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Protein

Peptide chain release factor RF2

Gene

prfB

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

Functioni

Peptide chain release factor 2 directs the termination of translation in response to the peptide chain termination codons UGA and UAA (PubMed:11118225, PubMed:17932046). Acts as a peptidyl-tRNA hydrolase (PubMed:22857598, PubMed:27934701). In the presence of truncated mRNA in the 70S ribosome, ArfA and RF2 interact such that the GGQ peptide hydrolysis motif of RF2 rises into the peptidyl-transferase center and releases the ribosome (PubMed:27906160, PubMed:27906161, PubMed:27934701, PubMed:28077875). Recruited by ArfA to rescue stalled ribosomes in the absence of a normal stop codon (PubMed:22857598, PubMed:22922063, PubMed:25355516).1 Publication9 Publications

Miscellaneous

The gene for this protein contains a UGA in-frame termination codon after Leu-25; a naturally occurring frameshift enables complete translation of RF-2. This provides a mechanism for the protein to regulate its own production.1 Publication

GO - Molecular functioni

  • translation release factor activity, codon specific Source: EcoCyc

GO - Biological processi

  • translational termination Source: EcoCyc

Keywordsi

Biological processProtein biosynthesis

Enzyme and pathway databases

BioCyciEcoCyc:EG10762-MONOMER.

Names & Taxonomyi

Protein namesi
Recommended name:
Peptide chain release factor RF2
Short name:
RF-2
Gene namesi
Name:prfB
Synonyms:supK
Ordered Locus Names:b2891, JW5847
OrganismiEscherichia coli (strain K12)
Taxonomic identifieri83333 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacteralesEnterobacteriaceaeEscherichia
Proteomesi
  • UP000000318 Componenti: Chromosome
  • UP000000625 Componenti: Chromosome

Organism-specific databases

EcoGeneiEG10762. prfB.

Subcellular locationi

GO - Cellular componenti

  • cytosol Source: EcoCyc

Keywords - Cellular componenti

Cytoplasm

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi200R → C: About 50% ribosome rescue activity with ArfA, initial rate. 1 Publication1
Mutagenesisi205S → C: About 50% ribosome rescue activity with ArfA, initial rate. 1 Publication1
Mutagenesisi206P → T: No effect on ArfA rescue of stalled ribosomes. 1 Publication1
Mutagenesisi221 – 223FVY → AVA: About 5% ribosome rescue activity with ArfA, initial rate. 1 Publication3
Mutagenesisi252Q → E: Loss of methylation. No longer allows ArfA to rescue stalled ribosomes. 3 Publications1
Mutagenesisi322 – 323QI → AA: About 20% ribosome rescue activity with ArfA, initial rate. 1 Publication2

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00001668161 – 365Peptide chain release factor RF2Add BLAST365

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei252N5-methylglutamine3 Publications1

Post-translational modificationi

Methylated by PrmC. Methylation increases the termination efficiency of RF2. Is absent when the factor is overproduced.4 Publications

Keywords - PTMi

Methylation

Proteomic databases

PaxDbiP07012.
PRIDEiP07012.

Interactioni

Subunit structurei

Interacts with the ribosome (PubMed:22857598, PubMed:22922063, PubMed:25355516, PubMed:12511960, PubMed:12511961). Recruited to stalled ribosomes by ArfA, in the pressence of truncated mRNA, ArfA influences RF2 conformation so RF2 can hydrolyze the peptidyl-tRNA bond (PubMed:27906160, PubMed:27906161, PubMed:27934701, PubMed:28077875).9 Publications

Protein-protein interaction databases

BioGridi4259706. 79 interactors.
DIPiDIP-10559N.
IntActiP07012. 19 interactors.
MINTiMINT-1238444.
STRINGi316385.ECDH10B_3065.

Structurei

Secondary structure

1365
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi6 – 24Combined sources19
Helixi27 – 42Combined sources16
Helixi44 – 48Combined sources5
Helixi50 – 90Combined sources41
Helixi93 – 113Combined sources21
Helixi114 – 118Combined sources5
Turni122 – 125Combined sources4
Beta strandi128 – 134Combined sources7
Helixi138 – 158Combined sources21
Beta strandi162 – 170Combined sources9
Beta strandi172 – 185Combined sources14
Helixi188 – 192Combined sources5
Helixi193 – 195Combined sources3
Beta strandi197 – 204Combined sources8
Beta strandi208 – 210Combined sources3
Beta strandi213 – 224Combined sources12
Helixi236 – 238Combined sources3
Beta strandi239 – 244Combined sources6
Beta strandi260 – 265Combined sources6
Turni266 – 268Combined sources3
Beta strandi271 – 274Combined sources4
Beta strandi276 – 278Combined sources3
Helixi280 – 306Combined sources27
Beta strandi321 – 327Combined sources7
Helixi328 – 330Combined sources3
Beta strandi332 – 335Combined sources4
Turni336 – 338Combined sources3
Beta strandi341 – 343Combined sources3
Helixi345 – 349Combined sources5
Helixi354 – 362Combined sources9

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1GQEX-ray1.81A1-365[»]
1MI6electron microscopy10.90A1-365[»]
1ML5electron microscopy14.00Z1-365[»]
5CZPX-ray3.30QY/XY1-365[»]
5DFEX-ray3.10QY/XY1-365[»]
5H5Uelectron microscopy3.0041-365[»]
5MDVelectron microscopy2.9771-365[»]
5MDWelectron microscopy3.0671-365[»]
5MGPelectron microscopy3.10z6-364[»]
5U4Ielectron microscopy3.50v1-365[»]
5U4Jelectron microscopy3.70v1-365[»]
5U9Felectron microscopy3.20Z1-365[»]
5U9Gelectron microscopy3.20Z1-365[»]
ProteinModelPortaliP07012.
SMRiP07012.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP07012.

Family & Domainsi

Motif

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Motifi250 – 252GGQ motif3

Sequence similaritiesi

Phylogenomic databases

eggNOGiENOG4105CG1. Bacteria.
COG1186. LUCA.
HOGENOMiHOG000074814.
InParanoidiP07012.
KOiK02836.
PhylomeDBiP07012.

Family and domain databases

HAMAPiMF_00094. Rel_fac_2. 1 hit.
InterProiView protein in InterPro
IPR005139. PCRF.
IPR000352. Pep_chain_release_fac_I_II.
IPR004374. PrfB.
IPR020853. RF2_bac.
PfamiView protein in Pfam
PF03462. PCRF. 1 hit.
PF00472. RF-1. 1 hit.
SMARTiView protein in SMART
SM00937. PCRF. 1 hit.
TIGRFAMsiTIGR00020. prfB. 1 hit.
PROSITEiView protein in PROSITE
PS00745. RF_PROK_I. 1 hit.

Sequencei

Sequence statusi: Complete.

P07012-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MFEINPVNNR IQDLTERSDV LRGYLDYDAK KERLEEVNAE LEQPDVWNEP
60 70 80 90 100
ERAQALGKER SSLEAVVDTL DQMKQGLEDV SGLLELAVEA DDEETFNEAV
110 120 130 140 150
AELDALEEKL AQLEFRRMFS GEYDSADCYL DIQAGSGGTE AQDWASMLER
160 170 180 190 200
MYLRWAESRG FKTEIIEESE GEVAGIKSVT IKISGDYAYG WLRTETGVHR
210 220 230 240 250
LVRKSPFDSG GRRHTSFSSA FVYPEVDDDI DIEINPADLR IDVYRTSGAG
260 270 280 290 300
GQHVNRTESA VRITHIPTGI VTQCQNDRSQ HKNKDQAMKQ MKAKLYELEM
310 320 330 340 350
QKKNAEKQAM EDNKSDIGWG SQIRSYVLDD SRIKDLRTGV ETRNTQAVLD
360
GSLDQFIEAS LKAGL
Length:365
Mass (Da):41,251
Last modified:November 1, 1997 - v3
Checksum:iEB8C802FDDE0A76D
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti201L → V in AAA24520 (PubMed:3889910).Curated1
Sequence conflicti201L → V (PubMed:3049538).Curated1

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural varianti246T → A in strain: BL21 and MRE-600; increased termination efficiency. 1 Publication1 Publication1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M11520 Genomic DNA. Translation: AAA24520.1.
U28375 Genomic DNA. Translation: AAA83072.1.
U00096 Genomic DNA. Translation: AAC75929.1.
AP009048 Genomic DNA. Translation: BAE76956.1.
J03795 Genomic DNA. Translation: AAA23958.1.
PIRiC65073. FCECR2.
RefSeqiNP_417367.1. NC_000913.3.

Genome annotation databases

EnsemblBacteriaiAAC75929; AAC75929; b2891.
BAE76956; BAE76956; BAE76956.
GeneIDi947369.
KEGGiecj:JW5847.
eco:b2891.
PATRICifig|511145.12.peg.2984.

Keywords - Coding sequence diversityi

Ribosomal frameshifting

Similar proteinsi

Entry informationi

Entry nameiRF2_ECOLI
AccessioniPrimary (citable) accession number: P07012
Secondary accession number(s): P76642, Q2M9V0
Entry historyiIntegrated into UniProtKB/Swiss-Prot: April 1, 1988
Last sequence update: November 1, 1997
Last modified: August 30, 2017
This is version 162 of the entry and version 3 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, 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