RPOA_CARRP
ID RPOA_CARRP Reviewed; 322 AA.
AC Q05FK5;
DT 24-JUL-2007, integrated into UniProtKB/Swiss-Prot.
DT 14-NOV-2006, sequence version 1.
DT 03-AUG-2022, entry version 81.
DE RecName: Full=DNA-directed RNA polymerase subunit alpha;
DE Short=RNAP subunit alpha;
DE EC=2.7.7.6;
DE AltName: Full=RNA polymerase subunit alpha;
DE AltName: Full=Transcriptase subunit alpha;
GN Name=rpoA; OrderedLocusNames=CRP_135;
OS Carsonella ruddii (strain PV).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Oceanospirillales;
OC Halomonadaceae; Zymobacter group; Candidatus Carsonella.
OX NCBI_TaxID=387662;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PV;
RX PubMed=17038615; DOI=10.1126/science.1134196;
RA Nakabachi A., Yamashita A., Toh H., Ishikawa H., Dunbar H.E., Moran N.A.,
RA Hattori M.;
RT "The 160-kilobase genome of the bacterial endosymbiont Carsonella.";
RL Science 314:267-267(2006).
CC -!- FUNCTION: DNA-dependent RNA polymerase catalyzes the transcription of
CC DNA into RNA using the four ribonucleoside triphosphates as substrates.
CC {ECO:0000250}.
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;
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 (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:0000250}.
CC -!- SIMILARITY: Belongs to the RNA polymerase alpha chain family.
CC {ECO:0000305}.
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DR EMBL; AP009180; BAF35166.1; -; Genomic_DNA.
DR AlphaFoldDB; Q05FK5; -.
DR SMR; Q05FK5; -.
DR STRING; 387662.CRP_135; -.
DR EnsemblBacteria; BAF35166; BAF35166; CRP_135.
DR KEGG; crp:CRP_135; -.
DR HOGENOM; CLU_053084_0_0_6; -.
DR OMA; LMKFRNF; -.
DR Proteomes; UP000000777; Chromosome.
DR GO; GO:0000428; C:DNA-directed RNA polymerase complex; IEA:UniProtKB-KW.
DR GO; GO:0003677; F:DNA binding; IEA:InterPro.
DR GO; GO:0003899; F:DNA-directed 5'-3' RNA polymerase activity; IEA:UniProtKB-EC.
DR GO; GO:0046983; F:protein dimerization activity; IEA:InterPro.
DR GO; GO:0006351; P:transcription, DNA-templated; IEA:InterPro.
DR Gene3D; 2.170.120.12; -; 1.
DR Gene3D; 3.30.1360.10; -; 1.
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; PF03118; RNA_pol_A_CTD; 1.
DR Pfam; PF01193; RNA_pol_L; 1.
DR SUPFAM; SSF55257; SSF55257; 1.
DR SUPFAM; SSF56553; SSF56553; 1.
PE 3: Inferred from homology;
KW DNA-directed RNA polymerase; Nucleotidyltransferase; Reference proteome;
KW Transcription; Transferase.
FT CHAIN 1..322
FT /note="DNA-directed RNA polymerase subunit alpha"
FT /id="PRO_0000296793"
FT REGION 1..229
FT /note="Alpha N-terminal domain (alpha-NTD)"
FT /evidence="ECO:0000250"
FT REGION 244..322
FT /note="Alpha C-terminal domain (alpha-CTD)"
FT /evidence="ECO:0000250"
SQ SEQUENCE 322 AA; 37759 MW; 56D8E2BB78D35098 CRC64;
MNFVNNLFTL KKISIKNISF FRSIIRIETF NNSFCDSLGN FIKRVIFLTT NSYKIIYLKI
YKIKSEFYDL PGIIENTQTI LKNLDNIIIK INNDNVANLI IKKKGPCIIT AKDIFSDKNI
TIFNPNKIIA NVSNNIVFYC IMKCVNSLFK NYTDEFFQFK IFKENIIFLN NFKSPIISLN
YYINKKIFNK KLKKLFFDIE TNGSIKPVDC FKNCIFYIKK YFDLIFSFIG FKKYKKINVE
KKNNLNLKIN SVYLNSINNL KLSIRSLNCL KNNNIFLIGD LIKISKNNLI NIPNLGKKSY
NEILNSLKNF GLNLNSKIEY DL