ID   RPOA_STRR6              Reviewed;         311 AA.
AC   P66709; Q97ST7;
DT   11-OCT-2004, integrated into UniProtKB/Swiss-Prot.
DT   11-OCT-2004, sequence version 1.
DT   03-AUG-2022, entry version 103.
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=spr0215;
OS   Streptococcus pneumoniae (strain ATCC BAA-255 / R6).
OC   Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae;
OC   Streptococcus.
OX   NCBI_TaxID=171101;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-255 / R6;
RX   PubMed=11544234; DOI=10.1128/jb.183.19.5709-5717.2001;
RA   Hoskins J., Alborn W.E. Jr., Arnold J., Blaszczak L.C., Burgett S.,
RA   DeHoff B.S., Estrem S.T., Fritz L., Fu D.-J., Fuller W., Geringer C.,
RA   Gilmour R., Glass J.S., Khoja H., Kraft A.R., Lagace R.E., LeBlanc D.J.,
RA   Lee L.N., Lefkowitz E.J., Lu J., Matsushima P., McAhren S.M., McHenney M.,
RA   McLeaster K., Mundy C.W., Nicas T.I., Norris F.H., O'Gara M., Peery R.B.,
RA   Robertson G.T., Rockey P., Sun P.-M., Winkler M.E., Yang Y.,
RA   Young-Bellido M., Zhao G., Zook C.A., Baltz R.H., Jaskunas S.R.,
RA   Rosteck P.R. Jr., Skatrud P.L., Glass J.I.;
RT   "Genome of the bacterium Streptococcus pneumoniae strain R6.";
RL   J. Bacteriol. 183:5709-5717(2001).
RN   [2]
RP   IDENTIFICATION BY MASS SPECTROMETRY.
RX   PubMed=15720398; DOI=10.1111/j.1742-4658.2005.04560.x;
RA   Novakova L., Saskova L., Pallova P., Janecek J., Novotna J., Ulrych A.,
RA   Echenique J., Trombe M.C., Branny P.;
RT   "Characterization of a eukaryotic type serine/threonine protein kinase and
RT   protein phosphatase of Streptococcus pneumoniae and identification of
RT   kinase substrates.";
RL   FEBS J. 272:1243-1254(2005).
RN   [3]
RP   LACK OF PHOSPHORYLATION, AND IDENTIFICATION BY MASS SPECTROMETRY.
RX   PubMed=20453092; DOI=10.1128/jb.01564-09;
RA   Novakova L., Bezouskova S., Pompach P., Spidlova P., Saskova L., Weiser J.,
RA   Branny P.;
RT   "Identification of multiple substrates of the StkP Ser/Thr protein kinase
RT   in Streptococcus pneumoniae.";
RL   J. Bacteriol. 192:3629-3638(2010).
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   -!- MISCELLANEOUS: Although RpoA was believed to be phosphorylated by StkP
CC       in vivo in a first study (PubMed:15720398), the same authors later
CC       showed that this protein is indeed not phosphorylated
CC       (PubMed:20453092). {ECO:0000305|PubMed:15720398,
CC       ECO:0000305|PubMed:20453092}.
CC   -!- SIMILARITY: Belongs to the RNA polymerase alpha chain family.
CC       {ECO:0000255|HAMAP-Rule:MF_00059}.
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DR   EMBL; AE007317; AAK99019.1; -; Genomic_DNA.
DR   PIR; G97898; G97898.
DR   RefSeq; NP_357809.1; NC_003098.1.
DR   RefSeq; WP_000568988.1; NC_003098.1.
DR   AlphaFoldDB; P66709; -.
DR   SMR; P66709; -.
DR   STRING; 171101.spr0215; -.
DR   EnsemblBacteria; AAK99019; AAK99019; spr0215.
DR   GeneID; 60232819; -.
DR   GeneID; 66805442; -.
DR   KEGG; spr:spr0215; -.
DR   PATRIC; fig|171101.6.peg.247; -.
DR   eggNOG; COG0202; Bacteria.
DR   HOGENOM; CLU_053084_0_1_9; -.
DR   OMA; LMKFRNF; -.
DR   Proteomes; UP000000586; 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   1: Evidence at protein level;
KW   DNA-directed RNA polymerase; Nucleotidyltransferase; Reference proteome;
KW   Transcription; Transferase.
FT   CHAIN           1..311
FT                   /note="DNA-directed RNA polymerase subunit alpha"
FT                   /id="PRO_0000175395"
FT   REGION          1..226
FT                   /note="Alpha N-terminal domain (alpha-NTD)"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00059"
FT   REGION          243..311
FT                   /note="Alpha C-terminal domain (alpha-CTD)"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00059"
SQ   SEQUENCE   311 AA;  34207 MW;  91F0C9744DD7B526 CRC64;
     MIEFEKPNIT KIDENKDYGK FVIEPLERGY GTTLGNSLRR VLLASLPGAA VTSINIDGVL
     HEFDTVPGVR EDVMQIILNI KGIAVKSYVE DEKIIELDVE GPAEVTAGDI LTDSDIEIVN
     PDHYLFTIGE GSSLKATMTV NSGRGYVPAD ENKKDNAPVG TLAVDSIYTP VTKVNYQVEP
     ARVGSNDGFD KLTLEILTNG TIIPEDALGL SARILTEHLD LFTNLTEIAK STEVMKEADT
     ESDDRILDRT IEELDLSVRS YNCLKRAGIN TVHDLTEKSE AEMMKVRNLG RKSLEEVKLK
     LIDLGLGLKD K