RPOB_OSTTA
ID RPOB_OSTTA Reviewed; 1088 AA.
AC Q0P3M6;
DT 06-FEB-2007, integrated into UniProtKB/Swiss-Prot.
DT 19-SEP-2006, sequence version 1.
DT 03-AUG-2022, entry version 79.
DE RecName: Full=DNA-directed RNA polymerase subunit beta {ECO:0000255|HAMAP-Rule:MF_01321};
DE EC=2.7.7.6 {ECO:0000255|HAMAP-Rule:MF_01321};
DE AltName: Full=PEP {ECO:0000255|HAMAP-Rule:MF_01321};
DE AltName: Full=Plastid-encoded RNA polymerase subunit beta {ECO:0000255|HAMAP-Rule:MF_01321};
DE Short=RNA polymerase subunit beta {ECO:0000255|HAMAP-Rule:MF_01321};
GN Name=rpoB {ECO:0000255|HAMAP-Rule:MF_01321}; OrderedLocusNames=OtCpg00260;
OS Ostreococcus tauri.
OG Plastid; Chloroplast.
OC Eukaryota; Viridiplantae; Chlorophyta; Mamiellophyceae; Mamiellales;
OC Bathycoccaceae; Ostreococcus.
OX NCBI_TaxID=70448;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=OTTH0595;
RX PubMed=17251180; DOI=10.1093/molbev/msm012;
RA Robbens S., Derelle E., Ferraz C., Wuyts J., Moreau H., Van de Peer Y.;
RT "The complete chloroplast and mitochondrial DNA sequence of Ostreococcus
RT tauri: organelle genomes of the smallest eukaryote are examples of
RT compaction.";
RL Mol. Biol. Evol. 24:956-968(2007).
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_01321}.
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_01321};
CC -!- SUBUNIT: In plastids the minimal PEP RNA polymerase catalytic core is
CC composed of four subunits: alpha, beta, beta', and beta''. When a
CC (nuclear-encoded) sigma factor is associated with the core the
CC holoenzyme is formed, which can initiate transcription.
CC {ECO:0000255|HAMAP-Rule:MF_01321}.
CC -!- SUBCELLULAR LOCATION: Plastid, chloroplast.
CC -!- SIMILARITY: Belongs to the RNA polymerase beta chain family.
CC {ECO:0000255|HAMAP-Rule:MF_01321}.
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DR EMBL; CR954199; CAL36351.1; -; Genomic_DNA.
DR RefSeq; YP_717229.1; NC_008289.1.
DR AlphaFoldDB; Q0P3M6; -.
DR SMR; Q0P3M6; -.
DR STRING; 70448.Q0P3M6; -.
DR PRIDE; Q0P3M6; -.
DR GeneID; 4238798; -.
DR KEGG; ota:OstapCp26; -.
DR eggNOG; KOG0214; Eukaryota.
DR InParanoid; Q0P3M6; -.
DR OrthoDB; 7046at2759; -.
DR Proteomes; UP000009170; Chloroplast.
DR GO; GO:0009507; C:chloroplast; IEA:UniProtKB-SubCell.
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:0032549; F:ribonucleoside binding; IEA:InterPro.
DR GO; GO:0006351; P:transcription, DNA-templated; IEA:UniProtKB-UniRule.
DR CDD; cd00653; RNA_pol_B_RPB2; 1.
DR Gene3D; 2.30.150.10; -; 1.
DR Gene3D; 2.40.270.10; -; 2.
DR Gene3D; 2.40.50.150; -; 1.
DR Gene3D; 3.90.1110.10; -; 1.
DR HAMAP; MF_01321; RNApol_bact_RpoB; 1.
DR InterPro; IPR042107; DNA-dir_RNA_pol_bsu_ext_1_sf.
DR InterPro; IPR015712; DNA-dir_RNA_pol_su2.
DR InterPro; IPR007120; DNA-dir_RNAP_su2_dom.
DR InterPro; IPR037033; DNA-dir_RNAP_su2_hyb_sf.
DR InterPro; IPR010243; RNA_pol_bsu_bac.
DR InterPro; IPR007121; RNA_pol_bsu_CS.
DR InterPro; IPR007644; RNA_pol_bsu_protrusion.
DR InterPro; IPR007642; RNA_pol_Rpb2_2.
DR InterPro; IPR037034; RNA_pol_Rpb2_2_sf.
DR InterPro; IPR007645; RNA_pol_Rpb2_3.
DR InterPro; IPR007641; RNA_pol_Rpb2_7.
DR InterPro; IPR014724; RNA_pol_RPB2_OB-fold.
DR PANTHER; PTHR20856; PTHR20856; 1.
DR Pfam; PF04563; RNA_pol_Rpb2_1; 1.
DR Pfam; PF04561; RNA_pol_Rpb2_2; 1.
DR Pfam; PF04565; RNA_pol_Rpb2_3; 1.
DR Pfam; PF00562; RNA_pol_Rpb2_6; 1.
DR Pfam; PF04560; RNA_pol_Rpb2_7; 1.
DR PROSITE; PS01166; RNA_POL_BETA; 1.
PE 3: Inferred from homology;
KW Chloroplast; DNA-directed RNA polymerase; Nucleotidyltransferase; Plastid;
KW Reference proteome; Transcription; Transferase.
FT CHAIN 1..1088
FT /note="DNA-directed RNA polymerase subunit beta"
FT /id="PRO_0000276593"
SQ SEQUENCE 1088 AA; 122797 MW; 7B81B60B9DE4C4D7 CRC64;
MTLFRQNSAL PNFLDSQRDS FRYFLETGIR EELDFFSPIV GQSLGSSSKR PTDRFISVSF
HSKDFYFKKP HYTPQEAVQK LGTYKSSLIV PVHVYSKYLN LNATFPVAFC DLPLMTEHGT
FILNGSPRVI VHQIVRCPGV YLKPQFDKQG NRTHLVSFLS AYGSWLRFET DKKGVVFAHI
DNLRKVPVTV FLQALGFSMD TIVGALKYPE ALDPTLKEVD WKLTTDEAIL LLMSRLFPNR
PATVLRGRKF LFNQFFNPRR YSLSDVGRKR VNQKFRMRSK TKHLTLTPQD ALAALDYLLR
CENGETEFLD DIDHLKNRRA RLAGELIQTQ FRLGLNRLER VIYNRISDEN ILRKTPGALG
SLNSLIRTQV LASVFQEFFG SNQLSQFMDQ TNPLAEITHK RRLSSLGPGG LNRDRAGLIV
RGIHPSYYGR ICPIETPEGK NAGLVGSIAT FTQINKNGFL ESPYYKLISE SNTPDRNGFF
LLSAFYEEDT VVAQGDVDLS NFRIPTRNKS QFTENTVQEI NFLGLCPIQF MSIATSLIPF
LEHDDANRAL MGSNMQRQAV SLLRSERPFV GTGLEAHVTR DIGATIVAKQ NSYISYVDAQ
RIDYFTPVIG DTNLIDYQNL TAEDVFASNQ FKHNTIWLTS YQRSNQDTCL NHKPLVEANT
WVEAGDCLAD NAATAKGELA LGRNILIGYM PWEGYNFEDA VLVSERLVYD DVFTSIHISR
YEVSTARLRE GQEYFTNQVD RNQYLDEFGV VKIGTWVEAG DVLVGKISPQ PDSDNDPESR
LLRAIFGGVA RNTKTTSYCL SSGVSGRILD VRCEFKRQTK NIEDESIEST GSVYVYLVEK
RRLQVGDKVA GRHGNKGIVS NILPRVDMPY LQSGKALDMV LNPLGVPSRM NVGQIFECLL
GLAANTLKQN FKVLPFDEMH GAEVSRGFVY HYLYKSRLLT QQKWLFKPNS PGKSIVFDGR
TGLNFDQPVT VGYPYILKLV HLVDDKIHAR STGPYSLVTQ QPLGGRSKKG GQRLGEMEVW
ALEGFGAAYV LQELLTIKSD DMIGRNRAFM SMIRGTLLPK SGIPESFKVL VSELRGLCLD
MSIARINF