CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-003044
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 DNA-directed RNA polymerase subunit alpha 
Protein Synonyms/Alias
 RNAP subunit alpha; RNA polymerase subunit alpha; Transcriptase subunit alpha 
Gene Name
 rpoA 
Gene Synonyms/Alias
 pez; phs; sez; b3295; JW3257 
Created Date
 July 27, 2013 
Organism
 Escherichia coli (strain K12) 
NCBI Taxa ID
 83333 
Lysine Modification
Position
Peptide
Type
References
10GSVTEFLKPRLVDIEacetylation[1, 2]
25QVSSTHAKVTLEPLEacetylation[1]
95LAVRVQGKDEVILTLacetylation[1, 2]
125DGDVEIVKPQHVICHacetylation[2]
200EQRTDLDKLVIEMETacetylation[2]
246QPEVKEEKPEFDPILacetylation[2, 3]
271VRSANCLKAEAIHYIacetylation[2, 3]
291RTEVELLKTPNLGKKacetylation[1, 2, 4]
297LKTPNLGKKSLTEIKacetylation[1, 2, 5]
298KTPNLGKKSLTEIKDacetylation[1, 2, 5]
304KKSLTEIKDVLASRGacetylation[1, 2, 3]
Reference
 [1] Inhibition of acetyl phosphate-dependent transcription by an acetylatable lysine on RNA polymerase.
 Lima BP, Thanh Huyen TT, Bäsell K, Becher D, Antelmann H, Wolfe AJ.
 J Biol Chem. 2012 Sep 14;287(38):32147-60. [PMID: 22829598]
 [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] 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]
 [4] 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]
 [5] Involvement of protein acetylation in glucose-induced transcription of a stress-responsive promoter.
 Lima BP, Antelmann H, Gronau K, Chi BK, Becher D, Brinsmade SR, Wolfe AJ.
 Mol Microbiol. 2011 Sep;81(5):1190-204. [PMID: 21696463] 
Functional Description
 DNA-dependent RNA polymerase catalyzes the transcription of DNA into RNA using the four ribonucleoside triphosphates as substrates. This subunit plays an important role in subunit assembly since its dimerization is the first step in the sequential assembly of subunits to form the holoenzyme. 
Sequence Annotation
 REGION 1 235 Alpha N-terminal domain (alpha-NTD).
 REGION 249 329 Alpha C-terminal domain (alpha-CTD).  
Keyword
 3D-structure; Complete proteome; Direct protein sequencing; DNA-directed RNA polymerase; Nucleotidyltransferase; Reference proteome; Transcription; Transferase. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 329 AA 
Protein Sequence
MQGSVTEFLK PRLVDIEQVS STHAKVTLEP LERGFGHTLG NALRRILLSS MPGCAVTEVE 60
IDGVLHEYST KEGVQEDILE ILLNLKGLAV RVQGKDEVIL TLNKSGIGPV TAADITHDGD 120
VEIVKPQHVI CHLTDENASI SMRIKVQRGR GYVPASTRIH SEEDERPIGR LLVDACYSPV 180
ERIAYNVEAA RVEQRTDLDK LVIEMETNGT IDPEEAIRRA ATILAEQLEA FVDLRDVRQP 240
EVKEEKPEFD PILLRPVDDL ELTVRSANCL KAEAIHYIGD LVQRTEVELL KTPNLGKKSL 300
TEIKDVLASR GLSLGMRLEN WPPASIADE 329 
Gene Ontology
 GO:0005737; C:cytoplasm; IDA:UniProtKB.
 GO:0016020; C:membrane; IDA:UniProtKB.
 GO:0003677; F:DNA binding; IEA:HAMAP.
 GO:0003899; F:DNA-directed RNA polymerase activity; IEA:HAMAP.
 GO:0008270; F:zinc ion binding; IDA:EcoliWiki.
 GO:0006351; P:transcription, DNA-dependent; IEA:HAMAP. 
Interpro
 IPR011261; DNA-dir_RNA_pol_dimersation.
 IPR011262; DNA-dir_RNA_pol_insert.
 IPR009025; DNA-dir_RNA_pol_RBP11-like.
 IPR011263; DNA-dir_RNA_pol_RpoA/D/Rpb3.
 IPR011773; DNA-dir_RpoA.
 IPR011260; RNAP_asu_C. 
Pfam
 PF01000; RNA_pol_A_bac
 PF03118; RNA_pol_A_CTD
 PF01193; RNA_pol_L 
SMART
 SM00662; RPOLD 
PROSITE
  
PRINTS