAGGA LREGLVYGML 

       310        320        330        340        350        360 
HLAVEQDIRS RTLRNIQRRF MIDIDQAQRV AKVAANFFDQ VENEWHLEAI SRDLLISACQ 

       370        380        390        400        410        420 
LHEIGLSVDF KQAPQHAAYL VRNLDLPGFT PAQKKLLATL LLNQTNPVDL SSLHQQNAVP 

       430        440        450        460        470        480 
PRVAEQLCRL LRLAIIFASR RRDDLVPEMT LQANHELLTL TLPQGWLTQH PLGKEIIAQE 

       490 
SQWQSYVHWP LEVH 

P25552 in FASTA format

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