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RPOA_STRCO
ID   RPOA_STRCO              Reviewed;         340 AA.
AC   P60312; O86774; P72404;
DT   02-FEB-2004, integrated into UniProtKB/Swiss-Prot.
DT   02-FEB-2004, sequence version 1.
DT   03-AUG-2022, entry version 107.
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=SCO4729;
GN   ORFNames=SC6G4.07;
OS   Streptomyces coelicolor (strain ATCC BAA-471 / A3(2) / M145).
OC   Bacteria; Actinobacteria; Streptomycetales; Streptomycetaceae;
OC   Streptomyces; Streptomyces albidoflavus group.
OX   NCBI_TaxID=100226;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=ATCC BAA-471 / A3(2) / M145;
RX   PubMed=8948650; DOI=10.1093/nar/24.22.4565;
RA   Cho E.-J., Bae J.-B., Kang J.-G., Roe J.-H.;
RT   "Molecular analysis of RNA polymerase alpha subunit gene from Streptomyces
RT   coelicolor A3(2).";
RL   Nucleic Acids Res. 24:4565-4571(1996).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-471 / A3(2) / M145;
RX   PubMed=12000953; DOI=10.1038/417141a;
RA   Bentley S.D., Chater K.F., Cerdeno-Tarraga A.-M., Challis G.L.,
RA   Thomson N.R., James K.D., Harris D.E., Quail M.A., Kieser H., Harper D.,
RA   Bateman A., Brown S., Chandra G., Chen C.W., Collins M., Cronin A.,
RA   Fraser A., Goble A., Hidalgo J., Hornsby T., Howarth S., Huang C.-H.,
RA   Kieser T., Larke L., Murphy L.D., Oliver K., O'Neil S., Rabbinowitsch E.,
RA   Rajandream M.A., Rutherford K.M., Rutter S., Seeger K., Saunders D.,
RA   Sharp S., Squares R., Squares S., Taylor K., Warren T., Wietzorrek A.,
RA   Woodward J.R., Barrell B.G., Parkhill J., Hopwood D.A.;
RT   "Complete genome sequence of the model actinomycete Streptomyces coelicolor
RT   A3(2).";
RL   Nature 417:141-147(2002).
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; X92107; CAA63080.1; -; Genomic_DNA.
DR   EMBL; AL939121; CAA20385.1; -; Genomic_DNA.
DR   PIR; T35558; T35558.
DR   RefSeq; NP_628887.1; NC_003888.3.
DR   RefSeq; WP_003966937.1; NZ_VNID01000016.1.
DR   AlphaFoldDB; P60312; -.
DR   SMR; P60312; -.
DR   STRING; 100226.SCO4729; -.
DR   GeneID; 1100170; -.
DR   GeneID; 63982151; -.
DR   GeneID; 67399260; -.
DR   KEGG; sco:SCO4729; -.
DR   PATRIC; fig|100226.15.peg.4800; -.
DR   eggNOG; COG0202; Bacteria.
DR   HOGENOM; CLU_053084_0_1_11; -.
DR   InParanoid; P60312; -.
DR   OMA; LMKFRNF; -.
DR   PhylomeDB; P60312; -.
DR   PRO; PR:P60312; -.
DR   Proteomes; UP000001973; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
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; Reference proteome;
KW   Transcription; Transferase.
FT   CHAIN           1..340
FT                   /note="DNA-directed RNA polymerase subunit alpha"
FT                   /id="PRO_0000175389"
FT   REGION          1..226
FT                   /note="Alpha N-terminal domain (alpha-NTD)"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00059"
FT   REGION          243..340
FT                   /note="Alpha C-terminal domain (alpha-CTD)"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00059"
FT   CONFLICT        98
FT                   /note="R -> S (in Ref. 1; CAA63080)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        154
FT                   /note="Q -> E (in Ref. 1; CAA63080)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        206
FT                   /note="Missing (in Ref. 1; CAA63080)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   340 AA;  36696 MW;  DD288188FAF08807 CRC64;
     MLIAQRPSLT EEVVDEFRSR FVIEPLEPGF GYTLGNSLRR TLLSSIPGAA VTSIRIDGVL
     HEFTTVPGVK EDVTDLILNI KQLVVSSEHD EPVVMYLRKQ GPGLVTAADI APPAGVEVHN
     PDLVLATLNG KGKLEMELTV ERGRGYVSAV QNKQVGQEIG RIPVDSIYSP VLKVTYKVEA
     TRVEQRTDFD KLIVDVETKQ AMRPRDAMAS AGKTLVELFG LARELNIDAE GIDMGPSPTD
     AALAADLALP IEELELTVRS YNCLKREGIH SVGELVARSE ADLLDIRNFG AKSIDEVKAK
     LAGMGLALKD SPPGFDPTAA ADAFGADDDA DAGFVETEQY
 
 
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