CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-003121
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 DNA-directed RNA polymerase subunit beta' 
Protein Synonyms/Alias
 RNAP subunit beta'; RNA polymerase subunit beta'; Transcriptase subunit beta' 
Gene Name
 rpoC 
Gene Synonyms/Alias
 tabB; b3988; JW3951 
Created Date
 July 27, 2013 
Organism
 Escherichia coli (strain K12) 
NCBI Taxa ID
 83333 
Lysine Modification
Position
Peptide
Type
References
6**MKDLLKFLKAQTKacetylation[1]
13KFLKAQTKTEEFDAIacetylation[1, 2, 3]
21TEEFDAIKIALASPDacetylation[1]
39SWSFGEVKKPETINYacetylation[1]
40WSFGEVKKPETINYRacetylation[1, 2, 3]
50TINYRTFKPERDGLFacetylation[1, 3]
66ARIFGPVKDYECLCGacetylation[3]
74DYECLCGKYKRLKHRacetylation[1]
87HRGVICEKCGVEVTQacetylation[1, 3]
118TAHIWFLKSLPSRIGacetylation[1]
190EAIQALLKSMDLEQEacetylation[1]
325GSNKRPLKSLADMIKacetylation[1]
371HQCGLPKKMALELFKacetylation[3]
378KMALELFKPFIYGKLacetylation[1]
384FKPFIYGKLELRGLAacetylation[1]
395RGLATTIKAAKKMVEacetylation[1, 2]
398ATTIKAAKKMVEREEacetylation[1]
521TRDCVNAKGEGMVLTacetylation[3]
531GMVLTGPKEAERLYRacetylation[1, 2]
557VRITEYEKDANGELVacetylation[1]
566ANGELVAKTSLKDTTacetylation[1]
570LVAKTSLKDTTVGRAacetylation[1, 2]
598IVNQALGKKAISKMLacetylation[1]
599VNQALGKKAISKMLNacetylation[1]
603LGKKAISKMLNTCYRacetylation[1, 3]
649DDMVIPEKKHEIISEacetylation[1, 2]
681TAGERYNKVIDIWAAacetylation[1]
695AANDRVSKAMMDNLQacetylation[1, 3]
715NRDGQEEKQVSFNSIacetylation[1]
749GMRGLMAKPDGSIIEacetylation[1]
789GLADTALKTANSGYLacetylation[1]
850VTAEDVLKPGTADILacetylation[1]
881ENSVDAVKVRSVVSCacetylation[1]
911ARGHIINKGEAIGVIacetylation[1]
953AESSIQVKNKGSIKLacetylation[2]
959VKNKGSIKLSNVKSVacetylation[1, 2]
964SIKLSNVKSVVNSSGacetylation[2, 3]
972SVVNSSGKLVITSRNacetylation[1, 3]
983TSRNTELKLIDEFGRacetylation[1, 2, 4]
996GRTKESYKVPYGAVLacetylation[1]
1072AERTAGGKDLRPALKacetylation[1]
1079KDLRPALKIVDAQGNacetylation[1]
1132PQESGGTKDITGGLPacetylation[1]
1151LFEARRPKEPAILAEacetylation[1]
1192PYEEMIPKWRQLNVFacetylation[1]
1247VYRLQGVKINDKHIEacetylation[2]
1251QGVKINDKHIEVIVRacetylation[1]
1340TEAAVAGKRDELRGLacetylation[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] 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]
 [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] 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
 DNA-dependent RNA polymerase catalyzes the transcription of DNA into RNA using the four ribonucleoside triphosphates as substrates. 
Sequence Annotation
 MOD_RES 983 983 N6-acetyllysine.  
Keyword
 3D-structure; Acetylation; Complete proteome; Direct protein sequencing; DNA-directed RNA polymerase; Nucleotidyltransferase; Reference proteome; Transcription; Transferase. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 1407 AA 
Protein Sequence
MKDLLKFLKA QTKTEEFDAI KIALASPDMI RSWSFGEVKK PETINYRTFK PERDGLFCAR 60
IFGPVKDYEC LCGKYKRLKH RGVICEKCGV EVTQTKVRRE RMGHIELASP TAHIWFLKSL 120
PSRIGLLLDM PLRDIERVLY FESYVVIEGG MTNLERQQIL TEEQYLDALE EFGDEFDAKM 180
GAEAIQALLK SMDLEQECEQ LREELNETNS ETKRKKLTKR IKLLEAFVQS GNKPEWMILT 240
VLPVLPPDLR PLVPLDGGRF ATSDLNDLYR RVINRNNRLK RLLDLAAPDI IVRNEKRMLQ 300
EAVDALLDNG RRGRAITGSN KRPLKSLADM IKGKQGRFRQ NLLGKRVDYS GRSVITVGPY 360
LRLHQCGLPK KMALELFKPF IYGKLELRGL ATTIKAAKKM VEREEAVVWD ILDEVIREHP 420
VLLNRAPTLH RLGIQAFEPV LIEGKAIQLH PLVCAAYNAD FDGDQMAVHV PLTLEAQLEA 480
RALMMSTNNI LSPANGEPII VPSQDVVLGL YYMTRDCVNA KGEGMVLTGP KEAERLYRSG 540
LASLHARVKV RITEYEKDAN GELVAKTSLK DTTVGRAILW MIVPKGLPYS IVNQALGKKA 600
ISKMLNTCYR ILGLKPTVIF ADQIMYTGFA YAARSGASVG IDDMVIPEKK HEIISEAEAE 660
VAEIQEQFQS GLVTAGERYN KVIDIWAAAN DRVSKAMMDN LQTETVINRD GQEEKQVSFN 720
SIYMMADSGA RGSAAQIRQL AGMRGLMAKP DGSIIETPIT ANFREGLNVL QYFISTHGAR 780
KGLADTALKT ANSGYLTRRL VDVAQDLVVT EDDCGTHEGI MMTPVIEGGD VKEPLRDRVL 840
GRVTAEDVLK PGTADILVPR NTLLHEQWCD LLEENSVDAV KVRSVVSCDT DFGVCAHCYG 900
RDLARGHIIN KGEAIGVIAA QSIGEPGTQL TMRTFHIGGA ASRAAAESSI QVKNKGSIKL 960
SNVKSVVNSS GKLVITSRNT ELKLIDEFGR TKESYKVPYG AVLAKGDGEQ VAGGETVANW 1020
DPHTMPVITE VSGFVRFTDM IDGQTITRQT DELTGLSSLV VLDSAERTAG GKDLRPALKI 1080
VDAQGNDVLI PGTDMPAQYF LPGKAIVQLE DGVQISSGDT LARIPQESGG TKDITGGLPR 1140
VADLFEARRP KEPAILAEIS GIVSFGKETK GKRRLVITPV DGSDPYEEMI PKWRQLNVFE 1200
GERVERGDVI SDGPEAPHDI LRLRGVHAVT RYIVNEVQDV YRLQGVKIND KHIEVIVRQM 1260
LRKATIVNAG SSDFLEGEQV EYSRVKIANR ELEANGKVGA TYSRDLLGIT KASLATESFI 1320
SAASFQETTR VLTEAAVAGK RDELRGLKEN VIVGRLIPAG TGYAYHQDRM RRRAAGEAPA 1380
APQVTAEDAS ASLAELLNAG LGGSDNE 1407 
Gene Ontology
 GO:0005737; C:cytoplasm; IDA:UniProtKB.
 GO:0016020; C:membrane; IDA:UniProtKB.
 GO:0003677; F:DNA binding; IEA:InterPro.
 GO:0003899; F:DNA-directed RNA polymerase activity; IEA:UniProtKB-KW.
 GO:0006351; P:transcription, DNA-dependent; IEA:InterPro. 
Interpro
 IPR009010; Asp_de-COase-like_dom.
 IPR012754; DNA-dir_RpoC_beta_prime.
 IPR000722; RNA_pol_asu.
 IPR006592; RNA_pol_N.
 IPR007080; RNA_pol_Rpb1_1.
 IPR007066; RNA_pol_Rpb1_3.
 IPR007083; RNA_pol_Rpb1_4.
 IPR007081; RNA_pol_Rpb1_5. 
Pfam
 PF04997; RNA_pol_Rpb1_1
 PF00623; RNA_pol_Rpb1_2
 PF04983; RNA_pol_Rpb1_3
 PF05000; RNA_pol_Rpb1_4
 PF04998; RNA_pol_Rpb1_5 
SMART
 SM00663; RPOLA_N 
PROSITE
  
PRINTS