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UniProtKB/Swiss-Prot entry P03842

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

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Entry information
Entry name RNPH_ECOLI
Primary accession number P03842
Secondary accession number A8DYQ0
Integrated into Swiss-Prot on July 21, 1986
Sequence was last modified on July 1, 1993 (Sequence version 2)
Annotations were last modified on    November 4, 2008 (Entry version 77)
Name and origin of the protein
Protein name Ribonuclease PH
Synonyms RNase PH
EC 2.7.7.56
tRNA nucleotidyltransferase
Gene name
Name: rph
OrderedLocusNames: b3643
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 / MC4100 / ATCC 35695 / DSM 6574;
PubMed=6207018 [NCBI, ExPASy, EBI, Israel, Japan]
Poulsen P., Bonekamp F., Jensen K.F.;
"Structure of the Escherichia coli pyrE operon and control of pyrE expression by a UTP modulated intercistronic attentuation.";
EMBO J. 3:1783-1790(1984).
[2]
 NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=K12 / MG1655 / ATCC 47076;
DOI=10.1006/geno.1993.1230; PubMed=7686882 [NCBI, ExPASy, EBI, Israel, Japan]
Burland V.D., Plunkett G. III, Daniels D.L., Blattner F.R.;
"DNA sequence and analysis of 136 kilobases of the Escherichia coli genome: organizational symmetry around the origin of replication.";
Genomics 16:551-561(1993).
[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]
 IMPORTANCE AT HIGH TEMPERATURE.
STRAIN=K12 / MC4100 / ATCC 35695 / DSM 6574;
DOI=10.1016/0923-2508(91)90042-9; PubMed=1925027 [NCBI, ExPASy, EBI, Israel, Japan]
Poulsen P., Jensen K.F.;
"Three genes preceding pyrE on the Escherichia coli chromosome are essential for survival and normal cell morphology in stationary culture and at high temperature.";
Res. Microbiol. 142:283-288(1991).
[5]
 FUNCTION, AND PARTIAL PROTEIN SEQUENCE OF 1-21.
PubMed=1885537 [NCBI, ExPASy, EBI, Israel, Japan]
Ost K.A., Deutscher M.P.;
"Escherichia coli orfE (upstream of pyrE) encodes RNase PH.";
J. Bacteriol. 173:5589-5591(1991).
[6]
 CHARACTERIZATION.
STRAIN=K12 / MC1000 / ATCC 39531;
PubMed=1512252 [NCBI, ExPASy, EBI, Israel, Japan]
Jensen K.F., Andersen J.T., Poulsen P.;
"Overexpression and rapid purification of the orfE/rph gene product, RNase PH of Escherichia coli.";
J. Biol. Chem. 267:17147-17152(1992).
[7]
 CHARACTERIZATION.
STRAIN=K12 / MC1000 / ATCC 39531;
PubMed=1512253 [NCBI, ExPASy, EBI, Israel, Japan]
Kelly K.O., Deutscher M.P.;
"Characterization of Escherichia coli RNase PH.";
J. Biol. Chem. 267:17153-17158(1992).
[8]
 NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 208-238 (STRAIN W3110), AND LOSS OF ACTIVITY IN SOME K12 STRAINS.
STRAIN=K12 / MG1655 / ATCC 47076, K12 / W1485, and K12 / W3110 / ATCC 27325 / DSM 5911;
PubMed=8501045 [NCBI, ExPASy, EBI, Israel, Japan]
Jensen K.F.;
"The Escherichia coli K-12 'wild types' W3110 and MG1655 have an rph frameshift mutation that leads to pyrimidine starvation due to low pyrE expression levels.";
J. Bacteriol. 175:3401-3407(1993).
Comments
  • FUNCTION: Phosphorolytic exoribonuclease that removes nucleotide residues following the -CCA terminus of tRNA and adds nucleotides to the ends of RNA molecules by using nucleoside diphosphates as substrates. Also acts to regulate the attenuation of pyrE.
  • CATALYTIC ACTIVITY: tRNA(n+1) + phosphate = tRNA(n) + a nucleoside diphosphate.
  • MISCELLANEOUS: The gene in K12 strains MG1655 and W3110 (and also other derivatives of K12 W1485) has a frameshift mutation that leads to loss of activity, although the protein may be translated. Thus in those strains rph is a pseudogene. The sequence shown here is the functional one corresponding to K12 strains MC1000 and MC4100.
  • SIMILARITY: Belongs to the RNase PH family.
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
X00781; CAA25357.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
V01578; -; NOT_ANNOTATED_CDS; Genomic_DNA.[EMBL / GenBank / DDBJ]
L10328; AAA61996.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
U00096; ABV59576.1; ALT_SEQ; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
X72920; -; NOT_ANNOTATED_CDS; Genomic_DNA.[EMBL / GenBank / DDBJ]
PIR A04470; QQECPE.
3D structure databases
SMR P03842; 2-237.
ModBase P03842.
Protein-protein interaction databases
DIP DIP:10738N; -.
Enzyme and pathway databases
BioCyc EcoCyc:EG10863-MON; -.
Organism-specific databases
EcoGene EG10863; rph.
Ontologies
GO
GO:0000049; Molecular function: tRNA binding (inferred from electronic annotation from HAMAP).
GO:0009022; Molecular function: tRNA nucleotidyltransferase activity (inferred from electronic annotation from HAMAP).
GO:0008033; Biological process: tRNA processing (inferred from electronic annotation from HAMAP).
QuickGo view.
Family and domain databases
HAMAP MF_00564; -; 1.
PBIL [Tree]
InterPro IPR001247; ExoRNase_PH_dom1.
IPR015847; ExoRNase_PH_dom2.
IPR002381; RNase_PH_bac-type.
Graphical view of domain structure.
Pfam PF01138; RNase_PH; 1.
PF03725; RNase_PH_C; 1.
Pfam graphical view of domain structure.
TIGRFAMs TIGR01966; RNasePH; 1.
PROSITE PS01277; RIBONUCLEASE_PH; 1.
BLOCKS P03842.
ProtoNet P03842.
Genome annotation databases
GenomeReviews U00096_GR; b3643.
KEGG eco:b3643; -.
Phylogenomic databases
HOGENOM P03842; -.
Genome annotation databases
CMR P03842; b3643.
Other
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
Complete proteome; Direct protein sequencing; Nucleotidyltransferase; Transferase; tRNA processing.
Features
SEVIEWER logo Feature table viewer
KeyFrom   To Length Description FTId
CHAIN   1   238  238     Ribonuclease PH. PRO_0000139889
VARIANT   224   238  15     GIESIVATQKAALAN -> ESNPL (in strain: K12 / MG1655 / ATCC 47076 and K12 / W3110 / ATCC 27325 / DSM 5911). 
CONFLICT   123   124        GG -> AW (in Ref. 1; CAA25357). 
Sequence information
Length: 238 AA [This is the length of the unprocessed precursor] Molecular weight: 25352 Da [This is the MW of the unprocessed precursor] CRC64: 7299C5C8F2364D34 [This is a checksum on the sequence] 
        10         20         30         40         50         60 
MRPAGRSNNQ VRPVTLTRNY TKHAEGSVLV EFGDTKVLCT ASIEEGVPRF LKGQGQGWIT 

        70         80         90        100        110        120 
AEYGMLPRST HTRNAREAAK GKQGGRTMEI QRLIARALRA AVDLKALGEF TITLDCDVLQ 

       130        140        150        160        170        180 
ADGGTRTASI TGACVALVDA LQKLVENGKL KTNPMKGMVA AVSVGIVNGE AVCDLEYVED 

       190        200        210        220        230 
SAAETDMNVV MTEDGRIIEV QGTAEGEPFT HEELLILLAL ARGGIESIVA TQKAALAN
P03842 in FASTA format

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