CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-003125
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
 rpoB 
Gene Synonyms/Alias
 groN; nitB; rif; ron; stl; stv; tabD; b3987; JW3950 
Created Date
 July 27, 2013 
Organism
 Escherichia coli (strain K12) 
NCBI Taxa ID
 83333 
Lysine Modification
Position
Peptide
Type
References
115EAPEGTVKDIKEQEVacetylation[1]
161GVFFDSDKGKTHSSGacetylation[1]
169GKTHSSGKVLYNARIacetylation[1]
191LDFEFDPKDNLFVRIacetylation[1]
236IFEIRDNKLQMELVPacetylation[1, 2]
265NGKVYVEKGRRITARacetylation[1, 3]
279RHIRQLEKDDVKLIEacetylation[1, 2]
283QLEKDDVKLIEVPVEacetylation[1]
422EGSGILSKDDIIDVMacetylation[1]
430DDIIDVMKKLIDIRNacetylation[1]
439LIDIRNGKGEVDDIDacetylation[1]
496PQDMINAKPISAAVKacetylation[1, 3]
503KPISAAVKEFFGSSQacetylation[1, 3]
639DLVTCRSKGESSLFSacetylation[1]
755IDIYNLTKYTRSNQNacetylation[1]
844ACVSRDTKLGPEEITacetylation[1]
890LVGKVTPKGETQLTPacetylation[1, 2, 3]
900TQLTPEEKLLRAIFGacetylation[1]
909LRAIFGEKASDVKDSacetylation[1, 2]
914GEKASDVKDSSLRVPacetylation[1, 2, 3]
954EIEEMQLKQAKKDLSacetylation[1, 2, 3]
957EMQLKQAKKDLSEELacetylation[1]
988AGGVEAEKLDKLPRDacetylation[1, 2, 3]
991VEAEKLDKLPRDRWLacetylation[1, 2, 3]
1007LGLTDEEKQNQLEQLacetylation[1]
1022AEQYDELKHEFEKKLacetylation[1, 4]
1027ELKHEFEKKLEAKRRacetylation[1]
1035KLEAKRRKITQGDDLacetylation[2]
1048DLAPGVLKIVKVYLAacetylation[1]
1065RRIQPGDKMAGRHGNacetylation[1]
1073MAGRHGNKGVISKINacetylation[1]
1122THLGMAAKGIGDKINacetylation[1, 2, 3]
1127AAKGIGDKINAMLKQacetylation[1, 3]
1133DKINAMLKQQQEVAKacetylation[1, 2, 3]
1140KQQQEVAKLREFIQRacetylation[1, 2, 3]
1158LGADVRQKVDLSTFSacetylation[1]
1178RLAENLRKGMPIATPacetylation[1, 2]
1191TPVFDGAKEAEIKELacetylation[1]
1196GAKEAEIKELLKLGDacetylation[1]
1200AEIKELLKLGDLPTSacetylation[1, 2, 3, 4]
1242LNHLVDDKMHARSTGacetylation[1]
1262TQQPLGGKAQFGGQRacetylation[1, 2]
1306NGRTKMYKNIVDGNHacetylation[1]
1328ESFNVLLKEIRSLGIacetylation[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 1022 1022 N6-acetyllysine.
 MOD_RES 1200 1200 N6-acetyllysine.  
Keyword
 3D-structure; Acetylation; Complete proteome; DNA-directed RNA polymerase; Nucleotidyltransferase; Reference proteome; Transcription; Transferase. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 1342 AA 
Protein Sequence
MVYSYTEKKR IRKDFGKRPQ VLDVPYLLSI QLDSFQKFIE QDPEGQYGLE AAFRSVFPIQ 60
SYSGNSELQY VSYRLGEPVF DVQECQIRGV TYSAPLRVKL RLVIYEREAP EGTVKDIKEQ 120
EVYMGEIPLM TDNGTFVING TERVIVSQLH RSPGVFFDSD KGKTHSSGKV LYNARIIPYR 180
GSWLDFEFDP KDNLFVRIDR RRKLPATIIL RALNYTTEQI LDLFFEKVIF EIRDNKLQME 240
LVPERLRGET ASFDIEANGK VYVEKGRRIT ARHIRQLEKD DVKLIEVPVE YIAGKVVAKD 300
YIDESTGELI CAANMELSLD LLAKLSQSGH KRIETLFTND LDHGPYISET LRVDPTNDRL 360
SALVEIYRMM RPGEPPTREA AESLFENLFF SEDRYDLSAV GRMKFNRSLL REEIEGSGIL 420
SKDDIIDVMK KLIDIRNGKG EVDDIDHLGN RRIRSVGEMA ENQFRVGLVR VERAVKERLS 480
LGDLDTLMPQ DMINAKPISA AVKEFFGSSQ LSQFMDQNNP LSEITHKRRI SALGPGGLTR 540
ERAGFEVRDV HPTHYGRVCP IETPEGPNIG LINSLSVYAQ TNEYGFLETP YRKVTDGVVT 600
DEIHYLSAIE EGNYVIAQAN SNLDEEGHFV EDLVTCRSKG ESSLFSRDQV DYMDVSTQQV 660
VSVGASLIPF LEHDDANRAL MGANMQRQAV PTLRADKPLV GTGMERAVAV DSGVTAVAKR 720
GGVVQYVDAS RIVIKVNEDE MYPGEAGIDI YNLTKYTRSN QNTCINQMPC VSLGEPVERG 780
DVLADGPSTD LGELALGQNM RVAFMPWNGY NFEDSILVSE RVVQEDRFTT IHIQELACVS 840
RDTKLGPEEI TADIPNVGEA ALSKLDESGI VYIGAEVTGG DILVGKVTPK GETQLTPEEK 900
LLRAIFGEKA SDVKDSSLRV PNGVSGTVID VQVFTRDGVE KDKRALEIEE MQLKQAKKDL 960
SEELQILEAG LFSRIRAVLV AGGVEAEKLD KLPRDRWLEL GLTDEEKQNQ LEQLAEQYDE 1020
LKHEFEKKLE AKRRKITQGD DLAPGVLKIV KVYLAVKRRI QPGDKMAGRH GNKGVISKIN 1080
PIEDMPYDEN GTPVDIVLNP LGVPSRMNIG QILETHLGMA AKGIGDKINA MLKQQQEVAK 1140
LREFIQRAYD LGADVRQKVD LSTFSDEEVM RLAENLRKGM PIATPVFDGA KEAEIKELLK 1200
LGDLPTSGQI RLYDGRTGEQ FERPVTVGYM YMLKLNHLVD DKMHARSTGS YSLVTQQPLG 1260
GKAQFGGQRF GEMEVWALEA YGAAYTLQEM LTVKSDDVNG RTKMYKNIVD GNHQMEPGMP 1320
ESFNVLLKEI RSLGINIELE DE 1342 
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:0032549; F:ribonucleoside binding; IEA:InterPro.
 GO:0006351; P:transcription, DNA-dependent; IEA:HAMAP. 
Interpro
 IPR010243; DNA-dir_RNA_pol_bsu.
 IPR019462; DNA-dir_RNA_pol_bsu_external_1.
 IPR015712; DNA-dir_RNA_pol_su2.
 IPR007120; DNA-dir_RNA_pol_su2_6.
 IPR007121; RNA_pol_bsu_CS.
 IPR007644; RNA_pol_bsu_protrusion.
 IPR007642; RNA_pol_Rpb2_2.
 IPR007645; RNA_pol_Rpb2_3.
 IPR007641; RNA_pol_Rpb2_7.
 IPR014724; RNA_pol_RPB2_OB-fold. 
Pfam
 PF04563; RNA_pol_Rpb2_1
 PF04561; RNA_pol_Rpb2_2
 PF04565; RNA_pol_Rpb2_3
 PF10385; RNA_pol_Rpb2_45
 PF00562; RNA_pol_Rpb2_6
 PF04560; RNA_pol_Rpb2_7 
SMART
  
PROSITE
 PS01166; RNA_POL_BETA 
PRINTS