CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-010356
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Uncharacterized protein YdiJ 
Protein Synonyms/Alias
  
Gene Name
 ydiJ 
Gene Synonyms/Alias
 b1687; JW1677 
Created Date
 July 27, 2013 
Organism
 Escherichia coli (strain K12) 
NCBI Taxa ID
 83333 
Lysine Modification
Position
Peptide
Type
References
128RVEAGVIKDQLNQYLacetylation[1]
136DQLNQYLKPFGYFFAacetylation[1]
234LIIDNFPKLNRFLTGacetylation[1]
283LDITRLPKVRRLVNVacetylation[1]
291VRRLVNVKYDSFDSAacetylation[1]
319SVETVDSKVLNLAREacetylation[1]
630DRGVDPLKLEQELPEacetylation[1]
657RNSWHANKGEYDFSHacetylation[1]
728PLMARAPKTFNFFINacetylation[1]
745LVRKLSEKHIGMVDLacetylation[1]
785ESLNAEQKARTVLVVacetylation[1]
814DFVRLVEKLGFQPVLacetylation[1]
846RFAKTAKKTADFLNRacetylation[1]
877LCYRDEYKLALGEERacetylation[1]
942IFARFGAKLENVSVGacetylation[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
  
Sequence Annotation
 DOMAIN 48 281 FAD-binding PCMH-type.
 DOMAIN 662 695 4Fe-4S ferredoxin-type.  
Keyword
 Complete proteome; Reference proteome. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 1018 AA 
Protein Sequence
MIPQISQAPG VVQLVLNFLQ ELEQQGFTGD TATSYADRLT MSTDNSIYQL LPDAVVFPRS 60
TADVALIARL AAQERYSSLI FTPRGGGTGT NGQALNQGII VDMSRHMNRI IEINPEEGWV 120
RVEAGVIKDQ LNQYLKPFGY FFAPELSTSN RATLGGMINT DASGQGSLVY GKTSDHVLGV 180
RAVLLGGDIL DTQPLPVELA ETLGKSNTTI GRIYNTVYQR CRQQRQLIID NFPKLNRFLT 240
GYDLRHVFND EMTEFDLTRI LTGSEGTLAF ITEARLDITR LPKVRRLVNV KYDSFDSALR 300
NAPFMVEARA LSVETVDSKV LNLAREDIVW HSVSELITDV PDQEMLGLNI VEFAGDDEAL 360
IDERVNALCA RLDELIASHQ AGVIGWQVCR ELAGVERIYA MRKKAVGLLG NAKGAAKPIP 420
FAEDTCVPPE HLADYIAEFR ALLDSHGLSY GMFGHVDAGV LHVRPALDMC DPQQEILMKQ 480
ISDDVVALTA KYGGLLWGEH GKGFRAEYSP AFFGEELFAE LRKVKAAFDP HNRLNPGKIC 540
PPEGLDAPMM KVDAVKRGTF DRQIPIAVRQ QWRGAMECNG NGLCFNFDAR SPMCPSMKIT 600
QNRIHSPKGR ATLVREWLRL LADRGVDPLK LEQELPESGV SLRTLIARTR NSWHANKGEY 660
DFSHEVKEAM SGCLACKACS TQCPIKIDVP EFRSRFLQLY HTRYLRPLRD HLVATVESYA 720
PLMARAPKTF NFFINQPLVR KLSEKHIGMV DLPLLSVPSL QQQMVGHRSA NMTLEQLESL 780
NAEQKARTVL VVQDPFTSYY DAQVVADFVR LVEKLGFQPV LLPFSPNGKA QHIKGFLNRF 840
AKTAKKTADF LNRMAKLGMP MVGVDPALVL CYRDEYKLAL GEERGEFNVL LANEWLASAL 900
ESQPVATVSG ESWYFFGHCT EVTALPGAPA QWAAIFARFG AKLENVSVGC CGMAGTYGHE 960
AKNHENSLGI YELSWHQAMQ RLPRNRCLAT GYSCRSQVKR VEGTGVRHPV QALLEIIK 1018 
Gene Ontology
 GO:0050660; F:flavin adenine dinucleotide binding; IEA:InterPro.
 GO:0051536; F:iron-sulfur cluster binding; IEA:InterPro.
 GO:0008762; F:UDP-N-acetylmuramate dehydrogenase activity; IEA:InterPro. 
Interpro
 IPR017896; 4Fe4S_Fe-S-bd.
 IPR017900; 4Fe4S_Fe_S_CS.
 IPR016169; CO_DH_flavot_FAD-bd_sub2.
 IPR016166; FAD-bd_2.
 IPR016167; FAD-bd_2_sub1.
 IPR016164; FAD-linked_Oxase-like_C.
 IPR004113; FAD-linked_oxidase_C.
 IPR012285; Fum_reductase_C.
 IPR009051; Helical_ferredxn.
 IPR006094; Oxid_FAD_bind_N. 
Pfam
 PF02913; FAD-oxidase_C
 PF01565; FAD_binding_4
 PF13183; Fer4_8 
SMART
  
PROSITE
 PS00198; 4FE4S_FER_1
 PS51379; 4FE4S_FER_2
 PS51387; FAD_PCMH 
PRINTS