CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-006808
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
 crsE; rfm; BSU01070 
Created Date
 July 27, 2013 
Organism
 Bacillus subtilis (strain 168) 
NCBI Taxa ID
 224308 
Lysine Modification
Position
Peptide
Type
References
82KYPVEESKERDVTYSacetylation[1]
Reference
 [1] The acetylproteome of Gram-positive model bacterium Bacillus subtilis.
 Kim D, Yu BJ, Kim JA, Lee YJ, Choi SG, Kang S, Pan JG.
 Proteomics. 2013 May;13(10-11):1726-36. [PMID: 23468065
Functional Description
 DNA-dependent RNA polymerase catalyzes the transcription of DNA into RNA using the four ribonucleoside triphosphates as substrates. 
Sequence Annotation
  
Keyword
 Antibiotic resistance; Complete proteome; DNA-directed RNA polymerase; Nucleotidyltransferase; Reference proteome; Transcription; Transferase. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 1193 AA 
Protein Sequence
MTGQLVQYGR HRQRRSYARI SEVLELPNLI EIQTSSYQWF LDEGLREMFQ DISPIEDFTG 60
NLSLEFIDYS LGEPKYPVEE SKERDVTYSA PLRVKVRLIN KETGEVKDQD VFMGDFPIMT 120
DTGTFIINGA ERVIVSQLVR SPSVYFSGKV DKNGKKGFTA TVIPNRGAWL EYETDAKDVV 180
YVRIDRTRKL PVTVLLRALG FGSDQEILDL IGENEYLRNT LDKDNTENSD KALLEIYERL 240
RPGEPPTVEN AKSLLDSRFF DPKRYDLANV GRYKINKKLH IKNRLFNQRL AETLVDPETG 300
EILAEKGQIL DRRTLDKVLP YLENGIGFRK LYPNGGVVED EVTLQSIKIF APTDQEGEQV 360
INVIGNAYIE EEIKNITPAD IISSISYFFN LLHGVGDTDD IDHLGNRRLR SVGELLQNQF 420
RIGLSRMERV VRERMSIQDT NTITPQQLIN IRPVIASIKE FFGSSQLSQF MDQTNPLAEL 480
THKRRLSALG PGGLTRERAG MEVRDVHYSH YGRMCPIETP EGPNIGLINS LSSYAKVNRF 540
GFIETPYRRV DPETGKVTGR IDYLTADEED NYVVAQANAR LDDEGAFIDD SIVARFRGEN 600
TVVSRNRVDY MDVSPKQVVS AATACIPFLE NDDSNRALMG ANMQRQAVPL MQPEAPFVGT 660
GMEYVSGKDS GAAVICKHPG IVERVEAKNV WVRRYEEVDG QKVKGNLDKY SLLKFVRSNQ 720
GTCYNQRPIV SVGDEVVKGE ILADGPSMEL GELALGRNVM VGFMTWDGYN YEDAIIMSER 780
LVKDDVYTSI HIEEYESEAR DTKLGPEEIT RDIPNVGEDA LRNLDDRGII RIGAEVKDGD 840
LLVGKVTPKG VTELTAEERL LHAIFGEKAR EVRDTSLRVP HGGGGIIHDV KVFNREDGDE 900
LPPGVNQLVR VYIVQKRKIS EGDKMAGRHG NKGVISKILP EEDMPYLPDG TPIDIMLNPL 960
GVPSRMNIGQ VLELHMGMAA RYLGIHIASP VFDGAREEDV WETLEEAGMS RDAKTVLYDG 1020
RTGEPFDNRV SVGIMYMIKL AHMVDDKLHA RSTGPYSLVT QQPLGGKAQF GGQRFGEMEV 1080
WALEAYGAAY TLQEILTVKS DDVVGRVKTY EAIVKGDNVP EPGVPESFKV LIKELQSLGM 1140
DVKILSGDEE EIEMRDLEDE EDAKQADGLA LSGDEEPEET ASADVERDVV TKE 1193 
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:0046677; P:response to antibiotic; IEA:UniProtKB-KW.
 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