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Annotation rule MF_01322
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General rule information [?]

Accession MF_01322
Dates 6-JAN-2004 (Created)
19-NOV-2019 (Last updated, Version 23)
Name RNApol_bact_RpoC
Scope
Bacteria; except Cyanobacteria
Templates P0A8T7 (RPOC_ECOLI); Q9KWU6 (RPOC_THEAQ): [Recover all]
Triggered by

Propagated annotation [?]


Identifier, protein and gene names [?]

Identifier
RPOC
Protein name
RecName: Full=DNA-directed RNA polymerase subunit beta';
Short=RNAP subunit beta';
EC 2.7.7.6;
AltName: Full=RNA polymerase subunit beta';
AltName: Full=Transcriptase subunit beta';
Gene name
rpoC

Comments [?]

Function DNA-dependent RNA polymerase catalyzes the transcription of DNA into RNA using the four ribonucleoside triphosphates as substrates.
Catalytic activity RHEA:21248: a ribonucleoside 5'-triphosphate + RNA(n) = diphosphate + RNA(n+1)
EC 2.7.7.6
case <FTGroup:2>
Cofactor Mg(2+)
Note: Binds 1 Mg(2+) ion per subunit.
end case
case <FTGroup:1> and <FTGroup:3>
Cofactor Zn(2+)
Note: Binds 2 Zn(2+) ions per subunit.
end case
Subunit 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.
Similarity Belongs to the RNA polymerase beta' chain family.

Keywords [?]

case (<OC:Escherichia> or <OC:Shigella>) and <FT:1>
Acetylation
end case
case <FTGroup:1> or <FTGroup:2> or <FTGroup:3>
Metal-binding
end case
case <FTGroup:2>
Magnesium
end case
Transcription
Transferase
Nucleotidyltransferase
DNA-directed RNA polymerase
case <FTGroup:1> or <FTGroup:3>
Zinc
end case

Gene Ontology [?]

GO:0003677; Molecular function: DNA binding.
GO:0003899; Molecular function: DNA-directed 5'-3' RNA polymerase activity.
case <FTGroup:2>
GO:0000287; Molecular function: magnesium ion binding.
end case
GO:0006351; Biological process: transcription, DNA-templated.
case <FTGroup:1> or <FTGroup:3>
GO:0008270; Molecular function: zinc ion binding.
end case

Cross-references [?]

Pfam PF04997; RNA_pol_Rpb1_1; 1;
PF00623; RNA_pol_Rpb1_2; 1-2;
PF04983; RNA_pol_Rpb1_3; 1;
PF05000; RNA_pol_Rpb1_4; 1;
PF04998; RNA_pol_Rpb1_5; 1-2;
TIGRFAMs TIGR02386; rpoC_TIGR; 1;

Features [?]

From: RPOC_ECOLI (P0A8T7)
Key     From     To       Description   Tag   Condition   FTGroup
METAL     70     70       Zinc 1     C   1
METAL     72     72       Zinc 1     C   1
METAL     85     85       Zinc 1     C   1
METAL     88     88       Zinc 1     C   1
METAL     460     460       Magnesium     D   2
METAL     462     462       Magnesium     D   2
METAL     464     464       Magnesium     D   2
METAL     814     814       Zinc 2     C   3
METAL     888     888       Zinc 2     C   3
METAL     895     895       Zinc 2     C   3
METAL     898     898       Zinc 2     C   3
case <OC:Escherichia> or <OC:Shigella>
MOD_RES     983     983       N6-acetyllysine     K  
end case

Additional information [?]

Size range 1135-1690 amino acids
Related rules MF_01323 (RPOC1); MF_01324 (RPOC2)
Fusion Nter: MF_01321 (rpoB), <Unknown>; Cter: None
Comments Fused with rpoB in Helicobacter species and least some Wolbachia, but not in other epsilon proteobateria. In Acholeplasmataceae there is an unknown N-terminal extension of about 110 amino acids. In cyanobacteria and chloroplasts this protein is split into two parts. The N-terminus is known as gamma in cyanobacteria and beta' in chloroplasts (MF_01323), while the C-terminus is known as beta' in cyanobacteria and beta'' in chloroplasts (MF_01324). Many Mycoplasma only have 1 Zn ion-binding site.


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