Reviewed,
UniProtKB/Swiss-Prot P0A8T7 (RPOC_ECOLI)
Last modified
November 3, 2009.
Version 48.
History...
Clusters with 100%,
90%,
50% identity |
Documents (3) |
Third-party data |
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Names and origin
| Protein names | Recommended name: DNA-directed RNA polymerase subunit beta' Short name=RNAP subunit beta' EC=2.7.7.6 Alternative name(s): Transcriptase subunit beta' RNA polymerase subunit beta' | ||||||
| Gene names |
| ||||||
| Organism | Escherichia coli (strain K12) [Complete proteome] [HAMAP] | ||||||
| Taxonomic identifier | 83333 [NCBI] | ||||||
| Taxonomic lineage | Bacteria › Proteobacteria › Gammaproteobacteria › Enterobacteriales › Enterobacteriaceae › Escherichia |
Protein attributes
| Sequence length | 1407 AA. |
| Sequence status | Complete. |
| Sequence processing | The displayed sequence is not processed. |
| Protein existence | Evidence 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. HAMAP MF_01322 |
| Catalytic activity | Nucleoside triphosphate + RNA(n) = diphosphate + RNA(n+1). HAMAP MF_01322 |
| 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 By similarity. |
| Sequence similarities | Belongs to the RNA polymerase beta' chain family. |
Ontologies
| Keywords | |
|---|---|
| Biological process | Transcription |
| Cellular component | DNA-directed RNA polymerase |
| Molecular function | Nucleotidyltransferase Transferase |
| PTM | Acetylation |
| Technical term | 3D-structure Complete proteome Direct protein sequencing |
| Gene Ontology (GO) | |
| Biological process | transcription, DNA-dependent Inferred from electronic annotation. Source: HAMAP |
| Cellular component | cytoplasm Inferred from direct assay. Source: UniProtKB membraneInferred from direct assay. Source: UniProtKB |
| Molecular function | DNA binding Inferred from electronic annotation. Source: HAMAP DNA-directed RNA polymerase activityInferred from electronic annotation. Source: HAMAP protein bindingInferred from physical interaction. Source: IntAct |
| Complete GO annotation... | |
Binary interactions
With | Entry | #Exp. | IntAct | Notes |
|---|---|---|---|---|
| adk | P69441 | 1 | EBI-543604,EBI-543592 | |
| htpG | P0A6Z3 | 1 | EBI-543604,EBI-369221 | |
| rpoD | P00579 | 1 | EBI-543604,EBI-545104 |
Sequence annotation (Features)
| Feature key | Position(s) | Length | Description | Graphical view | Feature identifier | ||||||||||||||||||||||||||||||||||||||||||||
Molecule processing | |||||||||||||||||||||||||||||||||||||||||||||||||
|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|
| Chain | 1 – 1407 | 1407 | DNA-directed RNA polymerase subunit beta' HAMAP MF_01322 | PRO_0000067741 | |||||||||||||||||||||||||||||||||||||||||||||
Amino acid modifications | |||||||||||||||||||||||||||||||||||||||||||||||||
| Modified residue | 983 | 1 | N6-acetyllysine Ref.11 | ||||||||||||||||||||||||||||||||||||||||||||||
Experimental info | |||||||||||||||||||||||||||||||||||||||||||||||||
| Sequence conflict | 1133 – 1177 | 45 | DITGG…RRLVI → ASPVVCRALRTCSKHVVRKS RQSWLKSAVSFPSVKKPKVN VVWLS Ref.10 | ||||||||||||||||||||||||||||||||||||||||||||||
Secondary structure | |||||||||||||||||||||||||||||||||||||||||||||||||
Helix Strand Turn | |||||||||||||||||||||||||||||||||||||||||||||||||
| Helix | 945 – 948 | 4 | |||||||||||||||||||||||||||||||||||||||||||||||
| Beta strand | 949 – 951 | 3 | |||||||||||||||||||||||||||||||||||||||||||||||
| Beta strand | 954 – 962 | 9 | |||||||||||||||||||||||||||||||||||||||||||||||
| Beta strand | 965 – 967 | 3 | |||||||||||||||||||||||||||||||||||||||||||||||
| Beta strand | 973 – 975 | 3 | |||||||||||||||||||||||||||||||||||||||||||||||
| Beta strand | 981 – 985 | 5 | |||||||||||||||||||||||||||||||||||||||||||||||
| Beta strand | 991 – 996 | 6 | |||||||||||||||||||||||||||||||||||||||||||||||
| Beta strand | 1002 – 1005 | 4 | |||||||||||||||||||||||||||||||||||||||||||||||
| Beta strand | 1016 – 1019 | 4 | |||||||||||||||||||||||||||||||||||||||||||||||
| Beta strand | 1022 – 1028 | 7 | |||||||||||||||||||||||||||||||||||||||||||||||
| Beta strand | 1033 – 1039 | 7 | |||||||||||||||||||||||||||||||||||||||||||||||
| Turn | 1042 – 1044 | 3 | |||||||||||||||||||||||||||||||||||||||||||||||
| Beta strand | 1045 – 1050 | 6 | |||||||||||||||||||||||||||||||||||||||||||||||
| Turn | 1052 – 1054 | 3 | |||||||||||||||||||||||||||||||||||||||||||||||
| Beta strand | 1057 – 1061 | 5 | |||||||||||||||||||||||||||||||||||||||||||||||
| Turn | 1064 – 1066 | 3 | |||||||||||||||||||||||||||||||||||||||||||||||
| Turn | 1070 – 1073 | 4 | |||||||||||||||||||||||||||||||||||||||||||||||
| Beta strand | 1077 – 1081 | 5 | |||||||||||||||||||||||||||||||||||||||||||||||
| Beta strand | 1098 – 1100 | 3 | |||||||||||||||||||||||||||||||||||||||||||||||
| Beta strand | 1106 – 1109 | 4 | |||||||||||||||||||||||||||||||||||||||||||||||
| Beta strand | 1120 – 1125 | 6 | |||||||||||||||||||||||||||||||||||||||||||||||
Sequences
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References
| « Hide 'large scale' references | |
| [1] | "The primary structure of E. coli RNA polymerase, Nucleotide sequence of the rpoC gene and amino acid sequence of the beta'-subunit." Ovchinnikov Y.A., Monastyrskaya G.S., Gubanov V.V., Guryev S.O., Salomatina I.S., Shuvaeva T.M., Lipkin V.M., Sverdlov E.D. Nucleic Acids Res. 10:4035-4044(1982) [PubMed: 6287430] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 1-8, PARTIAL PROTEIN SEQUENCE. |
| [2] | "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: 8265357] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: K12 / MG1655 / ATCC 47076. |
| [3] | "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 277:1453-1474(1997) [PubMed: 9278503] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: K12 / MG1655 / ATCC 47076. |
| [4] | "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: 16738553] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: K12 / W3110 / ATCC 27325 / DSM 5911. |
| [5] | "Primary structure of EcoRI-F fragment of rpoB, C genes and corresponding fragments of beta- and beta'-subunits of RNA polymerase from E.coli." Monastyrskaya G.S., Gubanov V.V., Guryev S.O., Lipkin V.M., Sverdlov E.D. Bioorg. Khim. 6:1106-1109(1980) Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-176. |
| [6] | "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 1-176. |
| [7] | "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: 6266829] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-176, PROTEIN SEQUENCE OF 1-8. |
| [8] | "Primary structure of EcoRI-D fragment of rpoC gene and corresponding fragment of beta-subunit of RNA polymerase from E.coli." Monastyrskaya G.S., Guryev S.O., Kalinina N.F., Sorokin A.V., Salomatina I.S., Shuvaeva T.M., Lipkin V.M., Sverdlov E.D., Ovchinnikov Y.A. Bioorg. Khim. 8:130-134(1982) Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 175-988. |
| [9] | "Primary structure of RNA polymerase from E.coli. Nucleotide sequence of E.coli DNA fragment containing a part of the rpoC gene and the corresponding C-terminal amino acid sequence of beta'-subunit." Ovchinnikov Y.A., Monastyrskaya G.S., Gubanov V.V., Salomatina I.S., Shuvaeva T.M., Lipkin V.M., Sverdlov E.D. Bioorg. Khim. 7:1107-1112(1981) Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 987-1407. |
| [10] | "Nucleotide sequence at the end of the gene for the RNA polymerase beta' subunit (rpoC)." Squires C., Krainer A., Barry G., Shen W.-F., Squires C.L. Nucleic Acids Res. 9:6827-6840(1981) [PubMed: 6278450] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1073-1407. Strain: K12. |
| [11] | "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: 18723842] [Abstract] Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-983, MASS SPECTROMETRY. |
| + | Additional computationally mapped references. |
Cross-references
Sequence databases | |||||||||||||
|---|---|---|---|---|---|---|---|---|---|---|---|---|---|
| V00339 Genomic DNA. Translation: CAA23626.1. U00006 Genomic DNA. Translation: AAC43086.1. U00096 Genomic DNA. Translation: AAC76962.1. AP009048 Genomic DNA. Translation: BAE77332.1. M38293 Genomic DNA. Translation: AAA24582.1. M38303 Genomic DNA. Translation: AAA24584.1. Sequence problems. V00340 Genomic DNA. Translation: CAA23628.1. M38305 Genomic DNA. Translation: AAA24586.1. M38288 Genomic DNA. Translation: AAA24408.1. | |||||||||||||
| PIR | RNECC. A00695. | ||||||||||||
| RefSeq | AP_003831.1. NP_418415.1. | ||||||||||||
3D structure databases | |||||||||||||
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| ModBase | Search... | ||||||||||||
Protein-protein interaction databases | |||||||||||||
| IntAct | P0A8T7. 111 interactions. | ||||||||||||
| STRING | P0A8T7. | ||||||||||||
PTM databases | |||||||||||||
| PhosSite | P0A8T7. | ||||||||||||
2-D gel databases | |||||||||||||
| ECO2DBASE | I160.0. 6TH EDITION. | ||||||||||||
Proteomic databases | |||||||||||||
| PRIDE | P0A8T7. | ||||||||||||
Genome annotation databases | |||||||||||||
| GeneID | 948487. | ||||||||||||
| GenomeReviews | Gene locus JW3951 in contig AP009048_GR. Gene locus b3988 in contig U00096_GR. | ||||||||||||
| KEGG | ecj:JW3951. eco:b3988. | ||||||||||||
Organism-specific databases | |||||||||||||
| EchoBASE | EB0888. | ||||||||||||
| EcoGene | EG10895. rpoC. | ||||||||||||
| CMR | Search... | ||||||||||||
Phylogenomic databases | |||||||||||||
| HOGENOM | P0A8T7. | ||||||||||||
| OMA | HIGGAAQ. | ||||||||||||
Enzyme and pathway databases | |||||||||||||
| BioCyc | EcoCyc:RPOC-MON. | ||||||||||||
Gene expression databases | |||||||||||||
| Genevestigator | P0A8T7. | ||||||||||||
Family and domain databases | |||||||||||||
| HAMAP | MF_01322. [Tree] | ||||||||||||
| InterPro | IPR000722. RNA_pol_asu. IPR006592. RNA_pol_N. IPR007080. RNA_pol_Rpb1_1. IPR007066. RNA_pol_Rpb1_3. IPR007083. RNA_pol_Rpb1_4. IPR007081. RNA_pol_Rpb1_5. IPR012754. RpoC_beta_prime. [Graphical view] | ||||||||||||
| Gene3D | G3DSA:2.40.40.30. RNA_pol_A. 1 hit. G3DSA:3.90.1120.10. RNA_pol_Rpb1_1. 1 hit. | ||||||||||||
| Pfam | PF04997. RNA_pol_Rpb1_1. 1 hit. PF00623. RNA_pol_Rpb1_2. 1 hit. PF04983. RNA_pol_Rpb1_3. 1 hit. PF05000. RNA_pol_Rpb1_4. 1 hit. PF04998. RNA_pol_Rpb1_5. 1 hit. [Graphical view] | ||||||||||||
| SMART | SM00663. RPOLA_N. 1 hit. [Graphical view] | ||||||||||||
| TIGRFAMs | TIGR02386. rpoC_TIGR. 1 hit. | ||||||||||||
| ProtoNet | Search... | ||||||||||||
Entry information
| Entry name | RPOC_ECOLI | ||||||||
| Accession | Primary (citable) accession number: P0A8T7 Secondary accession number(s): P00577 Q2M8S4 | ||||||||
| Entry history |
| ||||||||
| Entry status | Reviewed (UniProtKB/Swiss-Prot) | ||||||||
| Annotation project | HAMAP (High-quality Automated and Manual Annotation of microbial Proteomes) | ||||||||
Relevant documents
| Escherichia coli Escherichia coli (strain K12): entries and cross-references to EcoGene |
| PDB cross-references Index of Protein Data Bank (PDB) cross-references |
| SIMILARITY comments Index of protein domains and families |

Clusters with


