| Tag | Content |
|---|
| CPLM ID | CPLM-007138 |
UniProt Accession | |
Genbank Protein ID | |
Genbank Nucleotide ID | |
Protein Name | Uncharacterized protein YjjU |
Protein Synonyms/Alias | |
Gene Name | yjjU |
Gene Synonyms/Alias | b4377; JW4340 |
Created Date | July 27, 2013 |
Organism | Escherichia coli (strain K12) |
NCBI Taxa ID | 83333 |
Lysine Modification | Position | Peptide | Type | References |
|---|
| 255 | DIQQFIEKPPGKLRI | acetylation | [1] | | 259 | FIEKPPGKLRIFEIY | acetylation | [1] | | 308 | VGKLLTEKAPLTRHL | 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 | Probable lipid hydrolase (By similarity). |
Sequence Annotation | DOMAIN 27 196 Patatin.
MOTIF 59 63 GXSXG.
ACT_SITE 61 61 By similarity. |
Keyword | Complete proteome; Hydrolase; Lipid degradation; Lipid metabolism; Reference proteome. |
Sequence Source | UniProt (SWISSPROT/TrEMBL); GenBank; EMBL |
Protein Length | 357 AA |
Protein Sequence | MGQRIPVTLG NIAPLSLRPF QPGRIALVCE GGGQRGIFTA GVLDEFMRAQ FNPFDLYLGT 60
SAGAQNLSAF ICNQPGYARK VIMRYTTKRE FFDPLRFVRG GNLIDLDWLV EATASQMPLQ 120
MDTAARLFDS GKSFYMCACR QDDYAPNYFL PTKQNWLDVI RASSAIPGFY RSGVSLEGIN 180
YLDGGISDAI PVKEAARQGA KTLVVIRTVP SQMYYTPQWF KRMERWLGDS SLQPLVNLVQ 240
HHETSYRDIQ QFIEKPPGKL RIFEIYPPKP LHSIALGSRI PALREDYKLG RLCGRYFLAT 300
VGKLLTEKAP LTRHLVPVVT PESIVIPPAP VANDTLVAEV SDAPQANDPT FNNEDLA 357 |
Gene Ontology | GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW. GO:0016042; P:lipid catabolic process; IEA:UniProtKB-KW. GO:0006974; P:response to DNA damage stimulus; IEP:EcoliWiki. |
Interpro | |
Pfam | |
SMART | |
PROSITE | |
PRINTS | |