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Protein

Ribosome-recycling factor

Gene

frr

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

Functioni

Responsible for the release of ribosomes from messenger RNA at the termination of protein biosynthesis. May increase the efficiency of translation by recycling ribosomes from one round of translation to another.

GO - Molecular functioni

  • ribosomal large subunit binding Source: EcoCyc

GO - Biological processi

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

Keywords - Biological processi

Protein biosynthesis

Enzyme and pathway databases

BioCyciEcoCyc:EG10335-MONOMER.
ECOL316407:JW0167-MONOMER.

Names & Taxonomyi

Protein namesi
Recommended name:
Ribosome-recycling factorUniRule annotation
Short name:
RRFUniRule annotation
Alternative name(s):
Ribosome-releasing factorUniRule annotation
Gene namesi
Name:frrUniRule annotation
Synonyms:rrf
Ordered Locus Names:b0172, JW0167
OrganismiEscherichia coli (strain K12)
Taxonomic identifieri83333 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia
Proteomesi
  • UP000000318 Componenti: Chromosome
  • UP000000625 Componenti: Chromosome

Organism-specific databases

EcoGeneiEG10335. frr.

Subcellular locationi

GO - Cellular componenti

  • cytoplasm Source: EcoCyc
  • cytosol Source: EcoCyc
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 185185Ribosome-recycling factorPRO_0000167454Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei162 – 1621N6-acetyllysineUniRule annotation1 Publication

Keywords - PTMi

Acetylation

Proteomic databases

EPDiP0A805.
PaxDbiP0A805.
PRIDEiP0A805.

2D gel databases

SWISS-2DPAGEP0A805.

Interactioni

Binary interactionsi

WithEntry#Exp.IntActNotes
raiAP0AD494EBI-1114349,EBI-1129692
ycfPP0A8E12EBI-1114349,EBI-9129402

Protein-protein interaction databases

BioGridi4259750. 19 interactions.
DIPiDIP-48120N.
IntActiP0A805. 35 interactions.
MINTiMINT-1308979.
STRINGi511145.b0172.

Structurei

Secondary structure

1
185
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi3 – 2422Combined sources
Helixi34 – 374Combined sources
Beta strandi41 – 444Combined sources
Beta strandi47 – 504Combined sources
Helixi51 – 533Combined sources
Beta strandi55 – 617Combined sources
Beta strandi64 – 718Combined sources
Helixi72 – 743Combined sources
Helixi75 – 839Combined sources
Beta strandi92 – 10110Combined sources
Helixi107 – 14539Combined sources
Beta strandi146 – 1483Combined sources
Helixi150 – 18435Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1EK8X-ray2.30A1-185[»]
1ISEX-ray2.20A1-185[»]
1Y69X-ray3.3381-185[»]
1ZN0electron microscopy15.50A1-185[»]
1ZN1electron microscopy14.10A1-185[»]
2RDOelectron microscopy9.1081-185[»]
4V9CX-ray3.30CY1-185[»]
4V9DX-ray3.00AY2-183[»]
4WOIX-ray3.00AV1-185[»]
ProteinModelPortaliP0A805.
SMRiP0A805. Positions 1-185.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP0A805.

Family & Domainsi

Sequence similaritiesi

Belongs to the RRF family.UniRule annotation

Phylogenomic databases

eggNOGiENOG4108VCV. Bacteria.
COG0233. LUCA.
HOGENOMiHOG000040143.
InParanoidiP0A805.
KOiK02838.
OMAiVQPWEKK.
OrthoDBiEOG6SV5F9.
PhylomeDBiP0A805.

Family and domain databases

Gene3Di1.10.132.20. 1 hit.
HAMAPiMF_00040. RRF.
InterProiIPR002661. Ribosome_recyc_fac.
IPR023584. Ribosome_recyc_fac_dom.
[Graphical view]
PANTHERiPTHR20982. PTHR20982. 1 hit.
PfamiPF01765. RRF. 1 hit.
[Graphical view]
SUPFAMiSSF55194. SSF55194. 1 hit.
TIGRFAMsiTIGR00496. frr. 1 hit.

Sequencei

Sequence statusi: Complete.

P0A805-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MISDIRKDAE VRMDKCVEAF KTQISKIRTG RASPSLLDGI VVEYYGTPTP
60 70 80 90 100
LRQLASVTVE DSRTLKINVF DRSMSPAVEK AIMASDLGLN PNSAGSDIRV
110 120 130 140 150
PLPPLTEERR KDLTKIVRGE AEQARVAVRN VRRDANDKVK ALLKDKEISE
160 170 180
DDDRRSQDDV QKLTDAAIKK IEAALADKEA ELMQF
Length:185
Mass (Da):20,639
Last modified:June 7, 2005 - v1
Checksum:iCBFB9675AAD0CFD8
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
J05113 Genomic DNA. Translation: AAA24607.1.
D13334 Genomic DNA. Translation: BAA02599.1.
U70214 Genomic DNA. Translation: AAB08601.1.
U00096 Genomic DNA. Translation: AAC73283.1.
AP009048 Genomic DNA. Translation: BAB96748.1.
M69029 Genomic DNA. No translation available.
PIRiA34495.
RefSeqiNP_414714.1. NC_000913.3.
WP_000622418.1. NZ_LN832404.1.

Genome annotation databases

EnsemblBacteriaiAAC73283; AAC73283; b0172.
BAB96748; BAB96748; BAB96748.
GeneIDi946122.
KEGGiecj:JW0167.
eco:b0172.
PATRICi32115453. VBIEscCol129921_0178.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
J05113 Genomic DNA. Translation: AAA24607.1.
D13334 Genomic DNA. Translation: BAA02599.1.
U70214 Genomic DNA. Translation: AAB08601.1.
U00096 Genomic DNA. Translation: AAC73283.1.
AP009048 Genomic DNA. Translation: BAB96748.1.
M69029 Genomic DNA. No translation available.
PIRiA34495.
RefSeqiNP_414714.1. NC_000913.3.
WP_000622418.1. NZ_LN832404.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1EK8X-ray2.30A1-185[»]
1ISEX-ray2.20A1-185[»]
1Y69X-ray3.3381-185[»]
1ZN0electron microscopy15.50A1-185[»]
1ZN1electron microscopy14.10A1-185[»]
2RDOelectron microscopy9.1081-185[»]
4V9CX-ray3.30CY1-185[»]
4V9DX-ray3.00AY2-183[»]
4WOIX-ray3.00AV1-185[»]
ProteinModelPortaliP0A805.
SMRiP0A805. Positions 1-185.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi4259750. 19 interactions.
DIPiDIP-48120N.
IntActiP0A805. 35 interactions.
MINTiMINT-1308979.
STRINGi511145.b0172.

2D gel databases

SWISS-2DPAGEP0A805.

Proteomic databases

EPDiP0A805.
PaxDbiP0A805.
PRIDEiP0A805.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAC73283; AAC73283; b0172.
BAB96748; BAB96748; BAB96748.
GeneIDi946122.
KEGGiecj:JW0167.
eco:b0172.
PATRICi32115453. VBIEscCol129921_0178.

Organism-specific databases

EchoBASEiEB0331.
EcoGeneiEG10335. frr.

Phylogenomic databases

eggNOGiENOG4108VCV. Bacteria.
COG0233. LUCA.
HOGENOMiHOG000040143.
InParanoidiP0A805.
KOiK02838.
OMAiVQPWEKK.
OrthoDBiEOG6SV5F9.
PhylomeDBiP0A805.

Enzyme and pathway databases

BioCyciEcoCyc:EG10335-MONOMER.
ECOL316407:JW0167-MONOMER.

Miscellaneous databases

EvolutionaryTraceiP0A805.
PROiP0A805.

Family and domain databases

Gene3Di1.10.132.20. 1 hit.
HAMAPiMF_00040. RRF.
InterProiIPR002661. Ribosome_recyc_fac.
IPR023584. Ribosome_recyc_fac_dom.
[Graphical view]
PANTHERiPTHR20982. PTHR20982. 1 hit.
PfamiPF01765. RRF. 1 hit.
[Graphical view]
SUPFAMiSSF55194. SSF55194. 1 hit.
TIGRFAMsiTIGR00496. frr. 1 hit.
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Molecular cloning and expression of ribosome releasing factor."
    Ichikawa S., Kaji A.
    J. Biol. Chem. 264:20054-20059(1989) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], PARTIAL PROTEIN SEQUENCE.
    Strain: MRE-600.
  2. "Identification and characterization of the smbA gene, a suppressor of the mukB null mutant of Escherichia coli."
    Yamanaka K., Ogura T., Niki H., Hiraga S.
    J. Bacteriol. 174:7517-7526(1992) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  3. "Systematic sequencing of the Escherichia coli genome: analysis of the 2.4-4.1 min (110,917-193,643 bp) region."
    Fujita N., Mori H., Yura T., Ishihama A.
    Nucleic Acids Res. 22:1637-1639(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
  4. "Systematic sequencing of the Escherichia coli genome: analysis of the 4.0 - 6.0 min (189,987 - 281,416bp) region."
    Takemoto K., Mori H., Murayama N., Kataoka K., Yano M., Itoh T., Yamamoto Y., Inokuchi H., Miki T., Hatada E., Fukuda R., Ichihara S., Mizuno T., Makino K., Nakata A., Yura T., Sampei G., Mizobuchi K.
    Submitted (FEB-1996) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
  5. "Sequence of minutes 4-25 of Escherichia coli."
    Chung E., Allen E., Araujo R., Aparicio A.M., Davis K., Duncan M., Federspiel N., Hyman R., Kalman S., Komp C., Kurdi O., Lew H., Lin D., Namath A., Oefner P., Roberts D., Schramm S., Davis R.W.
    Submitted (JAN-1997) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: K12 / MG1655 / ATCC 47076.
  6. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: K12 / MG1655 / ATCC 47076.
  7. "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.
  8. "Comparing the predicted and observed properties of proteins encoded in the genome of Escherichia coli K-12."
    Link A.J., Robison K., Church G.M.
    Electrophoresis 18:1259-1313(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 1-12.
    Strain: K12 / EMG2.
  9. Cited for: PROTEIN SEQUENCE OF 1-11.
    Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
  10. "Identification of the promoter region of the ribosome-releasing factor cistron (frr)."
    Shimizu I., Kaji A.
    J. Bacteriol. 173:5181-5187(1991) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-5.
  11. "Ribosome recycling factor (ribosome releasing factor) is essential for bacterial growth."
    Janosi L., Shimizu I., Kaji A.
    Proc. Natl. Acad. Sci. U.S.A. 91:4249-4253(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: CHARACTERIZATION.
  12. "Lysine acetylation is a highly abundant and evolutionarily conserved modification in Escherichia coli."
    Zhang J., Sprung R., Pei J., Tan X., Kim S., Zhu H., Liu C.F., Grishin N.V., Zhao Y.
    Mol. Cell. Proteomics 8:215-225(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-162, IDENTIFICATION BY MASS SPECTROMETRY.
    Strain: K12 / JW1106 and K12 / MG1655 / ATCC 47076.
  13. "Visualization of ribosome-recycling factor on the Escherichia coli 70S ribosome: functional implications."
    Agrawal R.K., Sharma M.R., Kiel M.C., Hirokawa G., Booth T.M., Spahn C.M., Grassucci R.A., Kaji A., Frank J.
    Proc. Natl. Acad. Sci. U.S.A. 101:8900-8905(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: STRUCTURE BY ELECTRON MICROSCOPY (12.0 ANGSTROMS).

Entry informationi

Entry nameiRRF_ECOLI
AccessioniPrimary (citable) accession number: P0A805
Secondary accession number(s): P16174
Entry historyi
Integrated into UniProtKB/Swiss-Prot: June 7, 2005
Last sequence update: June 7, 2005
Last modified: March 16, 2016
This is version 103 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, 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

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.