ID   RPOA_MYCGA              Reviewed;         325 AA.
AC   Q9RDV6;
DT   11-JAN-2001, integrated into UniProtKB/Swiss-Prot.
DT   11-JAN-2001, sequence version 2.
DT   03-AUG-2022, entry version 134.
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=MYCGA6280;
GN   ORFNames=MGA_0443;
OS   Mycoplasma gallisepticum (strain R(low / passage 15 / clone 2))
OS   (Mycoplasmoides gallisepticum).
OC   Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mycoplasma.
OX   NCBI_TaxID=710127;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=A5969Var.B;
RX   PubMed=11959450; DOI=10.1111/j.1574-6968.2002.tb11095.x;
RA   Skamrov A.V., Feoktistova E.S., Gol'dman M.A., Bibilashvili R.S.;
RT   "Mycoplasma gallisepticum rpoA gene cluster.";
RL   FEMS Microbiol. Lett. 208:281-285(2002).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=R(low / passage 15 / clone 2);
RX   PubMed=12949158; DOI=10.1099/mic.0.26427-0;
RA   Papazisi L., Gorton T.S., Kutish G., Markham P.F., Browning G.F.,
RA   Nguyen D.K., Swartzell S., Madan A., Mahairas G., Geary S.J.;
RT   "The complete genome sequence of the avian pathogen Mycoplasma
RT   gallisepticum strain R(low).";
RL   Microbiology 149:2307-2316(2003).
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}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAP56978.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR   EMBL; L35043; AAF19039.2; -; Genomic_DNA.
DR   EMBL; AE015450; AAP56978.1; ALT_INIT; Genomic_DNA.
DR   RefSeq; WP_011883401.1; NC_004829.2.
DR   AlphaFoldDB; Q9RDV6; -.
DR   SMR; Q9RDV6; -.
DR   PRIDE; Q9RDV6; -.
DR   KEGG; mga:MGA_0443; -.
DR   HOGENOM; CLU_053084_0_1_14; -.
DR   OMA; LMKFRNF; -.
DR   Proteomes; UP000001418; 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; Reference proteome;
KW   Transcription; Transferase.
FT   CHAIN           1..325
FT                   /note="DNA-directed RNA polymerase subunit alpha"
FT                   /id="PRO_0000175335"
FT   REGION          1..239
FT                   /note="Alpha N-terminal domain (alpha-NTD)"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00059"
FT   REGION          255..325
FT                   /note="Alpha C-terminal domain (alpha-CTD)"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00059"
SQ   SEQUENCE   325 AA;  36495 MW;  17FA3CA15EAD8C31 CRC64;
     MQQFLRYNIN VIKEDNDKNY GKYIVKPLEK GFGITLGNAL RRVMLSHLPG SSVFALKIKG
     ISHEFGFIPG VKEDVTQIIL NIKNLVVWIS DNMITDETLS ETPIEKWPVM TIRANKAGII
     KAGDIECPLG FEVFNKDLEI CTLSEDAEVA IDIYATRGRG FKTAAENRSE IGSLSIIPID
     SNFNPIIKVG YHVEEETSDV ITDKLIIEVG TNGLIKSGDA IAIASKILSD HLKPLIDINK
     SLHDIQVLNE KNVEEKNKKL SIPIEQLDLT VRSYNCLKRH GIQTVEELVT RSKSEIENIR
     NLGKKSVREI NKKLSELYDL KLKNN