CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-006472
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Alkyl hydroperoxide reductase subunit F 
Protein Synonyms/Alias
 Alkyl hydroperoxide reductase F52A protein 
Gene Name
 ahpF 
Gene Synonyms/Alias
 b0606; JW0599 
Created Date
 July 27, 2013 
Organism
 Escherichia coli (strain K12) 
NCBI Taxa ID
 83333 
Lysine Modification
Position
Peptide
Type
References
11TNMKTQLKAYLEKLTacetylation[1, 2]
16QLKAYLEKLTKPVELacetylation[1, 2]
19AYLEKLTKPVELIATacetylation[1, 2, 3]
32ATLDDSAKSAEIKELacetylation[2]
37SAKSAEIKELLAEIAacetylation[2]
49EIAELSDKVTFKEDNacetylation[2]
53LSDKVTFKEDNSLPVacetylation[2, 4]
179PAVFVNGKEFGQGRMacetylation[2]
194TLTEIVAKIDTGAEKacetylation[2]
201KIDTGAEKRAAEELNacetylation[2]
209RAAEELNKRDAYDVLacetylation[2]
268VPKTEGQKLAGALKVacetylation[1, 2]
314TASGAVLKARSIIVAacetylation[1, 2]
325IIVATGAKWRNMNVPacetylation[2]
354HCDGPLFKGKRVAVIacetylation[2, 4]
399ADQVLQDKLRSLKNVacetylation[2]
404QDKLRSLKNVDIILNacetylation[2]
423EVKGDGSKVVGLEYRacetylation[2]
Reference
 [1] Comprehensive profiling of protein lysine acetylation in Escherichia coli.
 Zhang K, Zheng S, Yang JS, Chen Y, Cheng Z.
 J Proteome Res. 2013 Feb 1;12(2):844-51. [PMID: 23294111]
 [2] 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]
 [3] The diversity of lysine-acetylated proteins in Escherichia coli.
 Yu BJ, Kim JA, Moon JH, Ryu SE, Pan JG.
 J Microbiol Biotechnol. 2008 Sep;18(9):1529-36. [PMID: 18852508]
 [4] Lysine acetylation is a highly abundant and evolutionarily conserved modification in Escherichia coli.
 Zhang J, Sprung R, Pei J, Tan X, Kim S, Zhu H, Liu CF, Grishin NV, Zhao Y.
 Mol Cell Proteomics. 2009 Feb;8(2):215-25. [PMID: 18723842
Functional Description
 Serves to protect the cell against DNA damage by alkyl hydroperoxides. It can use either NADH or NADPH as electron donor for direct reduction of redox dyes or of alkyl hydroperoxides when combined with the AhpC protein. 
Sequence Annotation
 NP_BIND 214 229 FAD (By similarity).
 NP_BIND 357 371 NAD or NADP (By similarity).
 NP_BIND 478 488 FAD (By similarity).
 MOD_RES 53 53 N6-acetyllysine.
 MOD_RES 354 354 N6-acetyllysine.
 DISULFID 345 348 Redox-active (By similarity).  
Keyword
 3D-structure; Acetylation; Complete proteome; Disulfide bond; FAD; Flavoprotein; NAD; NADP; Oxidoreductase; Redox-active center; Reference proteome. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 521 AA 
Protein Sequence
MLDTNMKTQL KAYLEKLTKP VELIATLDDS AKSAEIKELL AEIAELSDKV TFKEDNSLPV 60
RKPSFLITNP GSNQGPRFAG SPLGHEFTSL VLALLWTGGH PSKEAQSLLE QIRHIDGDFE 120
FETYYSLSCH NCPDVVQALN LMSVLNPRIK HTAIDGGTFQ NEITDRNVMG VPAVFVNGKE 180
FGQGRMTLTE IVAKIDTGAE KRAAEELNKR DAYDVLIVGS GPAGAAAAIY SARKGIRTGL 240
MGERFGGQIL DTVDIENYIS VPKTEGQKLA GALKVHVDEY DVDVIDSQSA SKLIPAAVEG 300
GLHQIETASG AVLKARSIIV ATGAKWRNMN VPGEDQYRTK GVTYCPHCDG PLFKGKRVAV 360
IGGGNSGVEA AIDLAGIVEH VTLLEFAPEM KADQVLQDKL RSLKNVDIIL NAQTTEVKGD 420
GSKVVGLEYR DRVSGDIHNI ELAGIFVQIG LLPNTNWLEG AVERNRMGEI IIDAKCETNV 480
KGVFAAGDCT TVPYKQIIIA TGEGAKASLS AFDYLIRTKT A 521 
Gene Ontology
 GO:0005829; C:cytosol; IDA:UniProtKB.
 GO:0008785; F:alkyl hydroperoxide reductase activity; IGI:EcoliWiki.
 GO:0009055; F:electron carrier activity; IEA:InterPro.
 GO:0071949; F:FAD binding; IDA:EcoCyc.
 GO:0051287; F:NAD binding; IEA:InterPro.
 GO:0015035; F:protein disulfide oxidoreductase activity; IEA:InterPro.
 GO:0045454; P:cell redox homeostasis; IEA:InterPro.
 GO:0000302; P:response to reactive oxygen species; IEA:InterPro. 
Interpro
 IPR012081; Alkyl_hydroperoxide_Rdtase_suF.
 IPR013027; FAD_pyr_nucl-diS_OxRdtase.
 IPR002109; Glutaredoxin.
 IPR008255; Pyr_nucl-diS_OxRdtase_2_AS.
 IPR023753; Pyr_nucl-diS_OxRdtase_FAD/NAD.
 IPR001327; Pyr_OxRdtase_NAD-bd_dom.
 IPR000103; Pyridine_nuc-diS_OxRdtase_2.
 IPR012336; Thioredoxin-like_fold. 
Pfam
 PF00070; Pyr_redox
 PF07992; Pyr_redox_2
 PF13192; Thioredoxin_3 
SMART
  
PROSITE
 PS51354; GLUTAREDOXIN_2
 PS00573; PYRIDINE_REDOX_2 
PRINTS
 PR00368; FADPNR.
 PR00469; PNDRDTASEII.