ID   RPOA_SYNP6              Reviewed;         309 AA.
AC   O24710;
DT   30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT   01-JAN-1998, sequence version 1.
DT   03-AUG-2022, entry version 135.
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=syc1888_d;
OS   Synechococcus sp. (strain ATCC 27144 / PCC 6301 / SAUG 1402/1) (Anacystis
OS   nidulans).
OC   Bacteria; Cyanobacteria; Synechococcales; Synechococcaceae; Synechococcus.
OX   NCBI_TaxID=269084;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=9300823; DOI=10.1016/s0378-1119(97)00169-8;
RA   Sugita M., Sugishita H., Fujishiro T., Tsuboi M., Sugita C., Endo T.,
RA   Sugiura M.;
RT   "Organization of a large gene cluster encoding ribosomal proteins in the
RT   cyanobacterium Synechococcus sp. strain PCC 6301: comparison of gene
RT   clusters among cyanobacteria, eubacteria and chloroplast genomes.";
RL   Gene 195:73-79(1997).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 27144 / PCC 6301 / SAUG 1402/1;
RX   PubMed=17211581; DOI=10.1007/s11120-006-9122-4;
RA   Sugita C., Ogata K., Shikata M., Jikuya H., Takano J., Furumichi M.,
RA   Kanehisa M., Omata T., Sugiura M., Sugita M.;
RT   "Complete nucleotide sequence of the freshwater unicellular cyanobacterium
RT   Synechococcus elongatus PCC 6301 chromosome: gene content and
RT   organization.";
RL   Photosyn. Res. 93:55-67(2007).
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. In cyanobacteria the RNAP catalytic core is
CC       composed of 2 alpha, 1 beta, 1 beta', 1 gamma and 1 omega subunit. When
CC       a sigma factor is associated with the core the holoenzyme is formed,
CC       which can initiate transcription (By similarity). {ECO:0000250}.
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; AB000111; BAA22472.1; -; Genomic_DNA.
DR   EMBL; AP008231; BAD80078.1; -; Genomic_DNA.
DR   RefSeq; WP_011244198.1; NC_006576.1.
DR   AlphaFoldDB; O24710; -.
DR   SMR; O24710; -.
DR   STRING; 269084.syc1888_d; -.
DR   EnsemblBacteria; BAD80078; BAD80078; syc1888_d.
DR   KEGG; syc:syc1888_d; -.
DR   eggNOG; COG0202; Bacteria.
DR   OMA; LMKFRNF; -.
DR   Proteomes; UP000001175; 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..309
FT                   /note="DNA-directed RNA polymerase subunit alpha"
FT                   /id="PRO_0000175402"
FT   REGION          1..227
FT                   /note="Alpha N-terminal domain (alpha-NTD)"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00059"
FT   REGION          239..309
FT                   /note="Alpha C-terminal domain (alpha-CTD)"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00059"
SQ   SEQUENCE   309 AA;  33783 MW;  95F692DC01FF1F66 CRC64;
     MTFQVECVES RTEADQGQYG RFSIEPLARG QGTTVGNALR RVLLSNLEGT AVTAVRIGGV
     NHEFATIPGV REDVLDILLN VRELVVHAHS PQPQIGRLRV VGPATVTAAD VDFGPEVEVI
     NPNHYIASLS EGATLEMELK VEWGTGYRAI DRSHDETTAL DFLQLDAVFM PVRRVNYSVE
     DARVGESTAI DRLVLEVWTN GSLSPQEALS QAASCLVALF EPLKNVSVGS THTADPEPTP
     ESQTPIEDLQ LSVRAYNCLK RAQVNSVADL LSYTYEDLLE IKNFGQKSAE EVVEALERIG
     IKLQESKVS