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Protein

Peptide chain release factor RF2

Gene

prfB

Organism
Thermus thermophilus (strain HB8 / ATCC 27634 / DSM 579)
Status
Reviewed-Annotation score: Annotation score: 3 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 (Probable). In endogenous ribosomes interacts with P-site tRNA and 23S rRNA (PubMed:18988853, PubMed:20421507). 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 (By similarity). Recruited to stalled E.coli 70S ribosomes by E.coli ArfA, but cannot be functionally accomodated in the peptidyl-transferase center (PubMed:27934701, PubMed:28077875). Note T.thermophilus probably does not encode arfA (Ref. 1).By similarity2 Publications4 Publications

GO - Molecular functioni

Keywordsi

Molecular functionRNA-binding, rRNA-binding, tRNA-binding
Biological processProtein biosynthesis

Enzyme and pathway databases

BioCyciTTHE300852:GH8R-149-MONOMER.

Names & Taxonomyi

Protein namesi
Recommended name:
Peptide chain release factor RF2
Gene namesi
Name:prfB
Ordered Locus Names:TTHA0142
OrganismiThermus thermophilus (strain HB8 / ATCC 27634 / DSM 579)
Taxonomic identifieri300852 [NCBI]
Taxonomic lineageiBacteriaDeinococcus-ThermusDeinococciThermalesThermaceaeThermus
Proteomesi
  • UP000000532 Componenti: Chromosome

Subcellular locationi

Q5SM01:

GO - Cellular componenti

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00004397551 – 378Peptide chain release factor RF2Add BLAST378

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei253N5-methylglutamine1 Publication1

Keywords - PTMi

Methylation

PTM databases

iPTMnetiQ5SM01.

Interactioni

Subunit structurei

Interacts with the ribosome (PubMed:16377566, PubMed:17272297, PubMed:18988853, PubMed:20421507). Interacts with ribosomal protein L11 (PubMed:18988853). Recruited to stalled E.coli ribosomes by E.coli ArfA (PubMed:27934701, PubMed:28077875).1 Publication5 Publications

Protein-protein interaction databases

STRINGi300852.TTHA0142.

Structurei

Secondary structure

1378
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi29 – 31Combined sources3
Helixi32 – 39Combined sources8
Turni40 – 44Combined sources5
Helixi49 – 51Combined sources3
Turni52 – 54Combined sources3
Helixi55 – 57Combined sources3
Beta strandi58 – 60Combined sources3
Helixi63 – 67Combined sources5
Helixi69 – 81Combined sources13
Turni82 – 84Combined sources3
Helixi85 – 88Combined sources4
Helixi97 – 99Combined sources3
Helixi101 – 103Combined sources3
Helixi105 – 119Combined sources15
Beta strandi122 – 124Combined sources3
Beta strandi127 – 135Combined sources9
Helixi140 – 158Combined sources19
Turni159 – 161Combined sources3
Beta strandi163 – 171Combined sources9
Beta strandi173 – 186Combined sources14
Helixi189 – 193Combined sources5
Helixi194 – 196Combined sources3
Beta strandi198 – 205Combined sources8
Beta strandi209 – 211Combined sources3
Beta strandi214 – 226Combined sources13
Beta strandi229 – 232Combined sources4
Helixi237 – 239Combined sources3
Beta strandi240 – 245Combined sources6
Helixi255 – 257Combined sources3
Beta strandi260 – 266Combined sources7
Turni267 – 269Combined sources3
Beta strandi272 – 275Combined sources4
Beta strandi277 – 279Combined sources3
Helixi281 – 307Combined sources27
Turni308 – 312Combined sources5
Beta strandi324 – 328Combined sources5
Helixi329 – 331Combined sources3
Beta strandi333 – 336Combined sources4
Turni337 – 339Combined sources3
Beta strandi342 – 344Combined sources3
Helixi346 – 349Combined sources4
Turni350 – 352Combined sources3
Helixi355 – 366Combined sources12

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
2IHRX-ray2.50127-378[»]
4V4SX-ray6.76AY28-378[»]
4V5EX-ray3.45AY/CY31-369[»]
4V5JX-ray3.10AY/CY31-369[»]
5MDYelectron microscopy3.3571-378[»]
ProteinModelPortaliQ5SM01.
SMRiQ5SM01.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ5SM01.

Family & Domainsi

Sequence similaritiesi

Phylogenomic databases

eggNOGiENOG4105CG1. Bacteria.
COG1186. LUCA.
HOGENOMiHOG000074814.
KOiK02836.
OMAiYVFHPYQ.
PhylomeDBiQ5SM01.

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.
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.

Q5SM01-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MRLASQSAIL VKVWTWNASR NAWKASGGIF DIPQKETRLK ELERRLEDPS
60 70 80 90 100
LWNDPEAARK VSQEAARLRR TVDTFRSLES DLQGLLELME ELPAEEREAL
110 120 130 140 150
KPELEEAAKK LDELYHQTLL NFPHAEKNAI LTIQPGAGGT EACDWAEMLL
160 170 180 190 200
RMYTRFAERQ GFQVEVVDLT PGPEAGIDYA QILVKGENAY GLLSPEAGVH
210 220 230 240 250
RLVRPSPFDA SGRRHTSFAG VEVIPEVDEE VEVVLKPEEL RIDVMRASGP
260 270 280 290 300
GGQGVNTTDS AVRVVHLPTG ITVTCQTTRS QIKNKELALK ILKARLYELE
310 320 330 340 350
RKKREEELKA LRGEVRPIEW GSQIRSYVLD KNYVKDHRTG LMRHDPENVL
360 370
DGDLMDLIWA GLEWKAGRRQ GTEEVEAE
Length:378
Mass (Da):42,734
Last modified:December 21, 2004 - v1
Checksum:i55B4AC9C891AEEB7
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AP008226 Genomic DNA. Translation: BAD69965.1.
RefSeqiWP_011174207.1. NC_006461.1.
YP_143408.1. NC_006461.1.

Genome annotation databases

EnsemblBacteriaiBAD69965; BAD69965; BAD69965.
GeneIDi3168831.
KEGGittj:TTHA0142.
PATRICifig|300852.9.peg.140.

Similar proteinsi

Entry informationi

Entry nameiRF2_THET8
AccessioniPrimary (citable) accession number: Q5SM01
Entry historyiIntegrated into UniProtKB/Swiss-Prot: May 10, 2017
Last sequence update: December 21, 2004
Last modified: October 25, 2017
This is version 97 of the entry and version 1 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. SIMILARITY comments
    Index of protein domains and families