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P0A8V2 (RPOB_ECOLI) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 96. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
DNA-directed RNA polymerase subunit beta

Short name=RNAP subunit beta
EC=2.7.7.6
Alternative name(s):
RNA polymerase subunit beta
Transcriptase subunit beta
Gene names
Name:rpoB
Synonyms:groN, nitB, rif, ron, stl, stv, tabD
Ordered Locus Names:b3987, JW3950
OrganismEscherichia coli (strain K12) [Reference proteome] [HAMAP]
Taxonomic identifier83333 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia

Protein attributes

Sequence length1342 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

DNA-dependent RNA polymerase catalyzes the transcription of DNA into RNA using the four ribonucleoside triphosphates as substrates. Ref.15

Catalytic activity

Nucleoside triphosphate + RNA(n) = diphosphate + RNA(n+1). HAMAP-Rule MF_01321

Subunit structure

The RNAP catalytic core consists of 2 alpha, 1 beta, 1 beta' and 1 omega subunit. When a sigma factor is associated with the core the holoenzyme is formed, which can initiate transcription. Ref.15 Ref.19

Sequence similarities

Belongs to the RNA polymerase beta chain family.

Sequence caution

The sequence described in Ref.7 differs from that shown. Reason:

Binary interactions

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 13421342DNA-directed RNA polymerase subunit beta HAMAP-Rule MF_01321
PRO_0000047892

Amino acid modifications

Modified residue10221N6-acetyllysine Ref.18
Modified residue12001N6-acetyllysine Ref.18

Experimental info

Mutagenesis8131E → K: Disrupts the enzyme's active center. Ref.16
Sequence conflict41S → R AA sequence Ref.10
Sequence conflict106 – 1072ER → G in CAA23629. Ref.6
Sequence conflict384 – 3918LFENLFFS → CSRTCSSPT in CAA23629. Ref.6
Sequence conflict5161D → V in CAA23625. Ref.1
Sequence conflict5161D → V in CAA23627. Ref.1
Sequence conflict5161D → V in AAA24585. Ref.11

Secondary structure

....................................................................................... 1342
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P0A8V2 [UniParc].

Last modified June 7, 2005. Version 1.
Checksum: F9E95344C54AB118

FASTA1,342150,632
        10         20         30         40         50         60 
MVYSYTEKKR IRKDFGKRPQ VLDVPYLLSI QLDSFQKFIE QDPEGQYGLE AAFRSVFPIQ 

        70         80         90        100        110        120 
SYSGNSELQY VSYRLGEPVF DVQECQIRGV TYSAPLRVKL RLVIYEREAP EGTVKDIKEQ 

       130        140        150        160        170        180 
EVYMGEIPLM TDNGTFVING TERVIVSQLH RSPGVFFDSD KGKTHSSGKV LYNARIIPYR 

       190        200        210        220        230        240 
GSWLDFEFDP KDNLFVRIDR RRKLPATIIL RALNYTTEQI LDLFFEKVIF EIRDNKLQME 

       250        260        270        280        290        300 
LVPERLRGET ASFDIEANGK VYVEKGRRIT ARHIRQLEKD DVKLIEVPVE YIAGKVVAKD 

       310        320        330        340        350        360 
YIDESTGELI CAANMELSLD LLAKLSQSGH KRIETLFTND LDHGPYISET LRVDPTNDRL 

       370        380        390        400        410        420 
SALVEIYRMM RPGEPPTREA AESLFENLFF SEDRYDLSAV GRMKFNRSLL REEIEGSGIL 

       430        440        450        460        470        480 
SKDDIIDVMK KLIDIRNGKG EVDDIDHLGN RRIRSVGEMA ENQFRVGLVR VERAVKERLS 

       490        500        510        520        530        540 
LGDLDTLMPQ DMINAKPISA AVKEFFGSSQ LSQFMDQNNP LSEITHKRRI SALGPGGLTR 

       550        560        570        580        590        600 
ERAGFEVRDV HPTHYGRVCP IETPEGPNIG LINSLSVYAQ TNEYGFLETP YRKVTDGVVT 

       610        620        630        640        650        660 
DEIHYLSAIE EGNYVIAQAN SNLDEEGHFV EDLVTCRSKG ESSLFSRDQV DYMDVSTQQV 

       670        680        690        700        710        720 
VSVGASLIPF LEHDDANRAL MGANMQRQAV PTLRADKPLV GTGMERAVAV DSGVTAVAKR 

       730        740        750        760        770        780 
GGVVQYVDAS RIVIKVNEDE MYPGEAGIDI YNLTKYTRSN QNTCINQMPC VSLGEPVERG 

       790        800        810        820        830        840 
DVLADGPSTD LGELALGQNM RVAFMPWNGY NFEDSILVSE RVVQEDRFTT IHIQELACVS 

       850        860        870        880        890        900 
RDTKLGPEEI TADIPNVGEA ALSKLDESGI VYIGAEVTGG DILVGKVTPK GETQLTPEEK 

       910        920        930        940        950        960 
LLRAIFGEKA SDVKDSSLRV PNGVSGTVID VQVFTRDGVE KDKRALEIEE MQLKQAKKDL 

       970        980        990       1000       1010       1020 
SEELQILEAG LFSRIRAVLV AGGVEAEKLD KLPRDRWLEL GLTDEEKQNQ LEQLAEQYDE 

      1030       1040       1050       1060       1070       1080 
LKHEFEKKLE AKRRKITQGD DLAPGVLKIV KVYLAVKRRI QPGDKMAGRH GNKGVISKIN 

      1090       1100       1110       1120       1130       1140 
PIEDMPYDEN GTPVDIVLNP LGVPSRMNIG QILETHLGMA AKGIGDKINA MLKQQQEVAK 

      1150       1160       1170       1180       1190       1200 
LREFIQRAYD LGADVRQKVD LSTFSDEEVM RLAENLRKGM PIATPVFDGA KEAEIKELLK 

      1210       1220       1230       1240       1250       1260 
LGDLPTSGQI RLYDGRTGEQ FERPVTVGYM YMLKLNHLVD DKMHARSTGS YSLVTQQPLG 

      1270       1280       1290       1300       1310       1320 
GKAQFGGQRF GEMEVWALEA YGAAYTLQEM LTVKSDDVNG RTKMYKNIVD GNHQMEPGMP 

      1330       1340 
ESFNVLLKEI RSLGINIELE DE 

« Hide

References

« Hide 'large scale' references
[1]"The primary structure of Escherichia coli RNA polymerase. Nucleotide sequence of the rpoB gene and amino-acid sequence of the beta-subunit."
Ovchinnikov Y.A., Monastyrskaya G.S., Gubanov V.V., Guryev S.O., Chertov O.Y., Modyanov N.N., Grinkevich V.A., Makarova I.A., Marchenko T.V., Polovnikova I.N., Lipkin V.M., Sverdlov E.D.
Eur. J. Biochem. 116:621-629(1981) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[2]Miller E.S., Shih G.C., Chung S.K., Ballard D.N.
Submitted (NOV-1996) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: B.
[3]"Analysis of the Escherichia coli genome. IV. DNA sequence of the region from 89.2 to 92.8 minutes."
Blattner F.R., Burland V.D., Plunkett G. III, Sofia H.J., Daniels D.L.
Nucleic Acids Res. 21:5408-5417(1993) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: K12 / MG1655 / ATCC 47076.
[4]"The complete genome sequence of Escherichia coli K-12."
Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V., Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F., Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B., Shao Y.
Science 277:1453-1462(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: K12 / MG1655 / ATCC 47076.
[5]"Highly accurate genome sequences of Escherichia coli K-12 strains MG1655 and W3110."
Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S., Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.
Mol. Syst. Biol. 2:E1-E5(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
[6]"Nucleotide sequence of the proximal portion of the RNA polymerase beta subunit gene of Escherichia coli."
Delcuve G., Downing W., Lewis H., Dennis P.P.
Gene 11:367-373(1980) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-391.
[7]"The nucleotide sequence at the proximal end of rpoB gene of Escherichia coli."
Gurevich A.I., Avakov A.E., Kolosov M.N.
Bioorg. Khim. 5:1735-1739(1979)
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-188.
[8]"Primary structure of RNA polymerase from E.coli: nucleotide sequence of the rpoB gene fragment and corresponding N-terminal amino acid sequence of the beta-subunit."
Monastyrskaya G.S., Gubanov V.V., Guryev S.O., Lipkin V.M., Sverdlov E.D.
Bioorg. Khim. 6:1423-1426(1980)
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-188.
[9]"Nucleotide sequence of the ribosomal protein gene cluster adjacent to the gene for RNA polymerase subunit beta in Escherichia coli."
Post L.E., Strycharz G.D., Nomura M., Lewis H., Dennis P.P.
Proc. Natl. Acad. Sci. U.S.A. 76:1697-1701(1979) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-33.
[10]"The subunits of DNA-dependent RNA polymerase from E. coli: I. Amino acid analysis and primary structure of the N-terminal regions."
Fujiki H., Zurek G.
FEBS Lett. 55:242-244(1975) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 1-4.
Strain: K12.
[11]"Primary structure of RNA polymerase from E. coli; nucleotide sequence of EcoR1-C fragment of gene rpoB and amino acid sequence of the corresponding fragment of beta-subunit."
Ovchinnikov Y.A., Sverdlov E.D., Lipkin V.M., Monastyrskaya G.S., Chertov O.Y., Gubanov V.V., Guryev S.O., Modyanov N.N., Grinkevich V.A., Makarova I.A., Marchenko T.V., Polovnikova I.N.
Bioorg. Khim. 6:655-665(1980)
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 187-1144.
[12]"The nucleotide sequence of strong RNA polymerase binding site within the E.coli rpoB structural gene."
Sverdlov E.D., Lipkin V.M., Monastyrskaya G.S., Gubanov V.V., Guryev S.O., Chertov O.Y.
Bioorg. Khim. 6:309-312(1980)
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 187-354.
[13]"RNA polymerase beta-subunit."
Mollet C., Drancourt M., Raoult D.
Submitted (NOV-1996) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 500-669.
Strain: ATCC 25290.
[14]"Structure of a central part of E.coli operon rpoBC. Nucleotide sequence of the gene for beta subunit of RNA polymerase."
Gurevich A.I., Igoshin A.V., Kolosov M.N.
Bioorg. Khim. 6:1580-1584(1980)
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1143-1342.
[15]"Bipartite functional map of the E. coli RNA polymerase alpha subunit: involvement of the C-terminal region in transcription activation by cAMP-CRP."
Igarashi K., Ishihama A.
Cell 65:1015-1022(1991) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION IN TRANSCRIPTION, SUBUNIT.
[16]"A beta subunit mutation disrupting the catalytic function of Escherichia coli RNA polymerase."
Lee J., Kashlev M., Borukhov S., Goldfarb A.
Proc. Natl. Acad. Sci. U.S.A. 88:6018-6022(1991) [PubMed] [Europe PMC] [Abstract]
Cited for: MUTAGENESIS OF GLU-813.
[17]"Escherichia coli proteome analysis using the gene-protein database."
VanBogelen R.A., Abshire K.Z., Moldover B., Olson E.R., Neidhardt F.C.
Electrophoresis 18:1243-1251(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY 2D-GEL.
[18]"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 C.F., Grishin N.V., Zhao Y.
Mol. Cell. Proteomics 8:215-225(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-1022 AND LYS-1200, IDENTIFICATION BY MASS SPECTROMETRY.
Strain: K12 / JW1106 and K12 / MG1655 / ATCC 47076.
[19]"Three-dimensional EM structure of an intact activator-dependent transcription initiation complex."
Hudson B.P., Quispe J., Lara-Gonzalez S., Kim Y., Berman H.M., Arnold E., Ebright R.H., Lawson C.L.
Proc. Natl. Acad. Sci. U.S.A. 106:19830-19835(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: STRUCTURE BY ELECTRON MICROSCOPY (19.80 ANGSTROMS) IN COMPLEX WITH RPOA; RPOC; RPOD; RPOZ; CRP AND DNA, DNA-BINDING, SUBUNIT.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
V00339 Genomic DNA. Translation: CAA23625.1.
V00340 Genomic DNA. Translation: CAA23627.1.
U76222 Genomic DNA. Translation: AAB18647.1.
U00006 Genomic DNA. Translation: AAC43085.1.
U00096 Genomic DNA. Translation: AAC76961.1.
AP009048 Genomic DNA. Translation: BAE77333.1.
V00341 Genomic DNA. Translation: CAA23629.1.
M38292 Genomic DNA. Translation: AAA24579.1.
M38293 Genomic DNA. Translation: AAA24581.1.
M38287 Genomic DNA. Translation: AAA24585.1.
M38304 Genomic DNA. Translation: AAA24580.1.
U77436 Genomic DNA. Translation: AAD09605.1.
M38303 Genomic DNA. Translation: AAA24583.1.
PIRRNECB. F65205.
RefSeqNP_418414.1. NC_000913.3.
YP_491474.1. NC_007779.1.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
3IYDelectron microscopy-C1-1342[»]
3LTIX-ray1.60A152-443[»]
3LU0electron microscopy-C1-1342[»]
3T72X-ray4.33o/q896-910[»]
3TBIX-ray3.00B831-1057[»]
4IGCX-ray3.70C/H1-1342[»]
4JK1X-ray3.90C/H1-1342[»]
4JK2X-ray4.20C/H1-1342[»]
4KMUX-ray3.85C/H1-1342[»]
4KN4X-ray3.96C/H1-1342[»]
4KN7X-ray3.69C/H1-1342[»]
ProteinModelPortalP0A8V2.
SMRP0A8V2. Positions 3-1342.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid852782. 1 interaction.
DIPDIP-35777N.
IntActP0A8V2. 99 interactions.
MINTMINT-1222430.
STRING511145.b3987.

Chemistry

BindingDBP0A8V2.
ChEMBLCHEMBL1852.
DrugBankDB01045. Rifampin.
DB01220. Rifaximin.

2D gel databases

SWISS-2DPAGEP0A8V2.

Proteomic databases

PaxDbP0A8V2.
PRIDEP0A8V2.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAC76961; AAC76961; b3987.
BAE77333; BAE77333; BAE77333.
GeneID12934478.
948488.
KEGGecj:Y75_p3210.
eco:b3987.
PATRIC32123495. VBIEscCol129921_4100.

Organism-specific databases

EchoBASEEB0887.
EcoGeneEG10894. rpoB.

Phylogenomic databases

eggNOGCOG0085.
HOGENOMHOG000218612.
KOK03043.
OMANPKRYDL.
OrthoDBEOG6M9DS6.
PhylomeDBP0A8V2.
ProtClustDBPRK00405.

Enzyme and pathway databases

BioCycEcoCyc:RPOB-MONOMER.
ECOL316407:JW3950-MONOMER.
MetaCyc:RPOB-MONOMER.

Gene expression databases

GenevestigatorP0A8V2.

Family and domain databases

Gene3D2.30.150.10. 1 hit.
2.40.270.10. 2 hits.
2.40.50.150. 2 hits.
3.90.1110.10. 2 hits.
HAMAPMF_01321. RNApol_bact_RpoB.
InterProIPR010243. 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.
[Graphical view]
PANTHERPTHR20856. PTHR20856. 1 hit.
PTHR20856:SF3. PTHR20856:SF3. 1 hit.
PfamPF04563. RNA_pol_Rpb2_1. 1 hit.
PF04561. RNA_pol_Rpb2_2. 2 hits.
PF04565. RNA_pol_Rpb2_3. 1 hit.
PF10385. RNA_pol_Rpb2_45. 1 hit.
PF00562. RNA_pol_Rpb2_6. 1 hit.
PF04560. RNA_pol_Rpb2_7. 1 hit.
[Graphical view]
TIGRFAMsTIGR02013. rpoB. 1 hit.
PROSITEPS01166. RNA_POL_BETA. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceP0A8V2.
PROP0A8V2.

Entry information

Entry nameRPOB_ECOLI
AccessionPrimary (citable) accession number: P0A8V2
Secondary accession number(s): P00575 expand/collapse secondary AC list , P00576, P78242, Q2M8S3
Entry history
Integrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: June 7, 2005
Last modified: April 16, 2014
This is version 96 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

Escherichia coli

Escherichia coli (strain K12): entries and cross-references to EcoGene