RPOA_PSEAE
ID RPOA_PSEAE Reviewed; 333 AA.
AC O52760;
DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT 08-DEC-2000, sequence version 2.
DT 03-AUG-2022, entry version 137.
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=PA4238;
OS Pseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM
OS 14847 / LMG 12228 / 1C / PRS 101 / PAO1).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC Pseudomonadaceae; Pseudomonas.
OX NCBI_TaxID=208964;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=FRD1;
RX PubMed=10368148; DOI=10.1128/jb.181.12.3730-3742.1999;
RA Ma J.-F., Ochsner U.A., Klotz M.G., Nanayakkara V.K., Howell M.L.,
RA Johnson Z., Posey J.E., Vasil M.L., Monaco J.J., Hassett D.J.;
RT "Bacterioferritin A modulates catalase A (KatA) activity and resistance to
RT hydrogen peroxide in Pseudomonas aeruginosa.";
RL J. Bacteriol. 181:3730-3742(1999).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C /
RC PRS 101 / PAO1;
RX PubMed=10984043; DOI=10.1038/35023079;
RA Stover C.K., Pham X.-Q.T., Erwin A.L., Mizoguchi S.D., Warrener P.,
RA Hickey M.J., Brinkman F.S.L., Hufnagle W.O., Kowalik D.J., Lagrou M.,
RA Garber R.L., Goltry L., Tolentino E., Westbrock-Wadman S., Yuan Y.,
RA Brody L.L., Coulter S.N., Folger K.R., Kas A., Larbig K., Lim R.M.,
RA Smith K.A., Spencer D.H., Wong G.K.-S., Wu Z., Paulsen I.T., Reizer J.,
RA Saier M.H. Jr., Hancock R.E.W., Lory S., Olson M.V.;
RT "Complete genome sequence of Pseudomonas aeruginosa PAO1, an opportunistic
RT pathogen.";
RL Nature 406:959-964(2000).
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; AF047025; AAC03116.1; -; Genomic_DNA.
DR EMBL; AE004091; AAG07626.1; -; Genomic_DNA.
DR PIR; D83113; D83113.
DR RefSeq; NP_252928.1; NC_002516.2.
DR RefSeq; WP_003093675.1; NZ_QZGE01000028.1.
DR AlphaFoldDB; O52760; -.
DR SMR; O52760; -.
DR STRING; 287.DR97_3673; -.
DR PaxDb; O52760; -.
DR PRIDE; O52760; -.
DR DNASU; 881813; -.
DR EnsemblBacteria; AAG07626; AAG07626; PA4238.
DR GeneID; 881813; -.
DR KEGG; pae:PA4238; -.
DR PATRIC; fig|208964.12.peg.4439; -.
DR PseudoCAP; PA4238; -.
DR HOGENOM; CLU_053084_0_0_6; -.
DR InParanoid; O52760; -.
DR OMA; LMKFRNF; -.
DR PhylomeDB; O52760; -.
DR BioCyc; PAER208964:G1FZ6-4311-MON; -.
DR Proteomes; UP000002438; 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..333
FT /note="DNA-directed RNA polymerase subunit alpha"
FT /id="PRO_0000175359"
FT REGION 1..234
FT /note="Alpha N-terminal domain (alpha-NTD)"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00059"
FT REGION 248..333
FT /note="Alpha C-terminal domain (alpha-CTD)"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00059"
FT CONFLICT 326..333
FT /note="KKDDKATA -> TERRQGHCLIVVTTERKVWKGIEPCAIVKVVVT (in
FT Ref. 1; AAC03116)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 333 AA; 36650 MW; 50706D2926207CA9 CRC64;
MQSSVNEFLT PRHIDVQVVS QTRAKITLEP LERGFGHTLG NALRRILLSS MPGCAVVEAE
IDGVLHEYSA IEGVQEDVIE ILLNLKGLAI KLHGRDEVTL TLAKKGSGVV TAADIQLDHD
VEIINGDHVI ANLADNGALN MKLKVARGRG YEPADARQSD EDESRSIGRL QLDASFSPVR
RVSYVVENAR VEQRTNLDKL VLDLETNGTL DPEEAIRRAA TILQQQLAAF VDLKGDSEPV
VEEQEDEIDP ILLRPVDDLE LTVRSANCLK AENIYYIGDL IQRTEVELLK TPNLGKKSLT
EIKDVLASRG LSLGMRLDNW PPASLKKDDK ATA
