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HAMAP rule MF_01323

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General rule information [?]

Accession MF_01323
Dates 6-JAN-2004 (Created)
1-JUN-2023 (Last updated, Version 36)
Name RNApol_bact_RpoC1
Scope
Bacteria; Cyanobacteriota
Plastid
Templates P22704 (RPOC1_NOSS1); P11705 (RPOC1_SPIOL): [Recover all]
Triggered by

Propagated annotation [?]


Identifier, protein and gene names [?]

Identifier
RPOC1
case not <OG:Chloroplast>
Protein name
RecName: Full=DNA-directed RNA polymerase subunit gamma;
Short=RNAP subunit gamma;
EC 2.7.7.6;
AltName: Full=RNA polymerase subunit gamma;
AltName: Full=Transcriptase subunit gamma;
else case <OG:Chloroplast>
Protein name
RecName: Full=DNA-directed RNA polymerase subunit beta';
EC 2.7.7.6;
AltName: Full=PEP;
AltName: Full=Plastid-encoded RNA polymerase subunit beta';
Short=RNA polymerase subunit beta';
end case
Gene name
rpoC1

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>
Cofactor Zn(2+)
Note: Binds 1 Zn(2+) ion per subunit.
end case
case <OC:Cyanobacteriota>
Subunit In cyanobacteria the RNAP catalytic core is composed of 2 alpha, 1 beta, 1 beta', 1 gamma and 1 omega subunit. When a sigma factor is associated with the core the holoenzyme is formed, which can initiate transcription.
else case <OG:Chloroplast>
Subunit In plastids the minimal PEP RNA polymerase catalytic core is composed of four subunits: alpha, beta, beta', and beta''. When a (nuclear-encoded) sigma factor is associated with the core the holoenzyme is formed, which can initiate transcription.
Subcellular location Plastid, chloroplast.
end case
Similarity Belongs to the RNA polymerase beta' chain family. RpoC1 subfamily.

Keywords [?]

case <FTGroup:1> or <FTGroup:2>
Metal-binding
end case
case <FTGroup:2>
Magnesium
end case
Transcription
Transferase
Nucleotidyltransferase
DNA-directed RNA polymerase
case <FTGroup:1>
Zinc
end case

Gene Ontology [?]

GO:0003677; Molecular function: DNA binding.
GO:0003899; Molecular function: DNA-directed 5'-3' RNA polymerase activity.
GO:0006351; Biological process: DNA-templated transcription.
case <FTGroup:2>
GO:0000287; Molecular function: magnesium ion binding.
end case
case <FTGroup:1>
GO:0008270; Molecular function: zinc ion binding.
end case
case <OG:Chloroplast>
GO:0009507; Cellular component: chloroplast.
end case

Cross-references [?]

Pfam PF04997; RNA_pol_Rpb1_1; 1;
PF00623; RNA_pol_Rpb1_2; 1-2;
PF04983; RNA_pol_Rpb1_3; 0-1;
NCBIfam TIGR02387; rpoC1_cyan; 1;

Features [?]

From: RPOC1_NOSS1 (P22704)
Key     From     To       Description   Tag   Condition   FTGroup
BINDING     71     71       /ligand="Zn(2+)" /ligand_id="ChEBI:CHEBI:29105     C   1
BINDING     73     73       /ligand="Zn(2+)" /ligand_id="ChEBI:CHEBI:29105     C   1
BINDING     86     86       /ligand="Zn(2+)" /ligand_id="ChEBI:CHEBI:29105     C   1
BINDING     89     89       /ligand="Zn(2+)" /ligand_id="ChEBI:CHEBI:29105     C   1
BINDING     467     467       /ligand="Mg(2+)" /ligand_id="ChEBI:CHEBI:18420     D   2
BINDING     469     469       /ligand="Mg(2+)" /ligand_id="ChEBI:CHEBI:18420     D   2
BINDING     471     471       /ligand="Mg(2+)" /ligand_id="ChEBI:CHEBI:18420     D   2

Additional information [?]

Size range 575-760 amino acids
Related rules MF_01322 (RPOC supersedes the current rule)
Fusion Nter: None; Cter: MF_01324 (rpoC2)
Comments In cyanobacteria and plastids, there are two ORFs (this one, rpoC1, MF_01323 and rpoC2, MF_01324) that together are equivalent to the beta' subunit found in all other bacteria (rpoC, MF_01322). However,in the red algae CYAM1 the rpoC1 and rpoC2 genes are fused into one ORF. This seems to be the result of evolution acting to reduce protein size rather than horizontal transfer from a bacteria. Some algal proteins with inserts and C.reinhardtii (where this protein is split in 2) are considered to be atypical.


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