CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-017902
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
 TTHA1813 
Created Date
 July 27, 2013 
Organism
 Thermus thermophilus (strain HB8 / ATCC 27634 / DSM 579) 
NCBI Taxa ID
 300852 
Lysine Modification
Position
Peptide
Type
References
1004LYHMVEDKMHARSTGacetylation[1]
Reference
 [1] Acetylome with structural mapping reveals the significance of lysine acetylation in Thermus thermophilus.
 Okanishi H, Kim K, Masui R, Kuramitsu S.
 J Proteome Res. 2013 Aug 1;. [PMID: 23901841
Functional Description
 DNA-dependent RNA polymerase catalyzes the transcription of DNA into RNA using the four ribonucleoside triphosphates as substrates. 
Sequence Annotation
  
Keyword
 3D-structure; Complete proteome; DNA-directed RNA polymerase; Nucleotidyltransferase; Reference proteome; Transcription; Transferase. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 1119 AA 
Protein Sequence
MEIKRFGRIR EVIPLPPLTE IQVESYRRAL QADVPPEKRE NVGIQAAFRE TFPIEEEDKG 60
KGGLVLDFLE YRLGEPPFPQ DECREKDLTY QAPLYARLQL IHKDTGLIKE DEVFLGHIPL 120
MTEDGSFIIN GADRVIVSQI HRSPGVYFTP DPARPGRYIA SIIPLPKRGP WIDLEVEPNG 180
VVSMKVNKRK FPLVLLLRVL GYDQETLARE LGAYGELVQG LMDESVFAMR PEEALIRLFT 240
LLRPGDPPKR DKAVAYVYGL IADPRRYDLG EAGRYKAEEK LGIRLSGRTL ARFEDGEFKD 300
EVFLPTLRYL FALTAGVPGH EVDDIDHLGN RRIRTVGELM TDQFRVGLAR LARGVRERML 360
MGSEDSLTPA KLVNSRPLEA AIREFFSRSQ LSQFKDETNP LSSLRHKRRI SALGPGGLTR 420
ERAGFDVRDV HRTHYGRICP VETPEGANIG LITSLAAYAR VDELGFIRTP YRRVVGGVVT 480
DEVVYMTATE EDRYTIAQAN TPLEGNRIAA ERVVARRKGE PVIVSPEEVE FMDVSPKQVF 540
SVNTNLIPFL EHDDANRALM GSNMQTQAVP LIRAQAPVVM TGLEERVVRD SLAALYAEED 600
GEVAKVDGNR IVVRYEDGRL VEYPLRRFYR SNQGTALDQR PRVVVGQRVR KGDLLADGPA 660
SENGFLALGQ NVLVAIMPFD GYNFEDAIVI SEELLKRDFY TSIHIERYEI EARDTKLGPE 720
RITRDIPHLS EAALRDLDEE GVVRIGAEVK PGDILVGRTS FKGESEPTPE ERLLRSIFGE 780
KARDVKDTSL RVPPGEGGIV VRTVRLRRGD PGVELKPGVR EVVRVYVAQK RKLQVGDKLA 840
NRHGNKGVVA KILPVEDMPH LPDGTPVDVI LNPLGVPSRM NLGQILETHL GLAGYFLGQR 900
YISPIFDGAK EPEIKELLAQ AFEVYFGKRK GEGFGVDKRE VEVLRRAEKL GLVTPGKTPE 960
EQLKELFLQG KVVLYDGRTG EPIEGPIVVG QMFIMKLYHM VEDKMHARST GPYSLITQQP 1020
LGGKAQFGGQ RFGEMEVWAL EAYGAAHTLQ EMLTLKSDDI EGRNAAYEAI IKGEDVPEPS 1080
VPESFRVLVK ELQALALDVQ TLDEKDNPVD IFEGLASKR 1119 
Gene Ontology
 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