| Tag | Content |
|---|
| CPLM ID | CPLM-003555 |
UniProt Accession | |
Genbank Protein ID | |
Genbank Nucleotide ID | |
Protein Name | Peptidyl-prolyl cis-trans isomerase A |
Protein Synonyms/Alias | PPIase A; Cyclophilin A; Rotamase A |
Gene Name | ppiA |
Gene Synonyms/Alias | rot; rotA; b3363; JW3326 |
Created Date | July 27, 2013 |
Organism | Escherichia coli (strain K12) |
NCBI Taxa ID | 83333 |
Lysine Modification | Position | Peptide | Type | References |
|---|
| 120 | AMARTADKDSATSQF | acetylation | [1] | | 151 | FGYAVFGKVVKGMDV | acetylation | [1] | | 179 | PYQNVPSKPVVILSA | acetylation | [1] |
|
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 | PPIases accelerate the folding of proteins. It catalyzes the cis-trans isomerization of proline imidic peptide bonds in oligopeptides. |
Sequence Annotation | DOMAIN 27 188 PPIase cyclophilin-type. |
Keyword | 3D-structure; Complete proteome; Direct protein sequencing; Isomerase; Periplasm; Reference proteome; Rotamase; Signal. |
Sequence Source | UniProt (SWISSPROT/TrEMBL); GenBank; EMBL |
Protein Length | 190 AA |
Protein Sequence | MFKSTLAAMA AVFALSALSP AAMAAKGDPH VLLTTSAGNI ELELDKQKAP VSVQNFVDYV 60
NSGFYNNTTF HRVIPGFMIQ GGGFTEQMQQ KKPNPPIKNE ADNGLRNTRG TIAMARTADK 120
DSATSQFFIN VADNAFLDHG QRDFGYAVFG KVVKGMDVAD KISQVPTHDV GPYQNVPSKP 180
VVILSAKVLP 190 |
Gene Ontology | GO:0030288; C:outer membrane-bounded periplasmic space; IDA:EcoCyc. GO:0003755; F:peptidyl-prolyl cis-trans isomerase activity; IDA:EcoCyc. GO:0006457; P:protein folding; IEA:UniProtKB-KW. |
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Pfam | |
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PRINTS | |