RPOA_CHLT2
ID RPOA_CHLT2 Reviewed; 377 AA.
AC B0B881; O84515; Q46449;
DT 24-MAR-2009, integrated into UniProtKB/Swiss-Prot.
DT 26-FEB-2008, sequence version 1.
DT 03-AUG-2022, entry version 77.
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=CTL0769;
OS Chlamydia trachomatis serovar L2 (strain 434/Bu / ATCC VR-902B).
OC Bacteria; Chlamydiae; Chlamydiales; Chlamydiaceae;
OC Chlamydia/Chlamydophila group; Chlamydia.
OX NCBI_TaxID=471472;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=7730299; DOI=10.1128/jb.177.9.2594-2601.1995;
RA Gu L.J., Wenman W.M., Remacha M., Meuser R.U., Coffin J.M., Kaul R.;
RT "Chlamydia trachomatis RNA polymerase alpha subunit: sequence and
RT structural analysis.";
RL J. Bacteriol. 177:2594-2601(1995).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=434/Bu / ATCC VR-902B;
RX PubMed=18032721; DOI=10.1101/gr.7020108;
RA Thomson N.R., Holden M.T.G., Carder C., Lennard N., Lockey S.J., Marsh P.,
RA Skipp P., O'Connor C.D., Goodhead I., Norbertzcak H., Harris B., Ormond D.,
RA Rance R., Quail M.A., Parkhill J., Stephens R.S., Clarke I.N.;
RT "Chlamydia trachomatis: genome sequence analysis of lymphogranuloma
RT venereum isolates.";
RL Genome Res. 18:161-171(2008).
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; L33834; AAA74989.1; -; Genomic_DNA.
DR EMBL; AM884176; CAP04207.1; -; Genomic_DNA.
DR PIR; A71505; A71505.
DR RefSeq; WP_009873864.1; NC_010287.1.
DR RefSeq; YP_001654840.1; NC_010287.1.
DR AlphaFoldDB; B0B881; -.
DR SMR; B0B881; -.
DR EnsemblBacteria; CAP04207; CAP04207; CTL0769.
DR KEGG; ctb:CTL0769; -.
DR PATRIC; fig|471472.4.peg.825; -.
DR HOGENOM; CLU_053084_0_1_0; -.
DR OMA; LMKFRNF; -.
DR Proteomes; UP000000795; 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:transcription, DNA-templated; IEA:UniProtKB-UniRule.
DR Gene3D; 2.170.120.12; -; 1.
DR Gene3D; 3.30.1360.10; -; 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 PANTHER; PTHR32108; PTHR32108; 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; SSF55257; SSF55257; 1.
DR SUPFAM; SSF56553; SSF56553; 1.
DR TIGRFAMs; TIGR02027; rpoA; 1.
PE 3: Inferred from homology;
KW DNA-directed RNA polymerase; Nucleotidyltransferase; Transcription;
KW Transferase.
FT CHAIN 1..377
FT /note="DNA-directed RNA polymerase subunit alpha"
FT /id="PRO_1000091935"
FT REGION 1..259
FT /note="Alpha N-terminal domain (alpha-NTD)"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00059"
FT REGION 279..377
FT /note="Alpha C-terminal domain (alpha-CTD)"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00059"
FT CONFLICT 30
FT /note="G -> S (in Ref. 1; AAA74989)"
FT /evidence="ECO:0000305"
FT CONFLICT 92..93
FT /note="IV -> ML (in Ref. 1; AAA74989)"
FT /evidence="ECO:0000305"
FT CONFLICT 295
FT /note="R -> RLIR (in Ref. 1; AAA74989)"
FT /evidence="ECO:0000305"
FT CONFLICT 377
FT /note="G -> A (in Ref. 1; AAA74989)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 377 AA; 41810 MW; 09BF6CBBEC31234A CRC64;
MSDSSHNLLY NKFELPESVK MSPVEGAVGG IDKVARFVAD PLEKGMGHTL GSALRRALLI
GLEAPAIVSF SMTGVLHEYM AVEGIIEDVT NIVLNLKGSL LKKYPLQDCE GGRCSQKLRA
TISVDASDLA AAGGQKEVTL GDLLQEGTFE AVNPEHVIFT VTRPMQLEVM LRVAFGRGYS
PSERIVLEER GMNEIVLDAA FSPVVLVNYF VEDTRVGQDT DFDRLVLQVE TDGRVAPKEA
VAFATQILSK HFSVFEKMDE KRIVFEEAIS VEKENKDDIL HKLVLGINEI ELSVRSTNCL
SNANIETIGE LVIMPEPRLL QFRNFGKKSL CEIKNKLKEM KLELGMDLSQ FGVGLDNVKE
KMKWYAEKIR SSKNTKG
