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P0A8V2

- RPOB_ECOLI

UniProt

P0A8V2 - RPOB_ECOLI

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
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    • History
      Entry version 100 (01 Oct 2014)
      Sequence version 1 (07 Jun 2005)
      Previous versions | rss
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    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. protein binding Source: IntAct
    4. ribonucleoside binding Source: InterPro

    GO - Biological processi

    1. transcription, DNA-templated Source: UniProtKB-HAMAP

    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

    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-acetyllysine2 Publications
    Modified residuei1200 – 12001N6-acetyllysine2 Publications

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

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    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.
    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

    MVYSYTEKKR IRKDFGKRPQ VLDVPYLLSI QLDSFQKFIE QDPEGQYGLE     50
    AAFRSVFPIQ SYSGNSELQY VSYRLGEPVF DVQECQIRGV TYSAPLRVKL 100
    RLVIYEREAP EGTVKDIKEQ EVYMGEIPLM TDNGTFVING TERVIVSQLH 150
    RSPGVFFDSD KGKTHSSGKV LYNARIIPYR GSWLDFEFDP KDNLFVRIDR 200
    RRKLPATIIL RALNYTTEQI LDLFFEKVIF EIRDNKLQME LVPERLRGET 250
    ASFDIEANGK VYVEKGRRIT ARHIRQLEKD DVKLIEVPVE YIAGKVVAKD 300
    YIDESTGELI CAANMELSLD LLAKLSQSGH KRIETLFTND LDHGPYISET 350
    LRVDPTNDRL SALVEIYRMM RPGEPPTREA AESLFENLFF SEDRYDLSAV 400
    GRMKFNRSLL REEIEGSGIL SKDDIIDVMK KLIDIRNGKG EVDDIDHLGN 450
    RRIRSVGEMA ENQFRVGLVR VERAVKERLS LGDLDTLMPQ DMINAKPISA 500
    AVKEFFGSSQ LSQFMDQNNP LSEITHKRRI SALGPGGLTR ERAGFEVRDV 550
    HPTHYGRVCP IETPEGPNIG LINSLSVYAQ TNEYGFLETP YRKVTDGVVT 600
    DEIHYLSAIE EGNYVIAQAN SNLDEEGHFV EDLVTCRSKG ESSLFSRDQV 650
    DYMDVSTQQV VSVGASLIPF LEHDDANRAL MGANMQRQAV PTLRADKPLV 700
    GTGMERAVAV DSGVTAVAKR GGVVQYVDAS RIVIKVNEDE MYPGEAGIDI 750
    YNLTKYTRSN QNTCINQMPC VSLGEPVERG DVLADGPSTD LGELALGQNM 800
    RVAFMPWNGY NFEDSILVSE RVVQEDRFTT IHIQELACVS RDTKLGPEEI 850
    TADIPNVGEA ALSKLDESGI VYIGAEVTGG DILVGKVTPK GETQLTPEEK 900
    LLRAIFGEKA SDVKDSSLRV PNGVSGTVID VQVFTRDGVE KDKRALEIEE 950
    MQLKQAKKDL SEELQILEAG LFSRIRAVLV AGGVEAEKLD KLPRDRWLEL 1000
    GLTDEEKQNQ LEQLAEQYDE LKHEFEKKLE AKRRKITQGD DLAPGVLKIV 1050
    KVYLAVKRRI QPGDKMAGRH GNKGVISKIN PIEDMPYDEN GTPVDIVLNP 1100
    LGVPSRMNIG QILETHLGMA AKGIGDKINA MLKQQQEVAK LREFIQRAYD 1150
    LGADVRQKVD LSTFSDEEVM RLAENLRKGM PIATPVFDGA KEAEIKELLK 1200
    LGDLPTSGQI RLYDGRTGEQ FERPVTVGYM YMLKLNHLVD DKMHARSTGS 1250
    YSLVTQQPLG GKAQFGGQRF GEMEVWALEA YGAAYTLQEM LTVKSDDVNG 1300
    RTKMYKNIVD GNHQMEPGMP ESFNVLLKEI RSLGINIELE DE 1342
    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:

    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:
    EMBL
    GenBank
    DDBJ
    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:
    EMBL
    GenBank
    DDBJ
    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:
    PDBe
    RCSB PDB
    PDBj
    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 DB01045. Rifampin.
    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.
    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

    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: October 1, 2014
    This is version 100 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