※ Protein Information
Tag Content
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 DNA-directed RNA polymerase subunit beta
Protein Synonyms/Alias
 RNAP subunit beta
Gene Name
 rpoB
Gene Synonyms/Alias
 crsE, rfm; OrderedLocusNames=BSU01070
Created Date
 3-June-2014
Organism
 Bacillus subtilis (strain 168)
NCBI Taxa ID
 224308
Phosphorylation
Position
Peptide
Code
Type
References
313 KGQILDRRTLDKVLP R HTP [1]
314 GQILDRRTLDKVLPY T HTP [1]
539 SSYAKVNRFGFIETP R HTP [1]
694 AKNVWVRRYEEVDGQ R HTP [1]
1106 KSDDVVGRVKTYEAI R HTP [1]
827 ALRNLDDRGIIRIGA R HTP [1]
695 KNVWVRRYEEVDGQK Y HTP [1]
312 EKGQILDRRTLDKVL R HTP [1]
693 EAKNVWVRRYEEVDG R HTP [1]
Reference
 [1]Global impact of protein arginine phosphorylation on the physiology of Bacillus subtilis.
 Elsholz AK,Turgay K,Michalik S,Hessling B,Gronau K,Oertel D,Mäder U,Bernhardt J,Becher D,Hecker M,Gerth U
 Proc. Natl. Acad. Sci. U.S.A. 2012, May, 8;109(19):7451-6. [PMID:22517742]
Functional Description From UniProt
 FUNCTION: DNA-dependent RNA polymerase catalyzes the transcription of DNA into RNA using the four ribonucleoside triphosphates as substrates
Sequence Annotation From UniProt
 
Key Word From UniProt
 3D-structure; Antibioticresistance; Completeproteome; DNA-directedRNApolymerase; Nucleotidyltransferase; Referenceproteome; Transcription; Transferase
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
  GO:0003677   F:DNA binding IEA:UniProtKB-HAMAP
  GO:0003899   F:DNA-directed RNA polymerase activity IEA:UniProtKB-HAMAP
  GO:0032549   F:ribonucleoside binding IEA:InterPro
  GO:0046677   P:response to antibiotic IEA:UniProtKB-KW
  GO:0006351   P:transcription, DNA-templated IEA:UniProtKB-HAMAP
  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.
  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.
  PS01166   RNA_POL_BETA.