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P0A8V2

- RPOB_ECOLI

UniProt

P0A8V2 - RPOB_ECOLI

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Protein

DNA-directed RNA polymerase subunit beta

Gene

rpoB

Organism
Escherichia coli (strain K12)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli

Functioni

DNA-dependent RNA polymerase catalyzes the transcription of DNA into RNA using the four ribonucleoside triphosphates as substrates.1 Publication

Catalytic activityi

Nucleoside triphosphate + RNA(n) = diphosphate + RNA(n+1).

GO - Molecular functioni

  1. DNA binding Source: UniProtKB-HAMAP
  2. DNA-directed RNA polymerase activity Source: UniProtKB-HAMAP
  3. ribonucleoside binding Source: InterPro

GO - Biological processi

  1. transcription, DNA-templated Source: UniProtKB-HAMAP
Complete GO annotation...

Keywords - Molecular functioni

Nucleotidyltransferase, Transferase

Keywords - Biological processi

Transcription

Enzyme and pathway databases

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

Names & Taxonomyi

Protein namesi
Recommended name:
DNA-directed RNA polymerase subunit beta (EC:2.7.7.6)
Short name:
RNAP subunit beta
Alternative name(s):
RNA polymerase subunit beta
Transcriptase subunit beta
Gene namesi
Name:rpoB
Synonyms:groN, nitB, rif, ron, stl, stv, tabD
Ordered Locus Names:b3987, JW3950
OrganismiEscherichia coli (strain K12)
Taxonomic identifieri83333 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia
ProteomesiUP000000318: Chromosome, UP000000625: Chromosome

Organism-specific databases

EcoGeneiEG10894. rpoB.

Subcellular locationi

GO - Cellular componenti

  1. cytoplasm Source: UniProtKB
  2. membrane Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

DNA-directed RNA polymerase

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi813 – 8131E → K: Disrupts the enzyme's active center. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 13421342DNA-directed RNA polymerase subunit betaPRO_0000047892Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei1022 – 10221N6-acetyllysine1 Publication
Modified residuei1200 – 12001N6-acetyllysine1 Publication

Post-translational modificationi

Acetylated on several lysine residues in the presence of glucose.2 Publications

Keywords - PTMi

Acetylation

Proteomic databases

PaxDbiP0A8V2.
PRIDEiP0A8V2.

2D gel databases

SWISS-2DPAGEP0A8V2.

Expressioni

Gene expression databases

GenevestigatoriP0A8V2.

Interactioni

Subunit structurei

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.2 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
rapAP602403EBI-544996,EBI-551542
rpoCP0A8T77EBI-544996,EBI-543604

Protein-protein interaction databases

BioGridi852782. 1 interaction.
DIPiDIP-35777N.
IntActiP0A8V2. 99 interactions.
MINTiMINT-1222430.
STRINGi511145.b3987.

Structurei

Secondary structure

1
1342
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi154 – 1596Combined sources
Beta strandi172 – 1776Combined sources
Beta strandi179 – 1813Combined sources
Beta strandi184 – 1885Combined sources
Beta strandi194 – 1985Combined sources
Helixi207 – 2126Combined sources
Helixi217 – 2248Combined sources
Beta strandi227 – 2337Combined sources
Beta strandi236 – 2405Combined sources
Helixi243 – 2464Combined sources
Beta strandi255 – 2573Combined sources
Beta strandi260 – 2634Combined sources
Helixi271 – 2799Combined sources
Beta strandi284 – 2863Combined sources
Helixi289 – 2935Combined sources
Beta strandi295 – 2973Combined sources
Turni304 – 3063Combined sources
Beta strandi309 – 3113Combined sources
Helixi319 – 3279Combined sources
Beta strandi332 – 3365Combined sources
Beta strandi340 – 3434Combined sources
Helixi346 – 3538Combined sources
Helixi359 – 37012Combined sources
Helixi378 – 38912Combined sources
Turni392 – 3943Combined sources
Helixi398 – 40811Combined sources
Helixi422 – 43716Combined sources
Beta strandi832 – 84312Combined sources
Beta strandi849 – 8524Combined sources
Helixi859 – 8635Combined sources
Beta strandi869 – 8713Combined sources
Beta strandi882 – 8843Combined sources
Beta strandi886 – 8894Combined sources
Helixi892 – 8943Combined sources
Helixi897 – 90610Combined sources
Beta strandi913 – 9153Combined sources
Beta strandi925 – 93612Combined sources
Helixi943 – 98038Combined sources
Helixi986 – 9916Combined sources
Helixi994 – 9963Combined sources
Turni997 – 9993Combined sources
Beta strandi1003 – 10053Combined sources
Helixi1006 – 103732Combined sources
Beta strandi1046 – 105611Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
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[»]
4MEXX-ray3.90C/I1-1342[»]
4MEYX-ray3.95C/I1-1342[»]
ProteinModelPortaliP0A8V2.
SMRiP0A8V2. Positions 3-1342.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP0A8V2.

Family & Domainsi

Sequence similaritiesi

Belongs to the RNA polymerase beta chain family.Curated

Phylogenomic databases

eggNOGiCOG0085.
HOGENOMiHOG000218612.
InParanoidiP0A8V2.
KOiK03043.
OMAiICPANME.
OrthoDBiEOG6M9DS6.
PhylomeDBiP0A8V2.

Family and domain databases

Gene3Di2.30.150.10. 1 hit.
2.40.270.10. 2 hits.
2.40.50.150. 2 hits.
3.90.1110.10. 2 hits.
HAMAPiMF_01321. RNApol_bact_RpoB.
InterProiIPR010243. 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]
PANTHERiPTHR20856. PTHR20856. 1 hit.
PfamiPF04563. 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]
TIGRFAMsiTIGR02013. rpoB. 1 hit.
PROSITEiPS01166. RNA_POL_BETA. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P0A8V2-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MVYSYTEKKR IRKDFGKRPQ VLDVPYLLSI QLDSFQKFIE QDPEGQYGLE
60 70 80 90 100
AAFRSVFPIQ SYSGNSELQY VSYRLGEPVF DVQECQIRGV TYSAPLRVKL
110 120 130 140 150
RLVIYEREAP EGTVKDIKEQ EVYMGEIPLM TDNGTFVING TERVIVSQLH
160 170 180 190 200
RSPGVFFDSD KGKTHSSGKV LYNARIIPYR GSWLDFEFDP KDNLFVRIDR
210 220 230 240 250
RRKLPATIIL RALNYTTEQI LDLFFEKVIF EIRDNKLQME LVPERLRGET
260 270 280 290 300
ASFDIEANGK VYVEKGRRIT ARHIRQLEKD DVKLIEVPVE YIAGKVVAKD
310 320 330 340 350
YIDESTGELI CAANMELSLD LLAKLSQSGH KRIETLFTND LDHGPYISET
360 370 380 390 400
LRVDPTNDRL SALVEIYRMM RPGEPPTREA AESLFENLFF SEDRYDLSAV
410 420 430 440 450
GRMKFNRSLL REEIEGSGIL SKDDIIDVMK KLIDIRNGKG EVDDIDHLGN
460 470 480 490 500
RRIRSVGEMA ENQFRVGLVR VERAVKERLS LGDLDTLMPQ DMINAKPISA
510 520 530 540 550
AVKEFFGSSQ LSQFMDQNNP LSEITHKRRI SALGPGGLTR ERAGFEVRDV
560 570 580 590 600
HPTHYGRVCP IETPEGPNIG LINSLSVYAQ TNEYGFLETP YRKVTDGVVT
610 620 630 640 650
DEIHYLSAIE EGNYVIAQAN SNLDEEGHFV EDLVTCRSKG ESSLFSRDQV
660 670 680 690 700
DYMDVSTQQV VSVGASLIPF LEHDDANRAL MGANMQRQAV PTLRADKPLV
710 720 730 740 750
GTGMERAVAV DSGVTAVAKR GGVVQYVDAS RIVIKVNEDE MYPGEAGIDI
760 770 780 790 800
YNLTKYTRSN QNTCINQMPC VSLGEPVERG DVLADGPSTD LGELALGQNM
810 820 830 840 850
RVAFMPWNGY NFEDSILVSE RVVQEDRFTT IHIQELACVS RDTKLGPEEI
860 870 880 890 900
TADIPNVGEA ALSKLDESGI VYIGAEVTGG DILVGKVTPK GETQLTPEEK
910 920 930 940 950
LLRAIFGEKA SDVKDSSLRV PNGVSGTVID VQVFTRDGVE KDKRALEIEE
960 970 980 990 1000
MQLKQAKKDL SEELQILEAG LFSRIRAVLV AGGVEAEKLD KLPRDRWLEL
1010 1020 1030 1040 1050
GLTDEEKQNQ LEQLAEQYDE LKHEFEKKLE AKRRKITQGD DLAPGVLKIV
1060 1070 1080 1090 1100
KVYLAVKRRI QPGDKMAGRH GNKGVISKIN PIEDMPYDEN GTPVDIVLNP
1110 1120 1130 1140 1150
LGVPSRMNIG QILETHLGMA AKGIGDKINA MLKQQQEVAK LREFIQRAYD
1160 1170 1180 1190 1200
LGADVRQKVD LSTFSDEEVM RLAENLRKGM PIATPVFDGA KEAEIKELLK
1210 1220 1230 1240 1250
LGDLPTSGQI RLYDGRTGEQ FERPVTVGYM YMLKLNHLVD DKMHARSTGS
1260 1270 1280 1290 1300
YSLVTQQPLG GKAQFGGQRF GEMEVWALEA YGAAYTLQEM LTVKSDDVNG
1310 1320 1330 1340
RTKMYKNIVD GNHQMEPGMP ESFNVLLKEI RSLGINIELE DE
Length:1,342
Mass (Da):150,632
Last modified:June 7, 2005 - v1
Checksum:iF9E95344C54AB118
GO

Sequence cautioni

The sequence described in 1 Publication differs from that shown. Reason: Curated

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti4 – 41S → R AA sequence (PubMed:1095419)Curated
Sequence conflicti106 – 1072ER → G in CAA23629. (PubMed:7011900)Curated
Sequence conflicti384 – 3918LFENLFFS → CSRTCSSPT in CAA23629. (PubMed:7011900)Curated
Sequence conflicti516 – 5161D → V in CAA23625. (PubMed:6266829)Curated
Sequence conflicti516 – 5161D → V in CAA23627. (PubMed:6266829)Curated
Sequence conflicti516 – 5161D → V in AAA24585. 1 PublicationCurated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
PIRiF65205. RNECB.
RefSeqiNP_418414.1. NC_000913.3.
YP_491474.1. NC_007779.1.

Genome annotation databases

EnsemblBacteriaiAAC76961; AAC76961; b3987.
BAE77333; BAE77333; BAE77333.
GeneIDi12934478.
948488.
KEGGiecj:Y75_p3210.
eco:b3987.
PATRICi32123495. VBIEscCol129921_4100.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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 .
PIRi F65205. RNECB.
RefSeqi NP_418414.1. NC_000913.3.
YP_491474.1. NC_007779.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
3IYD electron microscopy - C 1-1342 [» ]
3LTI X-ray 1.60 A 152-443 [» ]
3LU0 electron microscopy - C 1-1342 [» ]
3T72 X-ray 4.33 o/q 896-910 [» ]
3TBI X-ray 3.00 B 831-1057 [» ]
4IGC X-ray 3.70 C/H 1-1342 [» ]
4JK1 X-ray 3.90 C/H 1-1342 [» ]
4JK2 X-ray 4.20 C/H 1-1342 [» ]
4KMU X-ray 3.85 C/H 1-1342 [» ]
4KN4 X-ray 3.96 C/H 1-1342 [» ]
4KN7 X-ray 3.69 C/H 1-1342 [» ]
4MEX X-ray 3.90 C/I 1-1342 [» ]
4MEY X-ray 3.95 C/I 1-1342 [» ]
ProteinModelPortali P0A8V2.
SMRi P0A8V2. Positions 3-1342.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 852782. 1 interaction.
DIPi DIP-35777N.
IntActi P0A8V2. 99 interactions.
MINTi MINT-1222430.
STRINGi 511145.b3987.

Chemistry

BindingDBi P0A8V2.
ChEMBLi CHEMBL1852.
DrugBanki DB00615. Rifabutin.
DB01045. Rifampicin.
DB01220. Rifaximin.

2D gel databases

SWISS-2DPAGE P0A8V2.

Proteomic databases

PaxDbi P0A8V2.
PRIDEi P0A8V2.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblBacteriai AAC76961 ; AAC76961 ; b3987 .
BAE77333 ; BAE77333 ; BAE77333 .
GeneIDi 12934478.
948488.
KEGGi ecj:Y75_p3210.
eco:b3987.
PATRICi 32123495. VBIEscCol129921_4100.

Organism-specific databases

EchoBASEi EB0887.
EcoGenei EG10894. rpoB.

Phylogenomic databases

eggNOGi COG0085.
HOGENOMi HOG000218612.
InParanoidi P0A8V2.
KOi K03043.
OMAi ICPANME.
OrthoDBi EOG6M9DS6.
PhylomeDBi P0A8V2.

Enzyme and pathway databases

BioCyci EcoCyc:RPOB-MONOMER.
ECOL316407:JW3950-MONOMER.
MetaCyc:RPOB-MONOMER.

Miscellaneous databases

EvolutionaryTracei P0A8V2.
PROi P0A8V2.

Gene expression databases

Genevestigatori P0A8V2.

Family and domain databases

Gene3Di 2.30.150.10. 1 hit.
2.40.270.10. 2 hits.
2.40.50.150. 2 hits.
3.90.1110.10. 2 hits.
HAMAPi MF_01321. RNApol_bact_RpoB.
InterProi 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.
[Graphical view ]
PANTHERi PTHR20856. PTHR20856. 1 hit.
Pfami PF04563. 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 ]
TIGRFAMsi TIGR02013. rpoB. 1 hit.
PROSITEi PS01166. RNA_POL_BETA. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  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. 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. "Involvement of protein acetylation in glucose-induced transcription of a stress-responsive promoter."
    Lima B.P., Antelmann H., Gronau K., Chi B.K., Becher D., Brinsmade S.R., Wolfe A.J.
    Mol. Microbiol. 81:1190-1204(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: ACETYLATION.
  20. "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.

Entry informationi

Entry nameiRPOB_ECOLI
AccessioniPrimary (citable) accession number: P0A8V2
Secondary accession number(s): P00575
, P00576, P78242, Q2M8S3
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: June 7, 2005
Last modified: November 26, 2014
This is version 102 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. Escherichia coli
    Escherichia coli (strain K12): entries and cross-references to EcoGene
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3