CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-003291
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Bacterioferritin 
Protein Synonyms/Alias
 BFR; Cytochrome b-1; Cytochrome b-557 
Gene Name
 bfr 
Gene Synonyms/Alias
 b3336; JW3298 
Created Date
 July 27, 2013 
Organism
 Escherichia coli (strain K12) 
NCBI Taxa ID
 83333 
Lysine Modification
Position
Peptide
Type
References
2******MKGDTKVINacetylation[1]
6**MKGDTKVINYLNKacetylation[1]
33FLHARMFKNWGLKRLacetylation[1]
38MFKNWGLKRLNDVEYacetylation[1]
53HESIDEMKHADRYIEacetylation[1]
99ALELDGAKNLREAIGacetylation[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
 Iron-storage protein, whose ferroxidase center binds Fe(2+) ions, oxidizes them by dioxygen to Fe(3+), and participates in the subsequent Fe(3+) oxide mineral core formation within the central cavity of the protein complex. The mineralized iron core can contain as many as 2700 iron atoms/24-meric molecule. 
Sequence Annotation
 DOMAIN 1 145 Ferritin-like diiron.
 METAL 18 18 Iron 1.
 METAL 46 46 Iron 3.
 METAL 50 50 Iron 3.
 METAL 51 51 Iron 1.
 METAL 51 51 Iron 2.
 METAL 52 52 Iron (heme axial ligand); shared with
 METAL 54 54 Iron 1.
 METAL 94 94 Iron 2.
 METAL 127 127 Iron 1.
 METAL 127 127 Iron 2.
 METAL 130 130 Iron 2.  
Keyword
 3D-structure; Complete proteome; Direct protein sequencing; Heme; Iron; Iron storage; Metal-binding; Oxidoreductase; Reference proteome. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 158 AA 
Protein Sequence
MKGDTKVINY LNKLLGNELV AINQYFLHAR MFKNWGLKRL NDVEYHESID EMKHADRYIE 60
RILFLEGLPN LQDLGKLNIG EDVEEMLRSD LALELDGAKN LREAIGYADS VHDYVSRDMM 120
IEILRDEEGH IDWLETELDL IQKMGLQNYL QAQIREEG 158 
Gene Ontology
 GO:0005829; C:cytosol; IDA:UniProtKB.
 GO:0016020; C:membrane; IDA:UniProtKB.
 GO:0008199; F:ferric iron binding; IEA:InterPro.
 GO:0004322; F:ferroxidase activity; IEA:EC.
 GO:0005506; F:iron ion binding; IDA:EcoCyc.
 GO:0016491; F:oxidoreductase activity; NAS:EcoliWiki.
 GO:0006880; P:intracellular sequestering of iron ion; IDA:EcoCyc.
 GO:0006826; P:iron ion transport; IEA:InterPro. 
Interpro
 IPR002024; Bacterioferritin.
 IPR009040; Ferritin-like_diiron.
 IPR009078; Ferritin-like_SF.
 IPR012347; Ferritin-rel.
 IPR008331; Ferritin_DPS_dom. 
Pfam
 PF00210; Ferritin 
SMART
  
PROSITE
 PS00549; BACTERIOFERRITIN
 PS50905; FERRITIN_LIKE 
PRINTS
 PR00601; BACFERRITIN.