AC   MF_01322;
DC   Protein; auto
TR   HAMAP; MF_01322; -; 1; level=0
XX
Names: RNApol_bact_RpoC
XX
ID   RPOC
DE   RecName: Full=DNA-directed RNA polymerase subunit beta';
DE            Short=RNAP subunit beta';
DE            EC=2.7.7.6;
DE   AltName: Full=RNA polymerase subunit beta';
DE   AltName: Full=Transcriptase subunit beta';
GN   Name=rpoC;
XX
CC   -!- FUNCTION: DNA-dependent RNA polymerase catalyzes the transcription of
CC       DNA into RNA using the four ribonucleoside triphosphates as substrates.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=a ribonucleoside 5'-triphosphate + RNA(n) = diphosphate +
CC         RNA(n+1); Xref=Rhea:RHEA:21248, Rhea:RHEA-COMP:14527, Rhea:RHEA-
CC         COMP:17342, ChEBI:CHEBI:33019, ChEBI:CHEBI:61557, ChEBI:CHEBI:140395;
CC         EC=2.7.7.6;
case <FTGroup:2>
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC       Note=Binds 1 Mg(2+) ion per subunit.;
end case
case <FTGroup:1> and <FTGroup:3>
CC   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC       Note=Binds 2 Zn(2+) ions per subunit.;
end case
CC   -!- SUBUNIT: The RNAP catalytic core consists of 2 alpha, 1 beta, 1 beta'
CC       and 1 omega subunit. When a sigma factor is associated with the core
CC       the holoenzyme is formed, which can initiate transcription.
CC   -!- SIMILARITY: Belongs to the RNA polymerase beta' chain family.
XX
DR   Pfam; PF04997; RNA_pol_Rpb1_1; 1; trigger=no
DR   Pfam; PF00623; RNA_pol_Rpb1_2; 1-2; trigger=no
DR   Pfam; PF04983; RNA_pol_Rpb1_3; 1; trigger=no
DR   Pfam; PF05000; RNA_pol_Rpb1_4; 1; trigger=no
DR   Pfam; PF04998; RNA_pol_Rpb1_5; 1-2; trigger=no
DR   NCBIfam; TIGR02386; rpoC_TIGR; 1; trigger=no
XX
case (<OC:Escherichia> or <OC:Shigella>) and <FT:1>
KW   Acetylation
end case
case <FTGroup:1> or <FTGroup:2> or <FTGroup:3>
KW   Metal-binding
end case
case <FTGroup:2>
KW   Magnesium
end case
KW   Transcription
KW   Transferase
KW   Nucleotidyltransferase
KW   DNA-directed RNA polymerase
case <FTGroup:1> or <FTGroup:3>
KW   Zinc
end case
XX
GO   GO:0003677; F:DNA binding
GO   GO:0003899; F:DNA-directed 5'-3' RNA polymerase activity
case <FTGroup:2>
GO   GO:0000287; F:magnesium ion binding
end case
GO   GO:0006351; P:DNA-templated transcription
case <FTGroup:1> or <FTGroup:3>
GO   GO:0008270; F:zinc ion binding
end case
XX
FT   From: RPOC_ECOLI (P0A8T7)
FT   BINDING         70
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="1"
FT   Group: 1; Condition: C
FT   BINDING         72
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="1"
FT   Group: 1; Condition: C
FT   BINDING         85
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="1"
FT   Group: 1; Condition: C
FT   BINDING         88
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="1"
FT   Group: 1; Condition: C
FT   BINDING         460
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT   Group: 2; Condition: D
FT   BINDING         462
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT   Group: 2; Condition: D
FT   BINDING         464
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT   Group: 2; Condition: D
FT   BINDING         814
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT   Group: 3; Condition: C
FT   BINDING         888
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT   Group: 3; Condition: C
FT   BINDING         895
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT   Group: 3; Condition: C
FT   BINDING         898
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT   Group: 3; Condition: C
case <OC:Escherichia> or <OC:Shigella>
FT   MOD_RES         983
FT                   /note="N6-acetyllysine"
FT   Condition: K
end case
XX
Size: 1135-1690;
Related: MF_01323; MF_01324;
Template: P0A8T7; Q9KWU6;
Scope:
 Bacteria
Fusion:
 Nter: MF_01321 (rpoB); <Unknown>
 Cter: None
Duplicate: in CERS1
Plasmid: 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.
XX
# Revision 1.30 2023/06/01
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