P40711 (ARFB_ECOLI) Reviewed, UniProtKB/Swiss-Prot
Last modified
May 1, 2013.
Version 87.
History...
Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order
Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize orderNames and origin
| Protein names | Recommended name: Peptidyl-tRNA hydrolase YaeJ Short name=PTH EC=3.1.1.29 Alternative name(s): Alternative ribosome-rescue factor B | ||||
| Gene names |
| ||||
| Organism | Escherichia coli (strain K12) [Reference proteome] [HAMAP] | ||||
| Taxonomic identifier | 83333 [NCBI] | ||||
| Taxonomic lineage | Bacteria › Proteobacteria › Gammaproteobacteria › Enterobacteriales › Enterobacteriaceae › Escherichia › ![]() |
Protein attributes
| Sequence length | 140 AA. |
| Sequence status | Complete. |
| Protein existence | Evidence at protein level |
General annotation (Comments)
| Function | Rescues stalled ribosomes. Can hydrolyze peptidyl-tRNA on ribosomes stalled by both non-stop mRNAs and mRNAs that contain rare codon clusters. May function as a complementary rescue system when the stalled ribosome can not be rescued by the SsrA(tmRNA)-SmpB quality control system or the alternative ribosome-rescue factor A. Ref.8 Ref.9 |
| Catalytic activity | N-substituted aminoacyl-tRNA + H2O = N-substituted amino acid + tRNA. Ref.8 Ref.9 |
| Subunit structure | Associated with 70S ribosomes and polysomes. |
| Subcellular location | Cytoplasm Probable. |
| Domain | The unstructured C-terminal region is required for ribosome binding and peptidyl-tRNA hydrolase activity. Ref.8 Ref.9 |
| Sequence similarities | Belongs to the prokaryotic/mitochondrial release factor family. |
Ontologies
| Keywords | |
|---|---|
| Biological process | Translation regulation |
| Cellular component | Cytoplasm |
| Molecular function | Hydrolase |
| Technical term | 3D-structure Complete proteome Reference proteome |
| Gene Ontology (GO) | |
| Biological_process | rescue of stalled ribosome Inferred from direct assay Ref.9Ref.8. Source: EcoCyc |
| Cellular_component | cytoplasm Inferred from electronic annotation. Source: UniProtKB-SubCell |
| Molecular_function | aminoacyl-tRNA hydrolase activity Inferred from direct assay Ref.9Ref.8. Source: EcoCyc ribosome bindingInferred from direct assay Ref.8. Source: EcoCyc translation release factor activityInferred from electronic annotation. Source: InterPro |
| Complete GO annotation... | |
Sequence annotation (Features)
| Feature key | Position(s) | Length | Description | Graphical view | Feature identifier | ||||||||||||||||||||||||
Molecule processing | |||||||||||||||||||||||||||||
|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|
| Chain | 1 – 140 | 140 | Peptidyl-tRNA hydrolase YaeJ | PRO_0000166858 | |||||||||||||||||||||||||
Experimental info | |||||||||||||||||||||||||||||
| Mutagenesis | 26 – 27 | 2 | GG → VA: Strong decrease in activity. Ref.8 Ref.9 | ||||||||||||||||||||||||||
| Mutagenesis | 27 – 28 | 2 | GQ → AE: Strong decrease in activity. Ref.8 Ref.9 | ||||||||||||||||||||||||||
| Mutagenesis | 27 | 1 | G → A: Decrease in activity. Ref.8 Ref.9 | ||||||||||||||||||||||||||
| Mutagenesis | 28 | 1 | Q → E: Decrease in activity. Ref.9 | ||||||||||||||||||||||||||
Secondary structure | |||||||||||||||||||||||||||||
Helix Strand Turn | |||||||||||||||||||||||||||||
| Beta strand | 6 – 8 | 3 | |||||||||||||||||||||||||||
| Beta strand | 15 – 20 | 6 | |||||||||||||||||||||||||||
| Beta strand | 24 – 27 | 4 | |||||||||||||||||||||||||||
| Helix | 28 – 31 | 4 | |||||||||||||||||||||||||||
| Beta strand | 37 – 41 | 5 | |||||||||||||||||||||||||||
| Beta strand | 44 – 48 | 5 | |||||||||||||||||||||||||||
| Helix | 51 – 57 | 7 | |||||||||||||||||||||||||||
| Beta strand | 72 – 74 | 3 | |||||||||||||||||||||||||||
| Helix | 80 – 99 | 20 | |||||||||||||||||||||||||||
| Turn | 113 – 115 | 3 | |||||||||||||||||||||||||||
| Helix | 116 – 128 | 13 | |||||||||||||||||||||||||||
Sequences
| ||||||||||||||||||
References
| « Hide 'large scale' references | |
| [1] | "Identification of cutC and cutF (nlpE) genes involved in copper tolerance in Escherichia coli." Gupta S.D., Lee B.T.O., Camakaris J., Wu H.C. J. Bacteriol. 177:4207-4215(1995) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: K12 / MC4100 / ATCC 35695 / DSM 6574. |
| [2] | Yamamoto Y. Submitted (DEC-1995) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: K12 / W3110 / ATCC 27325 / DSM 5911. |
| [3] | "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. |
| [4] | "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. |
| [5] | "The complete genome sequence of Escherichia coli K-12." 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. Science 277:1453-1474(1997) [PubMed] [Europe PMC] [Abstract] 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], SEQUENCE REVISION TO 36. Strain: K12 / W3110 / ATCC 27325 / DSM 5911. |
| [7] | "Overproduction of NlpE, a new outer membrane lipoprotein, suppresses the toxicity of periplasmic LacZ by activation of the Cpx signal transduction pathway." Snyder W.B., Davis L.J., Danese P.N., Cosma C.L., Silhavy T.J. J. Bacteriol. 177:4216-4223(1995) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 17-140. Strain: K12 / MC4100 / ATCC 35695 / DSM 6574. |
| [8] | "Escherichia coli YaeJ protein mediates a novel ribosome-rescue pathway distinct from SsrA- and ArfA-mediated pathways." Chadani Y., Ono K., Kutsukake K., Abo T. Mol. Microbiol. 80:772-785(2011) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION, CATALYTIC ACTIVITY, INTERACTION WITH RIBOSOMES, DOMAIN, MUTAGENESIS OF GLY-27. Strain: K12. |
| [9] | "YaeJ is a novel ribosome-associated protein in Escherichia coli that can hydrolyze peptidyl-tRNA on stalled ribosomes." Handa Y., Inaho N., Nameki N. Nucleic Acids Res. 39:1739-1748(2011) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION, CATALYTIC ACTIVITY, INTERACTION WITH RIBOSOMES, DOMAIN, MUTAGENESIS OF 26-GLY-GLY-27; 27-GLY-GLN-28; GLY-27 AND GLN-28. Strain: K12. |
| + | Additional computationally mapped references. |
Cross-references
Sequence databases | |||||||||||||
|---|---|---|---|---|---|---|---|---|---|---|---|---|---|
| EMBL GenBank DDBJ | L38619 Genomic DNA. Translation: AAA82971.1. D49445 Genomic DNA. Translation: BAA08432.1. U70214 Genomic DNA. Translation: AAB08619.1. U00096 Genomic DNA. Translation: AAC73302.1. AP009048 Genomic DNA. Translation: BAA77867.2. U18345 Genomic DNA. Translation: AAA86092.1. | ||||||||||||
| PIR | G64743. | ||||||||||||
| RefSeq | NP_414733.1. NC_000913.2. YP_488494.1. NC_007779.1. | ||||||||||||
3D structure databases | |||||||||||||
| PDBe RCSB PDB PDBj |
| ||||||||||||
| ProteinModelPortal | P40711. | ||||||||||||
| SMR | P40711. Positions 2-133. | ||||||||||||
| ModBase | Search... | ||||||||||||
Protein-protein interaction databases | |||||||||||||
| IntAct | P40711. 8 interactions. | ||||||||||||
| STRING | 511145.b0191. | ||||||||||||
Proteomic databases | |||||||||||||
| PaxDb | P40711. | ||||||||||||
| PRIDE | P40711. | ||||||||||||
Protocols and materials databases | |||||||||||||
| StructuralBiologyKnowledgebase | Search... | ||||||||||||
Genome annotation databases | |||||||||||||
| EnsemblBacteria | AAC73302; AAC73302; b0191. BAA77867; BAA77867; BAA77867. | ||||||||||||
| GeneID | 12934377. 946046. | ||||||||||||
| KEGG | ecj:Y75_p0188. eco:b0191. | ||||||||||||
| PATRIC | 32115495. VBIEscCol129921_0199. | ||||||||||||
Organism-specific databases | |||||||||||||
| EchoBASE | EB2258. | ||||||||||||
| EcoGene | EG12354. yaeJ. | ||||||||||||
Phylogenomic databases | |||||||||||||
| eggNOG | COG1186. | ||||||||||||
| HOGENOM | HOG000244440. | ||||||||||||
| KO | K15034. | ||||||||||||
| OMA | VLIIKAQ. | ||||||||||||
| ProtClustDB | PRK09256. | ||||||||||||
Enzyme and pathway databases | |||||||||||||
| BioCyc | EcoCyc:EG12354-MONOMER. ECOL316407:JW0187-MONOMER. MetaCyc:EG12354-MONOMER. | ||||||||||||
Gene expression databases | |||||||||||||
| Genevestigator | P40711. | ||||||||||||
Family and domain databases | |||||||||||||
| InterPro | IPR000352. Pep_chain_release_fac_I_II. [Graphical view] | ||||||||||||
| Pfam | PF00472. RF-1. 1 hit. [Graphical view] | ||||||||||||
| PROSITE | PS00745. RF_PROK_I. 1 hit. [Graphical view] | ||||||||||||
| ProtoNet | Search... | ||||||||||||
Entry information
| Entry name | ARFB_ECOLI | ||||||||
| Accession | Primary (citable) accession number: P40711 | ||||||||
| Entry history |
| ||||||||
| Entry status | Reviewed (UniProtKB/Swiss-Prot) | ||||||||
| Annotation program | Prokaryotic Protein Annotation Program | ||||||||
Relevant documents
| Escherichia coli Escherichia coli (strain K12): entries and cross-references to EcoGene |
| PDB cross-references Index of Protein Data Bank (PDB) cross-references |
| SIMILARITY comments Index of protein domains and families |

Clusters with
