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Database: UniProt
Entry: RPOA_CLOD6
LinkDB: RPOA_CLOD6
Original site: RPOA_CLOD6 
ID   RPOA_CLOD6              Reviewed;         315 AA.
AC   Q18CI5;
DT   12-DEC-2006, integrated into UniProtKB/Swiss-Prot.
DT   25-JUL-2006, sequence version 1.
DT   27-MAR-2024, entry version 109.
DE   RecName: Full=DNA-directed RNA polymerase subunit alpha {ECO:0000255|HAMAP-Rule:MF_00059};
DE            Short=RNAP subunit alpha {ECO:0000255|HAMAP-Rule:MF_00059};
DE            EC=2.7.7.6 {ECO:0000255|HAMAP-Rule:MF_00059};
DE   AltName: Full=RNA polymerase subunit alpha {ECO:0000255|HAMAP-Rule:MF_00059};
DE   AltName: Full=Transcriptase subunit alpha {ECO:0000255|HAMAP-Rule:MF_00059};
GN   Name=rpoA {ECO:0000255|HAMAP-Rule:MF_00059}; OrderedLocusNames=CD630_00980;
OS   Clostridioides difficile (strain 630) (Peptoclostridium difficile).
OC   Bacteria; Bacillota; Clostridia; Eubacteriales; Peptostreptococcaceae;
OC   Clostridioides.
OX   NCBI_TaxID=272563;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=630;
RX   PubMed=16804543; DOI=10.1038/ng1830;
RA   Sebaihia M., Wren B.W., Mullany P., Fairweather N.F., Minton N.,
RA   Stabler R., Thomson N.R., Roberts A.P., Cerdeno-Tarraga A.M., Wang H.,
RA   Holden M.T.G., Wright A., Churcher C., Quail M.A., Baker S., Bason N.,
RA   Brooks K., Chillingworth T., Cronin A., Davis P., Dowd L., Fraser A.,
RA   Feltwell T., Hance Z., Holroyd S., Jagels K., Moule S., Mungall K.,
RA   Price C., Rabbinowitsch E., Sharp S., Simmonds M., Stevens K., Unwin L.,
RA   Whithead S., Dupuy B., Dougan G., Barrell B., Parkhill J.;
RT   "The multidrug-resistant human pathogen Clostridium difficile has a highly
RT   mobile, mosaic genome.";
RL   Nat. Genet. 38:779-786(2006).
CC   -!- FUNCTION: DNA-dependent RNA polymerase catalyzes the transcription of
CC       DNA into RNA using the four ribonucleoside triphosphates as substrates.
CC       {ECO:0000255|HAMAP-Rule:MF_00059}.
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; Evidence={ECO:0000255|HAMAP-Rule:MF_00059};
CC   -!- SUBUNIT: Homodimer. The RNAP catalytic core consists of 2 alpha, 1
CC       beta, 1 beta' and 1 omega subunit. When a sigma factor is associated
CC       with the core the holoenzyme is formed, which can initiate
CC       transcription. {ECO:0000255|HAMAP-Rule:MF_00059}.
CC   -!- DOMAIN: The N-terminal domain is essential for RNAP assembly and basal
CC       transcription, whereas the C-terminal domain is involved in interaction
CC       with transcriptional regulators and with upstream promoter elements.
CC       {ECO:0000255|HAMAP-Rule:MF_00059}.
CC   -!- SIMILARITY: Belongs to the RNA polymerase alpha chain family.
CC       {ECO:0000255|HAMAP-Rule:MF_00059}.
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DR   EMBL; AM180355; CAJ66917.1; -; Genomic_DNA.
DR   RefSeq; WP_003427733.1; NZ_JAUPES010000043.1.
DR   RefSeq; YP_001086566.1; NC_009089.1.
DR   PDB; 7L7B; EM; 3.26 A; A/B=1-315.
DR   PDBsum; 7L7B; -.
DR   AlphaFoldDB; Q18CI5; -.
DR   EMDB; EMD-23210; -.
DR   SMR; Q18CI5; -.
DR   STRING; 272563.CD630_00980; -.
DR   ChEMBL; CHEMBL2363852; -.
DR   DrugCentral; Q18CI5; -.
DR   EnsemblBacteria; CAJ66917; CAJ66917; CD630_00980.
DR   GeneID; 66352600; -.
DR   KEGG; cdf:CD630_00980; -.
DR   KEGG; pdc:CDIF630_00168; -.
DR   PATRIC; fig|272563.120.peg.108; -.
DR   eggNOG; COG0202; Bacteria.
DR   OrthoDB; 9805706at2; -.
DR   PhylomeDB; Q18CI5; -.
DR   BioCyc; PDIF272563:G12WB-156-MONOMER; -.
DR   PRO; PR:Q18CI5; -.
DR   Proteomes; UP000001978; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProt.
DR   GO; GO:0000428; C:DNA-directed RNA polymerase complex; IEA:UniProtKB-KW.
DR   GO; GO:0003677; F:DNA binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0003899; F:DNA-directed 5'-3' RNA polymerase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0046983; F:protein dimerization activity; IEA:InterPro.
DR   GO; GO:0006351; P:DNA-templated transcription; IEA:UniProtKB-UniRule.
DR   CDD; cd06928; RNAP_alpha_NTD; 1.
DR   Gene3D; 1.10.150.20; 5' to 3' exonuclease, C-terminal subdomain; 1.
DR   Gene3D; 2.170.120.12; DNA-directed RNA polymerase, insert domain; 1.
DR   Gene3D; 3.30.1360.10; RNA polymerase, RBP11-like subunit; 1.
DR   HAMAP; MF_00059; RNApol_bact_RpoA; 1.
DR   InterPro; IPR011262; DNA-dir_RNA_pol_insert.
DR   InterPro; IPR011263; DNA-dir_RNA_pol_RpoA/D/Rpb3.
DR   InterPro; IPR011773; DNA-dir_RpoA.
DR   InterPro; IPR036603; RBP11-like.
DR   InterPro; IPR011260; RNAP_asu_C.
DR   InterPro; IPR036643; RNApol_insert_sf.
DR   NCBIfam; TIGR02027; rpoA; 1.
DR   Pfam; PF01000; RNA_pol_A_bac; 1.
DR   Pfam; PF03118; RNA_pol_A_CTD; 1.
DR   Pfam; PF01193; RNA_pol_L; 1.
DR   SMART; SM00662; RPOLD; 1.
DR   SUPFAM; SSF47789; C-terminal domain of RNA polymerase alpha subunit; 1.
DR   SUPFAM; SSF56553; Insert subdomain of RNA polymerase alpha subunit; 1.
DR   SUPFAM; SSF55257; RBP11-like subunits of RNA polymerase; 1.
PE   1: Evidence at protein level;
KW   3D-structure; DNA-directed RNA polymerase; Nucleotidyltransferase;
KW   Reference proteome; Transcription; Transferase.
FT   CHAIN           1..315
FT                   /note="DNA-directed RNA polymerase subunit alpha"
FT                   /id="PRO_0000264492"
FT   REGION          1..228
FT                   /note="Alpha N-terminal domain (alpha-NTD)"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00059"
FT   REGION          245..315
FT                   /note="Alpha C-terminal domain (alpha-CTD)"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00059"
FT   STRAND          8..11
FT                   /evidence="ECO:0007829|PDB:7L7B"
FT   STRAND          22..29
FT                   /evidence="ECO:0007829|PDB:7L7B"
FT   HELIX           32..46
FT                   /evidence="ECO:0007829|PDB:7L7B"
FT   STRAND          49..58
FT                   /evidence="ECO:0007829|PDB:7L7B"
FT   STRAND          63..66
FT                   /evidence="ECO:0007829|PDB:7L7B"
FT   STRAND          71..73
FT                   /evidence="ECO:0007829|PDB:7L7B"
FT   HELIX           76..82
FT                   /evidence="ECO:0007829|PDB:7L7B"
FT   STRAND          90..93
FT                   /evidence="ECO:0007829|PDB:7L7B"
FT   STRAND          95..104
FT                   /evidence="ECO:0007829|PDB:7L7B"
FT   HELIX           109..111
FT                   /evidence="ECO:0007829|PDB:7L7B"
FT   STRAND          135..147
FT                   /evidence="ECO:0007829|PDB:7L7B"
FT   HELIX           151..154
FT                   /evidence="ECO:0007829|PDB:7L7B"
FT   STRAND          173..176
FT                   /evidence="ECO:0007829|PDB:7L7B"
FT   STRAND          186..188
FT                   /evidence="ECO:0007829|PDB:7L7B"
FT   STRAND          191..200
FT                   /evidence="ECO:0007829|PDB:7L7B"
FT   STRAND          202..204
FT                   /evidence="ECO:0007829|PDB:7L7B"
FT   HELIX           206..220
FT                   /evidence="ECO:0007829|PDB:7L7B"
SQ   SEQUENCE   315 AA;  34920 MW;  E75526C3C02D9B16 CRC64;
     MIEIEKPKVD IVELSEDYRY GKFVIEPLER GYGITIGNAL RRILLSSLPG VAVNAIKIDG
     VLHEFSTIPG VKEDVTEIIL TLKELSATID GEGSRTLKIE AQGPCSITGA DIICPPDVEI
     LSKDLAIATL DDNAKLNMEI FVDKGRGYVS AEENKTENVP IGVLPVDSIY TPVEKVSYHV
     ENTRVGQKTD YDKLVLEVWT NGSINPQEGI SLAAKVLVEH LNLFIDLTEH VSSVEIMVEK
     EEDQKEKVLE MTIEELDLSV RSYNCLKRAG INTVEELANK SEDDMMKVRN LGKKSLEEVI
     QKLEELGLGL KPSEE
//
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