Tag | Content |
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CPLM ID | CPLM-002992 |
UniProt Accession | |
Genbank Protein ID | |
Genbank Nucleotide ID | |
Protein Name | Peptidyl-tRNA hydrolase |
Protein Synonyms/Alias | PTH |
Gene Name | pth |
Gene Synonyms/Alias | b1204; JW1195 |
Created Date | July 27, 2013 |
Organism | Escherichia coli (strain K12) |
NCBI Taxa ID | 83333 |
Lysine Modification | Position | Peptide | Type | References |
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44 | APLREEAKFFGYTSR | acetylation | [1] | 104 | DLPPGVAKFKLGGGH | acetylation | [1] | 106 | PPGVAKFKLGGGHGG | acetylation | [1] | 118 | HGGHNGLKDIISKLG | acetylation | [1] | 123 | GLKDIISKLGNNPNF | acetylation | [1] | 153 | VVGFVLGKPPVSEQK | acetylation | [1] | 160 | KPPVSEQKLIDEAID | acetylation | [1] |
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Reference | [1] Acetyl-Phosphate Is a Critical Determinant of Lysine Acetylation in E. coli. Weinert BT, Iesmantavicius V, Wagner SA, Schölz C, Gummesson B, Beli P, Nyström T, Choudhary C. Mol Cell. 2013 Jul 25;51(2):265-72. [ PMID: 23830618] |
Functional Description | The natural substrate for this enzyme may be peptidyl- tRNAs which drop off the ribosome during protein synthesis. Involved in lambda inhibition of host protein synthesis. PTH activity may, directly or indirectly, be the target for lambda bar RNA leading to rap cell death. |
Sequence Annotation | |
Keyword | 3D-structure; Complete proteome; Cytoplasm; Direct protein sequencing; Hydrolase; Reference proteome. |
Sequence Source | UniProt (SWISSPROT/TrEMBL); GenBank; EMBL |
Protein Length | 194 AA |
Protein Sequence | MTIKLIVGLA NPGAEYAATR HNAGAWFVDL LAERLRAPLR EEAKFFGYTS RVTLGGEDVR 60 LLVPTTFMNL SGKAVAAMAS FFRINPDEIL VAHDELDLPP GVAKFKLGGG HGGHNGLKDI 120 ISKLGNNPNF HRLRIGIGHP GDKNKVVGFV LGKPPVSEQK LIDEAIDEAA RCTEMWFTDG 180 LTKATNRLHA FKAQ 194 |
Gene Ontology | GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. GO:0004045; F:aminoacyl-tRNA hydrolase activity; IDA:EcoCyc. GO:0006515; P:misfolded or incompletely synthesized protein catabolic process; IDA:EcoCyc. |
Interpro | |
Pfam | |
SMART | |
PROSITE | |
PRINTS | |