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Protein

Peptide chain release factor 1

Gene

prfA

Organism
Escherichia coli (strain K12)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

Peptide chain release factor 1 directs the termination of translation in response to the peptide chain termination codons UAG and UAA.

GO - Molecular functioni

  • ribosome binding Source: EcoCyc
  • translation release factor activity, codon specific Source: EcoCyc

GO - Biological processi

  • translational termination Source: EcoCyc
Complete GO annotation...

Keywords - Biological processi

Protein biosynthesis

Enzyme and pathway databases

BioCyciEcoCyc:EG10761-MONOMER.
ECOL316407:JW1202-MONOMER.

Names & Taxonomyi

Protein namesi
Recommended name:
Peptide chain release factor 1
Short name:
RF-1
Gene namesi
Name:prfA
Synonyms:sueB, uar
Ordered Locus Names:b1211, JW1202
OrganismiEscherichia coli (strain K12)
Taxonomic identifieri83333 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia
Proteomesi
  • UP000000318 Componenti: Chromosome
  • UP000000625 Componenti: Chromosome

Organism-specific databases

EcoGeneiEG10761. prfA.

Subcellular locationi

GO - Cellular componenti

  • cytosol Source: EcoCyc
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi235 – 2351Q → E or A: Loss of methylation. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 360360Peptide chain release factor 1PRO_0000177668Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei235 – 2351N5-methylglutamine2 Publications

Post-translational modificationi

Methylated by PrmC. Methylation increases the termination efficiency of RF1.3 Publications

Keywords - PTMi

Methylation

Proteomic databases

EPDiP0A7I0.
PaxDbiP0A7I0.
PRIDEiP0A7I0.

Interactioni

Protein-protein interaction databases

BioGridi4260107. 6 interactions.
DIPiDIP-35936N.
IntActiP0A7I0. 13 interactions.
MINTiMINT-1219241.
STRINGi511145.b1211.

Structurei

Secondary structure

1
360
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi10 – 2617Combined sources
Helixi35 – 5521Combined sources
Helixi106 – 1083Combined sources
Beta strandi111 – 1177Combined sources
Beta strandi119 – 1213Combined sources
Helixi122 – 14120Combined sources
Beta strandi148 – 1536Combined sources
Beta strandi157 – 16610Combined sources
Beta strandi168 – 1703Combined sources
Helixi172 – 1754Combined sources
Helixi176 – 1783Combined sources
Beta strandi180 – 1867Combined sources
Beta strandi197 – 2048Combined sources
Turni211 – 2133Combined sources
Beta strandi219 – 2268Combined sources
Turni234 – 2363Combined sources
Beta strandi240 – 2489Combined sources
Turni249 – 2513Combined sources
Beta strandi254 – 2618Combined sources
Helixi263 – 27816Combined sources
Turni279 – 2846Combined sources
Beta strandi306 – 3116Combined sources
Turni312 – 3154Combined sources
Beta strandi316 – 3194Combined sources
Helixi320 – 3223Combined sources
Beta strandi324 – 3274Combined sources
Helixi329 – 3346Combined sources
Helixi338 – 35215Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2B3TX-ray3.10B1-356[»]
5J4DX-ray3.10JA/OC1-360[»]
ProteinModelPortaliP0A7I0.
SMRiP0A7I0. Positions 7-354.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP0A7I0.

Family & Domainsi

Sequence similaritiesi

Phylogenomic databases

eggNOGiENOG4105C8K. Bacteria.
COG0216. LUCA.
HOGENOMiHOG000074815.
InParanoidiP0A7I0.
KOiK02835.
OMAiLRIDVFC.
OrthoDBiEOG6TN48J.
PhylomeDBiP0A7I0.

Family and domain databases

Gene3Di3.30.160.20. 1 hit.
HAMAPiMF_00093. Rel_fac_1.
InterProiIPR014720. dsRBD_dom.
IPR005139. PCRF.
IPR000352. Pep_chain_release_fac_I_II.
IPR004373. PrfA.
[Graphical view]
PfamiPF03462. PCRF. 1 hit.
PF00472. RF-1. 1 hit.
[Graphical view]
SMARTiSM00937. PCRF. 1 hit.
[Graphical view]
TIGRFAMsiTIGR00019. prfA. 1 hit.
PROSITEiPS00745. RF_PROK_I. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P0A7I0-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MKPSIVAKLE ALHERHEEVQ ALLGDAQTIA DQERFRALSR EYAQLSDVSR
60 70 80 90 100
CFTDWQQVQE DIETAQMMLD DPEMREMAQD ELREAKEKSE QLEQQLQVLL
110 120 130 140 150
LPKDPDDERN AFLEVRAGTG GDEAALFAGD LFRMYSRYAE ARRWRVEIMS
160 170 180 190 200
ASEGEHGGYK EIIAKISGDG VYGRLKFESG GHRVQRVPAT ESQGRIHTSA
210 220 230 240 250
CTVAVMPELP DAELPDINPA DLRIDTFRSS GAGGQHVNTT DSAIRITHLP
260 270 280 290 300
TGIVVECQDE RSQHKNKAKA LSVLGARIHA AEMAKRQQAE ASTRRNLLGS
310 320 330 340 350
GDRSDRNRTY NFPQGRVTDH RINLTLYRLD EVMEGKLDML IEPIIQEHQA
360
DQLAALSEQE
Length:360
Mass (Da):40,517
Last modified:June 7, 2005 - v1
Checksum:i47B3B77705A71954
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti72 – 9120PEMRE…EKSEQ → LRYLLYLRLFVVLFRHVVGD (PubMed:2684779).CuratedAdd
BLAST
Sequence conflicti211 – 2111D → E in AAC43437 (PubMed:7543480).Curated
Sequence conflicti241 – 2411D → G in AAA24519 (PubMed:3889910).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M11519 Genomic DNA. Translation: AAA24519.1.
U18555 Genomic DNA. Translation: AAC43437.1.
U00096 Genomic DNA. Translation: AAC74295.1.
AP009048 Genomic DNA. Translation: BAA36069.1.
M25323 Genomic DNA. Translation: AAA23955.1.
D28567 Genomic DNA. Translation: BAA05914.1.
PIRiH64867. FCECR1.
RefSeqiNP_415729.1. NC_000913.3.
WP_000804726.1. NZ_LN832404.1.

Genome annotation databases

EnsemblBacteriaiAAC74295; AAC74295; b1211.
BAA36069; BAA36069; BAA36069.
GeneIDi949002.
KEGGiecj:JW1202.
eco:b1211.
PATRICi32117674. VBIEscCol129921_1259.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M11519 Genomic DNA. Translation: AAA24519.1.
U18555 Genomic DNA. Translation: AAC43437.1.
U00096 Genomic DNA. Translation: AAC74295.1.
AP009048 Genomic DNA. Translation: BAA36069.1.
M25323 Genomic DNA. Translation: AAA23955.1.
D28567 Genomic DNA. Translation: BAA05914.1.
PIRiH64867. FCECR1.
RefSeqiNP_415729.1. NC_000913.3.
WP_000804726.1. NZ_LN832404.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2B3TX-ray3.10B1-356[»]
5J4DX-ray3.10JA/OC1-360[»]
ProteinModelPortaliP0A7I0.
SMRiP0A7I0. Positions 7-354.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi4260107. 6 interactions.
DIPiDIP-35936N.
IntActiP0A7I0. 13 interactions.
MINTiMINT-1219241.
STRINGi511145.b1211.

Proteomic databases

EPDiP0A7I0.
PaxDbiP0A7I0.
PRIDEiP0A7I0.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAC74295; AAC74295; b1211.
BAA36069; BAA36069; BAA36069.
GeneIDi949002.
KEGGiecj:JW1202.
eco:b1211.
PATRICi32117674. VBIEscCol129921_1259.

Organism-specific databases

EchoBASEiEB0754.
EcoGeneiEG10761. prfA.

Phylogenomic databases

eggNOGiENOG4105C8K. Bacteria.
COG0216. LUCA.
HOGENOMiHOG000074815.
InParanoidiP0A7I0.
KOiK02835.
OMAiLRIDVFC.
OrthoDBiEOG6TN48J.
PhylomeDBiP0A7I0.

Enzyme and pathway databases

BioCyciEcoCyc:EG10761-MONOMER.
ECOL316407:JW1202-MONOMER.

Miscellaneous databases

EvolutionaryTraceiP0A7I0.
PROiP0A7I0.

Family and domain databases

Gene3Di3.30.160.20. 1 hit.
HAMAPiMF_00093. Rel_fac_1.
InterProiIPR014720. dsRBD_dom.
IPR005139. PCRF.
IPR000352. Pep_chain_release_fac_I_II.
IPR004373. PrfA.
[Graphical view]
PfamiPF03462. PCRF. 1 hit.
PF00472. RF-1. 1 hit.
[Graphical view]
SMARTiSM00937. PCRF. 1 hit.
[Graphical view]
TIGRFAMsiTIGR00019. prfA. 1 hit.
PROSITEiPS00745. RF_PROK_I. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Bacterial peptide chain release factors: conserved primary structure and possible frameshift regulation of release factor 2."
    Craigen W.J., Cook R.G., Tate W.P., Caskey C.T.
    Proc. Natl. Acad. Sci. U.S.A. 82:3616-3620(1985) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  2. "Rapid and precise mapping of the Escherichia coli release factor genes by two physical approaches."
    Lee C.C., Kohara Y., Akiyama K., Smith C.L., Craigen W.J., Caskey C.T.
    J. Bacteriol. 170:4537-4541(1988) [PubMed] [Europe PMC] [Abstract]
    Cited for: SEQUENCE REVISION.
  3. "Expression of genes kdsA and kdsB involved in 3-deoxy-D-manno-octulosonic acid metabolism and biosynthesis of enterobacterial lipopolysaccharide is growth phase regulated primarily at the transcriptional level in Escherichia coli K-12."
    Strohmaier H., Remler P., Renner W., Hoegenauer G.
    J. Bacteriol. 177:4488-4500(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: K12.
  4. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
  5. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: K12 / MG1655 / ATCC 47076.
  6. "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655 and W3110."
    Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S., Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.
    Mol. Syst. Biol. 2:E1-E5(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
  7. "Cloning and structure of the hem A gene of Escherichia coli K-12."
    Li J.-M., Russell C.S., Cosloy S.D.
    Gene 82:209-217(1989) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-91.
    Strain: K12.
  8. "Isolation, nucleotide sequence, and preliminary characterization of the Escherichia coli K-12 hemA gene."
    Verkamp E., Chelm B.K.
    J. Bacteriol. 171:4728-4735(1989) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-6.
    Strain: K12.
  9. "Cloning and sequencing of a previously unidentified gene that is involved in the biosynthesis of heme in Escherichia coli."
    Nakayashiki T., Nishimura K., Inokuchi H.
    Gene 153:67-70(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 339-360.
    Strain: K12.
  10. "Escherichia coli proteome analysis using the gene-protein database."
    VanBogelen R.A., Abshire K.Z., Moldover B., Olson E.R., Neidhardt F.C.
    Electrophoresis 18:1243-1251(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY 2D-GEL.
  11. "A post-translational modification in the GGQ motif of RF2 from Escherichia coli stimulates termination of translation."
    Dincbas-Renqvist V., Engstroem A., Mora L., Heurgue-Hamard V., Buckingham R., Ehrenberg M.
    EMBO J. 19:6900-6907(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: METHYLATION AT GLN-235.
  12. "The hemK gene in Escherichia coli encodes the N(5)-glutamine methyltransferase that modifies peptide release factors."
    Heurgue-Hamard V., Champ S., Engstroem A., Ehrenberg M., Buckingham R.H.
    EMBO J. 21:769-778(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: METHYLATION AT GLN-235 BY PRMC, MUTAGENESIS OF GLN-235.
    Strain: K12.
  13. "HemK, a class of protein methyl transferase with similarity to DNA methyl transferases, methylates polypeptide chain release factors, and hemK knockout induces defects in translational termination."
    Nakahigashi K., Kubo N., Narita S., Shimaoka T., Goto S., Oshima T., Mori H., Maeda M., Wada C., Inokuchi H.
    Proc. Natl. Acad. Sci. U.S.A. 99:1473-1478(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: METHYLATION BY PRMC.
    Strain: K12.
  14. "Methylation of bacterial release factors RF1 and RF2 is required for normal translation termination in vivo."
    Mora L., Heurgue-Hamard V., de Zamaroczy M., Kervestin S., Buckingham R.H.
    J. Biol. Chem. 282:35638-35645(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: PTM, EFFECT OF METHYLATION.
    Strain: K12.
  15. "Molecular basis for bacterial class I release factor methylation by PrmC."
    Graille M., Heurgue-Hamard V., Champ S., Mora L., Scrima N., Ulryck N., van Tilbeurgh H., Buckingham R.H.
    Mol. Cell 20:917-927(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (3.1 ANGSTROMS) IN COMPLEX WITH METHYLTRANSFERASE PRMC.

Entry informationi

Entry nameiRF1_ECOLI
AccessioniPrimary (citable) accession number: P0A7I0
Secondary accession number(s): P07011, P77340
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 1, 1988
Last sequence update: June 7, 2005
Last modified: July 6, 2016
This is version 101 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. Escherichia coli
    Escherichia coli (strain K12): entries and cross-references to EcoGene
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.