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HAMAP rule MF_01322

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General rule information [?]

Accession MF_01322
Dates 6-JAN-2004 (Created)
2-SEP-2024 (Last updated, Version 31)
Name RNApol_bact_RpoC
Scope(s) Bacteria
Template(s) P0A8T7 (RPOC_ECOLI); Q9KWU6 (RPOC_THEAQ); [ Recover all ]
Triggered by HAMAP; MF_01322 (Get profile general information and statistics)

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 Name=rpoC;

Comments [?]

FUNCTIONDNA-dependent RNA polymerase catalyzes the transcription of DNA into RNA using the four ribonucleoside triphosphates as substrates.
CATALYTIC ACTIVITY Reaction=RNA(n) + a ribonucleoside 5'-triphosphate = RNA(n+1) + diphosphate; Xref=Rhea:RHEA:21248, Rhea:RHEA-COMP:14527, Rhea:RHEA- COMP:17342, ChEBI:CHEBI:33019, ChEBI:CHEBI:61557, ChEBI:CHEBI:140395; EC=2.7.7.6;
case <FTGroup:2>
COFACTOR Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Note=Binds 1 Mg(2+) ion per subunit.;
end case
case <FTGroup:1> and <FTGroup:3>
COFACTOR Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Note=Binds 2 Zn(2+) ions per subunit.;
end case
SUBUNITThe 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.
SIMILARITYBelongs 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:DNA-templated transcription
case <FTGroup:1> or <FTGroup:3>
GO:0008270; Molecular function:zinc ion binding
end case

Cross-references [?]

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

Features [?]

From: RPOC_ECOLI (P0A8T7)
Key From To Description Tag Condition FTGroup
BINDING 70 70 /ligand="Zn(2+)"
/ligand_id="ChEBI:CHEBI:29105"
/ligand_label="1"		 C 1
BINDING 72 72 /ligand="Zn(2+)"
/ligand_id="ChEBI:CHEBI:29105"
/ligand_label="1"		 C 1
BINDING 85 85 /ligand="Zn(2+)"
/ligand_id="ChEBI:CHEBI:29105"
/ligand_label="1"		 C 1
BINDING 88 88 /ligand="Zn(2+)"
/ligand_id="ChEBI:CHEBI:29105"
/ligand_label="1"		 C 1
BINDING 460 460 /ligand="Mg(2+)"
/ligand_id="ChEBI:CHEBI:18420"		 D 2
BINDING 462 462 /ligand="Mg(2+)"
/ligand_id="ChEBI:CHEBI:18420"		 D 2
BINDING 464 464 /ligand="Mg(2+)"
/ligand_id="ChEBI:CHEBI:18420"		 D 2
BINDING 814 814 /ligand="Zn(2+)"
/ligand_id="ChEBI:CHEBI:29105"
/ligand_label="2"		 C 3
BINDING 888 888 /ligand="Zn(2+)"
/ligand_id="ChEBI:CHEBI:29105"
/ligand_label="2"		 C 3
BINDING 895 895 /ligand="Zn(2+)"
/ligand_id="ChEBI:CHEBI:29105"
/ligand_label="2"		 C 3
BINDING 898 898 /ligand="Zn(2+)"
/ligand_id="ChEBI:CHEBI:29105"
/ligand_label="2"		 C 3
case <OC:Escherichia> or <OC:Shigella>
MOD_RES 983 983 /note="N6-acetyllysine" K
end case

Additional information [?]

Size range 1135-1690 amino acids
Related rules MF_01323
MF_01324
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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