Tag | Content |
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CPLM ID | CPLM-003446 |
UniProt Accession | |
Genbank Protein ID | |
Genbank Nucleotide ID | |
Protein Name | Putative peroxiredoxin bcp |
Protein Synonyms/Alias | Bacterioferritin comigratory protein; Thioredoxin reductase |
Gene Name | bcp |
Gene Synonyms/Alias | b2480; JW2465 |
Created Date | July 27, 2013 |
Organism | Escherichia coli (strain K12) |
NCBI Taxa ID | 83333 |
Lysine Modification | Position | Peptide | Type | References |
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12 | KAGDIAPKFSLPDQD | acetylation | [1] | 40 | VLVYFYPKAMTPGCT | acetylation | [1] | 61 | RDNMDELKKAGVDVL | acetylation | [1] | 62 | DNMDELKKAGVDVLG | acetylation | [1] | 74 | VLGISTDKPEKLSRF | acetylation | [1] | 77 | ISTDKPEKLSRFAEK | acetylation | [1] | 114 | GEKSFMGKTYDGIHR | acetylation | [1] | 131 | FLIDADGKIEHVFDD | acetylation | [1] | 140 | EHVFDDFKTSNHHDV | acetylation | [1] | 153 | DVVLNWLKEHA**** | 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 | |
Sequence Annotation | DOMAIN 4 156 Thioredoxin. ACT_SITE 46 46 Cysteine sulfenic acid (-SOH) |
Keyword | Complete proteome; Direct protein sequencing; Oxidoreductase; Peroxidase; Redox-active center; Reference proteome. |
Sequence Source | UniProt (SWISSPROT/TrEMBL); GenBank; EMBL |
Protein Length | 156 AA |
Protein Sequence | MNPLKAGDIA PKFSLPDQDG EQVNLTDFQG QRVLVYFYPK AMTPGCTVQA CGLRDNMDEL 60 KKAGVDVLGI STDKPEKLSR FAEKELLNFT LLSDEDHQVC EQFGVWGEKS FMGKTYDGIH 120 RISFLIDADG KIEHVFDDFK TSNHHDVVLN WLKEHA 156 |
Gene Ontology | GO:0032843; F:hydroperoxide reductase activity; IDA:EcoCyc. GO:0008379; F:thioredoxin peroxidase activity; IDA:EcoCyc. GO:0006979; P:response to oxidative stress; IMP:EcoCyc. |
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PRINTS | |