CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-003795
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 DNA polymerase III subunit alpha 
Protein Synonyms/Alias
  
Gene Name
 dnaE 
Gene Synonyms/Alias
 polC; b0184; JW0179 
Created Date
 July 27, 2013 
Organism
 Escherichia coli (strain K12) 
NCBI Taxa ID
 83333 
Lysine Modification
Position
Peptide
Type
References
229GFTLDDPKRPRNYSPacetylation[1]
543HPVTQFDKSDVEYAGacetylation[1]
594AAIPLDDKKSFDMLQacetylation[1]
595AIPLDDKKSFDMLQRacetylation[1, 2]
750KIFDLVEKFAGYGFNacetylation[1]
881LNRRVLEKLIMSGAFacetylation[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]
 [2] 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] 
Functional Description
 DNA polymerase III is a complex, multichain enzyme responsible for most of the replicative synthesis in bacteria. This DNA polymerase also exhibits 3' to 5' exonuclease activity. The alpha chain is the DNA polymerase. 
Sequence Annotation
  
Keyword
 3D-structure; Complete proteome; Cytoplasm; DNA replication; DNA-directed DNA polymerase; Nucleotidyltransferase; Reference proteome; Transferase. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 1160 AA 
Protein Sequence
MSEPRFVHLR VHSDYSMIDG LAKTAPLVKK AAALGMPALA ITDFTNLCGL VKFYGAGHGA 60
GIKPIVGADF NVQCDLLGDE LTHLTVLAAN NTGYQNLTLL ISKAYQRGYG AAGPIIDRDW 120
LIELNEGLIL LSGGRMGDVG RSLLRGNSAL VDECVAFYEE HFPDRYFLEL IRTGRPDEES 180
YLHAAVELAE ARGLPVVATN DVRFIDSSDF DAHEIRVAIH DGFTLDDPKR PRNYSPQQYM 240
RSEEEMCELF ADIPEALANT VEIAKRCNVT VRLGEYFLPQ FPTGDMSTED YLVKRAKEGL 300
EERLAFLFPD EEERLKRRPE YDERLETELQ VINQMGFPGY FLIVMEFIQW SKDNGVPVGP 360
GRGSGAGSLV AYALKITDLD PLEFDLLFER FLNPERVSMP DFDVDFCMEK RDQVIEHVAD 420
MYGRDAVSQI ITFGTMAAKA VIRDVGRVLG HPYGFVDRIS KLIPPDPGMT LAKAFEAEPQ 480
LPEIYEADEE VKALIDMARK LEGVTRNAGK HAGGVVIAPT KITDFAPLYC DEEGKHPVTQ 540
FDKSDVEYAG LVKFDFLGLR TLTIINWALE MINKRRAKNG EPPLDIAAIP LDDKKSFDML 600
QRSETTAVFQ LESRGMKDLI KRLQPDCFED MIALVALFRP GPLQSGMVDN FIDRKHGREE 660
ISYPDVQWQH ESLKPVLEPT YGIILYQEQV MQIAQVLSGY TLGGADMLRR AMGKKKPEEM 720
AKQRSVFAEG AEKNGINAEL AMKIFDLVEK FAGYGFNKSH SAAYALVSYQ TLWLKAHYPA 780
EFMAAVMTAD MDNTEKVVGL VDECWRMGLK ILPPDINSGL YHFHVNDDGE IVYGIGAIKG 840
VGEGPIEAII EARNKGGYFR ELFDLCARTD TKKLNRRVLE KLIMSGAFDR LGPHRAALMN 900
SLGDALKAAD QHAKAEAIGQ ADMFGVLAEE PEQIEQSYAS CQPWPEQVVL DGERETLGLY 960
LTGHPINQYL KEIERYVGGV RLKDMHPTER GKVITAAGLV VAARVMVTKR GNRIGICTLD 1020
DRSGRLEVML FTDALDKYQQ LLEKDRILIV SGQVSFDDFS GGLKMTAREV MDIDEAREKY 1080
ARGLAISLTD RQIDDQLLNR LRQSLEPHRS GTIPVHLYYQ RADARARLRF GATWRVSPSD 1140
RLLNDLRGLI GSEQVELEFD 1160 
Gene Ontology
 GO:0005737; C:cytoplasm; IDA:EcoliWiki.
 GO:0003677; F:DNA binding; IEA:InterPro.
 GO:0003887; F:DNA-directed DNA polymerase activity; IDA:EcoliWiki.
 GO:0006260; P:DNA replication; IEA:UniProtKB-KW. 
Interpro
 IPR011708; DNA_pol3_alpha.
 IPR012340; NA-bd_OB-fold.
 IPR004365; NA-bd_OB_tRNA-helicase.
 IPR004013; PHP_C.
 IPR003141; Pol/His_phosphatase_N.
 IPR016195; Pol/histidinol_Pase-like.
 IPR004805; PolC_alpha. 
Pfam
 PF07733; DNA_pol3_alpha
 PF02811; PHP
 PF01336; tRNA_anti 
SMART
 SM00481; POLIIIAc 
PROSITE
  
PRINTS