P0AAR3 (YBAK_ECOLI) Reviewed, UniProtKB/Swiss-Prot
Last modified
January 25, 2012.
Version 57.
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: Cys-tRNA(Pro)/Cys-tRNA(Cys) deacylase ybaK | ||||
| Gene names |
| ||||
| Organism | Escherichia coli (strain K12) | ||||
| Taxonomic identifier | 83333 [NCBI] | ||||
| Taxonomic lineage | Bacteria › Proteobacteria › Gammaproteobacteria › Enterobacteriales › Enterobacteriaceae › Escherichia |
Protein attributes
| Sequence length | 159 AA. |
| Sequence status | Complete. |
| Protein existence | Evidence at protein level |
General annotation (Comments)
| Function | Functions in trans to edit the amino acid from incorrectly charged Cys-tRNA(Pro). May compensate for the lack of Cys-tRNA(Pro) editing by ProRS. Additionally serves as a general deacylase with weak activity against Cys-tRNA(Cys) and Gly-tRNA(Gly), as well as, at higher concentrations, some other correctly charged tRNAs. Unlike some of its orthologs it is not able to remove the amino acid moiety from incorrectly charged Ala-tRNA(Pro). |
| Subcellular location | Cytoplasm By similarity. |
| Disruption phenotype | Non-essential gene. Ref.8 |
| Miscellaneous | Has been suggested to be potentially involved in suppression of transcription of ushA. |
| Sequence similarities | Belongs to the prolyl-tRNA editing family. ProX subfamily. |
Ontologies
| Keywords | |
|---|---|
| Biological process | Transcription Transcription regulation |
| Cellular component | Cytoplasm |
| Technical term | 3D-structure Complete proteome Reference proteome |
| Gene Ontology (GO) | |
| Biological process | regulation of transcription, DNA-dependent Inferred from electronic annotation. Source: UniProtKB-KW transcription, DNA-dependentInferred from electronic annotation. Source: UniProtKB-KW |
| Cellular component | cytoplasm Inferred from electronic annotation. Source: UniProtKB-SubCell |
| Molecular function | aminoacyl-tRNA editing activity Inferred from direct assay Ref.8. Source: UniProtKB |
| Complete GO annotation... | |
Sequence annotation (Features)
| Feature key | Position(s) | Length | Description | Graphical view | Feature identifier | ||||||||||||||||||||||||||||||||||||
Molecule processing | |||||||||||||||||||||||||||||||||||||||||
|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|
| Chain | 1 – 159 | 159 | Cys-tRNA(Pro)/Cys-tRNA(Cys) deacylase ybaK | PRO_0000168620 | |||||||||||||||||||||||||||||||||||||
Secondary structure | |||||||||||||||||||||||||||||||||||||||||
Helix Strand Turn | |||||||||||||||||||||||||||||||||||||||||
| Helix | 3 – 10 | 8 | |||||||||||||||||||||||||||||||||||||||
| Beta strand | 16 – 19 | 4 | |||||||||||||||||||||||||||||||||||||||
| Helix | 32 – 37 | 6 | |||||||||||||||||||||||||||||||||||||||
| Turn | 41 – 43 | 3 | |||||||||||||||||||||||||||||||||||||||
| Beta strand | 44 – 52 | 9 | |||||||||||||||||||||||||||||||||||||||
| Beta strand | 55 – 65 | 11 | |||||||||||||||||||||||||||||||||||||||
| Beta strand | 68 – 70 | 3 | |||||||||||||||||||||||||||||||||||||||
| Helix | 72 – 79 | 8 | |||||||||||||||||||||||||||||||||||||||
| Beta strand | 84 – 86 | 3 | |||||||||||||||||||||||||||||||||||||||
| Helix | 89 – 96 | 8 | |||||||||||||||||||||||||||||||||||||||
| Beta strand | 105 – 107 | 3 | |||||||||||||||||||||||||||||||||||||||
| Beta strand | 114 – 117 | 4 | |||||||||||||||||||||||||||||||||||||||
| Helix | 118 – 122 | 5 | |||||||||||||||||||||||||||||||||||||||
| Beta strand | 126 – 132 | 7 | |||||||||||||||||||||||||||||||||||||||
| Beta strand | 135 – 139 | 5 | |||||||||||||||||||||||||||||||||||||||
| Helix | 141 – 148 | 8 | |||||||||||||||||||||||||||||||||||||||
| Beta strand | 151 – 153 | 3 | |||||||||||||||||||||||||||||||||||||||
Sequences
| ||||||||||||||||||
References
| « Hide 'large scale' references | |
| [1] | "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. |
| [2] | "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: 9278503] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: K12 / MG1655 / ATCC 47076. |
| [3] | "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: 16738553] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: K12 / W3110 / ATCC 27325 / DSM 5911. |
| [4] | "Nucleotide sequence and transcriptional analysis of the E. coli ushA gene, encoding periplasmic UDP-sugar hydrolase (5'-nucleotidase): regulation of the ushA gene, and the signal sequence of its encoded protein product." Burns D.M., Beacham I.R. Nucleic Acids Res. 14:4325-4342(1986) [PubMed: 3012467] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 149-159. |
| [5] | Jimenez S., Bairoch A. Unpublished observations (AUG-1994) Cited for: IDENTIFICATION. |
| [6] | "Enrichment of low abundance proteins of Escherichia coli by hydroxyapatite chromatography." Fountoulakis M., Takacs M.-F., Berndt P., Langen H., Takacs B. Electrophoresis 20:2181-2195(1999) [PubMed: 10493123] [Abstract] Cited for: IDENTIFICATION BY MASS SPECTROMETRY. Strain: B / BL21. |
| [7] | "Trans-editing of mischarged tRNAs." Ahel I., Korencic D., Ibba M., Soll D. Proc. Natl. Acad. Sci. U.S.A. 100:15422-15427(2003) [PubMed: 14663147] [Abstract] Cited for: LACK OF EDITING ACTIVITY ON MISCHARGED ALA-TRNA(PRO). |
| [8] | "The bacterial YbaK protein is a Cys-tRNAPro and Cys-tRNA Cys deacylase." Ruan B., Soll D. J. Biol. Chem. 280:25887-25891(2005) [PubMed: 15886196] [Abstract] Cited for: CHARACTERIZATION OF GENERAL DEACYLASE ACTIVITY, DISRUPTION PHENOTYPE. |
| [9] | "Crystal structure of trans editing enzyme ProX from E.coli." RIKEN structural genomics initiative (RSGI) Submitted (FEB-2009) to the PDB data bank Cited for: X-RAY CRYSTALLOGRAPHY (1.58 ANGSTROMS). |
| + | Additional computationally mapped references. |
Cross-references
Sequence databases | |||||||||||||
|---|---|---|---|---|---|---|---|---|---|---|---|---|---|
| EMBL GenBank DDBJ | U82664 Genomic DNA. Translation: AAB40235.1. U00096 Genomic DNA. Translation: AAC73583.1. AP009048 Genomic DNA. Translation: BAE76260.1. X03895 Genomic DNA. No translation available. | ||||||||||||
| PIR | H64778. | ||||||||||||
| RefSeq | NP_415014.1. NC_000913.2. | ||||||||||||
3D structure databases | |||||||||||||
| PDBe RCSB PDB PDBj |
| ||||||||||||
| ProteinModelPortal | P0AAR3. | ||||||||||||
| SMR | P0AAR3. Positions 1-158. | ||||||||||||
| ModBase | Search... | ||||||||||||
Protein-protein interaction databases | |||||||||||||
| DIP | DIP-48133N. | ||||||||||||
| IntAct | P0AAR3. 17 interactions. | ||||||||||||
| MINT | MINT-1228144. | ||||||||||||
Protocols and materials databases | |||||||||||||
| StructuralBiologyKnowledgebase | Search... | ||||||||||||
Genome annotation databases | |||||||||||||
| EnsemblBacteria | EBESCT00000003221; EBESCP00000003221; EBESCG00000002646. EBESCT00000016125; EBESCP00000015416; EBESCG00000015185. | ||||||||||||
| GeneID | 947083. | ||||||||||||
| GenomeReviews | Gene locus JW0470 in contig AP009048_GR. Gene locus b0481 in contig U00096_GR. | ||||||||||||
| KEGG | ecj:JW0470. eco:b0481. | ||||||||||||
| PATRIC | 32116119. VBIEscCol129921_0501. | ||||||||||||
Organism-specific databases | |||||||||||||
| EchoBASE | EB2348. | ||||||||||||
| EcoGene | EG12454. ybaK. | ||||||||||||
Phylogenomic databases | |||||||||||||
| eggNOG | COG2606. | ||||||||||||
| GeneTree | EBGT00050000011115. | ||||||||||||
| HOGENOM | HBG727700. | ||||||||||||
| OMA | VSPLGQK. | ||||||||||||
| PhylomeDB | P0AAR3. | ||||||||||||
| ProtClustDB | PRK10670. | ||||||||||||
Enzyme and pathway databases | |||||||||||||
| BioCyc | EcoCyc:EG12454-MONOMER. | ||||||||||||
Gene expression databases | |||||||||||||
| Genevestigator | P0AAR3. | ||||||||||||
Family and domain databases | |||||||||||||
| InterPro | IPR004369. Prolyl-tRNA_editing_YbaK/EbsC. IPR007214. YbaK/aa-tRNA-synth-assoc-dom. [Graphical view] | ||||||||||||
| Gene3D | G3DSA:3.90.960.10. YbaK/aa-tRNA-synth-assoc-reg. 1 hit. | ||||||||||||
| Pfam | PF04073. YbaK. 1 hit. [Graphical view] | ||||||||||||
| SUPFAM | SSF55826. YbaK/aa-tRNA-synth-assoc-reg. 1 hit. | ||||||||||||
| TIGRFAMs | TIGR00011. YbaK_EbsC. 1 hit. | ||||||||||||
| ProtoNet | Search... | ||||||||||||
Entry information
| Entry name | YBAK_ECOLI | ||||||||
| Accession | Primary (citable) accession number: P0AAR3 Secondary accession number(s): P37175, P77281, Q2MBU6 | ||||||||
| 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