ID   RPOA_MYCSP              Reviewed;         353 AA.
AC   P38018; Q46452; Q8VVM1;
DT   01-OCT-1994, integrated into UniProtKB/Swiss-Prot.
DT   11-JAN-2001, sequence version 2.
DT   03-AUG-2022, entry version 95.
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};
OS   Mycoplasma sp.
OC   Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mycoplasma;
OC   unclassified Mycoplasma.
OX   NCBI_TaxID=2108;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=8226662; DOI=10.1128/jb.175.22.7150-7159.1993;
RA   Tan M., Klein R., Grant R., Ganem D., Engel J.N.;
RT   "Cloning and characterization of the RNA polymerase alpha-subunit operon of
RT   Chlamydia trachomatis.";
RL   J. Bacteriol. 175:7150-7159(1993).
RN   [2]
RP   ERRATUM OF PUBMED:8226662, AND CORRECTION OF SPECIES OF ORIGIN.
RA   Tan M., Klein R., Grant R., Ganem D., Engel J.N.;
RL   J. Bacteriol. 177:2607-2607(1995).
CC   -!- FUNCTION: DNA-dependent RNA polymerase catalyzes the transcription of
CC       DNA into RNA using the four ribonucleoside triphosphates as substrates.
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}.
CC   -!- CAUTION: Was originally thought to originate from Chlamydia
CC       trachomatis. {ECO:0000305|PubMed:8226662}.
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DR   EMBL; L09636; AAA61685.2; -; Genomic_DNA.
DR   EMBL; L09636; AAA61684.1; -; Genomic_DNA.
DR   AlphaFoldDB; P38018; -.
DR   SMR; P38018; -.
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..353
FT                   /note="DNA-directed RNA polymerase subunit alpha"
FT                   /id="PRO_0000175344"
FT   REGION          1..245
FT                   /note="Alpha N-terminal domain (alpha-NTD)"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00059"
FT   REGION          261..353
FT                   /note="Alpha C-terminal domain (alpha-CTD)"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00059"
SQ   SEQUENCE   353 AA;  40097 MW;  F10F1C601C5E73DC CRC64;
     MEKIQKITYK ELVAEKVNDF NTTFVIEPLA RGYANTMGTV LRRTLLSSIT SVAPFAIKIN
     NVEHEFQTIS GLKEDAITLV RNIRNIRFVY NEEIFEKENL AKISFKTNKE GEIFASDIPE
     VSGLEIVNKD QYIANIAKGG SLEFDLFLRK GRGFIDFEEN KNVISQYGSR LESSIKNGQF
     LAMDSDFSPV KKCAISFEEL NSSSKLIEER LKIKIETDCT VSAKEAIEQA AKIIVAHFQI
     IGNINALETI ELFEENKEKK EREIKSTTPI TKLGLSVRSE NALRRAKYNT VEEVLGLSDE
     ELSNIKNLGK KSIQDIIEKR NEWKERIGYD DGQSDNFIIE SLDQLNNSEE GEE