Tag | Content |
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CPLM ID | CPLM-002925 |
UniProt Accession | |
Genbank Protein ID | |
Genbank Nucleotide ID | |
Protein Name | Co-chaperone protein HscB |
Protein Synonyms/Alias | Hsc20 |
Gene Name | hscB |
Gene Synonyms/Alias | yfhE; b2527; JW2511 |
Created Date | July 27, 2013 |
Organism | Escherichia coli (strain K12) |
NCBI Taxa ID | 83333 |
Lysine Modification | Position | Peptide | Type | References |
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35 | QRQYHPDKFASGSQA | acetylation | [1] | 119 | ARLESFIKRVKKMFD | acetylation | [1] | 156 | RKLRFLDKLRSSAEQ | acetylation | [1] | 167 | SAEQLEEKLLDF*** | 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 | Co-chaperone involved in the maturation of iron-sulfur cluster-containing proteins. Seems to help targeting proteins to be folded toward HscA. |
Sequence Annotation | DOMAIN 2 74 J. |
Keyword | 3D-structure; Chaperone; Complete proteome; Reference proteome. |
Sequence Source | UniProt (SWISSPROT/TrEMBL); GenBank; EMBL |
Protein Length | 171 AA |
Protein Sequence | MDYFTLFGLP ARYQLDTQAL SLRFQDLQRQ YHPDKFASGS QAEQLAAVQQ SATINQAWQT 60 LRHPLMRAEY LLSLHGFDLA SEQHTVRDTA FLMEQLELRE ELDEIEQAKD EARLESFIKR 120 VKKMFDTRHQ LMVEQLDNET WDAAADTVRK LRFLDKLRSS AEQLEEKLLD F 171 |
Gene Ontology | |
Interpro | |
Pfam | |
SMART | |
PROSITE | |
PRINTS | |