※ 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
 SPD_1759
Created Date
 3-June-2014
Organism
 Streptococcus pneumoniae serotype 2 (strain D39 / NCTC 7466)
NCBI Taxa ID
 373153
Phosphorylation
Position
Peptide
Code
Type
References
702 EVRREDGSLDVYHIQ S HTP [1]
Reference
 [1]Phosphoproteomic analysis reveals the multiple roles of phosphorylation in pathogenic bacterium Streptococcus pneumoniae.
 Sun X,Ge F,Xiao CL,Yin XF,Ge R,Zhang LH,He QY
 J. Proteome Res. 2010, Jan;9(1):275-82. [PMID:19894762]
Functional Description From UniProt
 FUNCTION: DNA-dependent RNA polymerase catalyzes the transcription of DNA into RNA using the four ribonucleoside triphosphates as substrates (By similarity)
Sequence Annotation From UniProt
 
Key Word From UniProt
 Completeproteome; DNA-directedRNApolymerase; Nucleotidyltransferase; Transcription; Transferase
Protein Sequence
 MAGHDVQYGK HRTRRSFSRI KEVLDLPNLI EIQTDSFKAF LDHGLKEVFE DVLPISNFTD 60
 TMELEFVGYE IKEPKYTLEE ARIHDASYSA PIFVTFRLIN KETGEIKTQE VFFGDFPIMT 120
 EMGTFIINGG ERIIVSQLVR SPGVYFNDKV DKNGKVGYGS TVIPNRGAWL ELESDSKDIT 180
 YTRIDRTRKI PFTTLVRALG FSGDDEIFDI FGDSELVRNT VEKDIHKNPM DSRTDEALKE 240
 IYERLRPGEP KTAESSRSLL VARFFDPRRY DLAAVGRYKI NKKLNVKTRL LNQTIAEPLV 300
 DPETGEILVE AGTIMTRSVI ESIESHLDGD LNKIVYIPND AAVVTEPVVL QKFKVVAPTD 360
 PDRVVTIIGN ANPDDKVRTV TPADILAEMS YFLNLAEGLG RVDDIDHLGN RRIRAVGELL 420
 ANQVRLGLSR MERNVRERMS VQDNEVLTPQ QIINIRPVTA AVKEFFGSSQ LSQFMDQHNP 480
 LSELSHKRRL SALGPGGLTR DRAGYEVRDV HYTHYGRMCP IETPEGPNIG LINNLSSYGH 540
 LNKYGFVQTP YRKVDRETGV VTNEIVWLTA DEEDEYTVAQ ANSRLNEDGT FAEKIVMGRH 600
 QGVNQEYPAN IVDYMDVSPK QVVAVATACI PFLENDDSNR ALMGANMQRQ AVPLINPQAP 660
 YVGTGMEYQA AHDSGAAVIA QYDGKVTYAD ADKVEVRRED GSLDVYHIQK FRRSNSGTAY 720
 NQRTLVKVGD VVEKGDFIAD GPSMENGEMA LGQNPIVAYM TWEGYNFEDA VIMSERLVKD 780
 DVYTSVHLEE YESETRDTKL GPEEITREIP NVGEDALKDL DEMGIIRIGA EVKEGDILVG 840
 KVTPKGEKDL SAEERLLHAI FGDKSREVRD TSLRVPHGAD GVVRDVKIFT RVNGDELQSG 900
 VNMLVRVYIA QKRKIKVGDK MAGRHGNKGV VSRIVPVEDM PYLPDGTPVD IMLNPLGVPS 960
 RMNIGQVMEL HLGMAARTLG IHIATPVFDG ASSEDLWSTV KEAGMDSDAK TILYDGRTGE 1020
 PFDNRVSVGV MYMIKLHHMV DDKLHARSVG PYSTVTQQPL GGKAQFGGQR FGEMEVWALE 1080
 AYGASNVLQE ILTYKSDDIN GRLKAYEAIT KGKPIPKPGV PESFRVLVKE LQSLGLDMRV 1140
 LDEDDQEVEL RDLDEGMDED VIHVDDLEKA REKAAQEAKA AFEAEEAEKA TKAEATEEAA 1200
 EQE 1203
  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: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.