RPOA_LEPCP
ID RPOA_LEPCP Reviewed; 328 AA.
AC B1Y7M9;
DT 24-MAR-2009, integrated into UniProtKB/Swiss-Prot.
DT 20-MAY-2008, sequence version 1.
DT 03-AUG-2022, entry version 78.
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=Lcho_3923;
OS Leptothrix cholodnii (strain ATCC 51168 / LMG 8142 / SP-6) (Leptothrix
OS discophora (strain SP-6)).
OC Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales; Leptothrix.
OX NCBI_TaxID=395495;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 51168 / LMG 8142 / SP-6;
RG US DOE Joint Genome Institute;
RA Copeland A., Lucas S., Lapidus A., Glavina del Rio T., Dalin E., Tice H.,
RA Bruce D., Goodwin L., Pitluck S., Chertkov O., Brettin T., Detter J.C.,
RA Han C., Kuske C.R., Schmutz J., Larimer F., Land M., Hauser L.,
RA Kyrpides N., Lykidis A., Emerson D., Richardson P.;
RT "Complete sequence of Leptothrix cholodnii SP-6.";
RL Submitted (MAR-2008) to the EMBL/GenBank/DDBJ databases.
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 ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; CP001013; ACB36177.1; -; Genomic_DNA.
DR RefSeq; WP_012348923.1; NC_010524.1.
DR AlphaFoldDB; B1Y7M9; -.
DR SMR; B1Y7M9; -.
DR STRING; 395495.Lcho_3923; -.
DR EnsemblBacteria; ACB36177; ACB36177; Lcho_3923.
DR KEGG; lch:Lcho_3923; -.
DR eggNOG; COG0202; Bacteria.
DR HOGENOM; CLU_053084_0_0_4; -.
DR OMA; LMKFRNF; -.
DR OrthoDB; 662686at2; -.
DR Proteomes; UP000001693; 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..328
FT /note="DNA-directed RNA polymerase subunit alpha"
FT /id="PRO_1000091955"
FT REGION 1..231
FT /note="Alpha N-terminal domain (alpha-NTD)"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00059"
FT REGION 248..328
FT /note="Alpha C-terminal domain (alpha-CTD)"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00059"
SQ SEQUENCE 328 AA; 36309 MW; 2B6F5EBCC9183C66 CRC64;
MQTNLLKPKA INVDPLGGHR AKVTLEPFER GFGHTLGNAL RRVLLSSMVG YAPTEVTIAG
VLHEYSTVDG VQEDVVHIML NLKGVVFRLH NRDEVTLVLR KEGEGPVKAS DIQTPHDVEI
INPDHVIAHL AQGGKLDMQI KVEKGRGYVP GSMRRYADEP TKSIGRIVLD ASFSPLKRVS
YTVESARVEQ RTDLDKLVME IETNGAISPE EAIRASAKIL VEQLAVFAQL EGSDLAIFEA
PAPRAQHFDP ILLRPVDELE LTVRSANCLK AENIYYIGDL IQRTETELLK TPNLGRKSLN
EIKEVLASRG LTLGARLENW PPQGLDKR