RPOB_ARATH
ID RPOB_ARATH Reviewed; 1072 AA.
AC P50546;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 03-MAY-2011, sequence version 4.
DT 03-AUG-2022, entry version 157.
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=AtCg00190;
OS Arabidopsis thaliana (Mouse-ear cress).
OG Plastid; Chloroplast.
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; malvids; Brassicales; Brassicaceae; Camelineae; Arabidopsis.
OX NCBI_TaxID=3702;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=cv. Landsberg erecta; TISSUE=Leaf;
RX PubMed=10601874; DOI=10.1046/j.1432-1327.2000.00991.x;
RA Pfannschmidt T., Ogrzewalla K., Baginsky S., Sickmann A., Meyer H.E.,
RA Link G.;
RT "The multisubunit chloroplast RNA polymerase A from mustard (Sinapis alba
RT L.). Integration of a prokaryotic core into a larger complex with
RT organelle-specific functions.";
RL Eur. J. Biochem. 267:253-261(2000).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=10574454; DOI=10.1093/dnares/6.5.283;
RA Sato S., Nakamura Y., Kaneko T., Asamizu E., Tabata S.;
RT "Complete structure of the chloroplast genome of Arabidopsis thaliana.";
RL DNA Res. 6:283-290(1999).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 346-713.
RC STRAIN=cv. Landsberg erecta; TISSUE=Cotyledon;
RA Knut J., Pfannschmidt T., Liere K., Link G.;
RL Submitted (FEB-1995) 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 -!- 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}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAA74024.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR EMBL; Y13690; CAA74024.1; ALT_INIT; Genomic_DNA.
DR EMBL; AP000423; BAA84377.1; -; Genomic_DNA.
DR EMBL; X84159; CAA58965.1; -; Genomic_DNA.
DR PIR; S52324; S52324.
DR RefSeq; NP_051051.1; NC_000932.1.
DR AlphaFoldDB; P50546; -.
DR SMR; P50546; -.
DR BioGRID; 29977; 19.
DR IntAct; P50546; 2.
DR MINT; P50546; -.
DR STRING; 3702.ATCG00190.1; -.
DR PaxDb; P50546; -.
DR PRIDE; P50546; -.
DR ProteomicsDB; 228238; -.
DR EnsemblPlants; ATCG00190.1; ATCG00190.1; ATCG00190.
DR GeneID; 844783; -.
DR Gramene; ATCG00190.1; ATCG00190.1; ATCG00190.
DR KEGG; ath:ArthCp014; -.
DR Araport; ATCG00190; -.
DR TAIR; locus:504954643; ATCG00190.
DR eggNOG; KOG0214; Eukaryota.
DR HOGENOM; CLU_000524_4_3_1; -.
DR InParanoid; P50546; -.
DR OMA; FMTWEGY; -.
DR OrthoDB; 944344at2759; -.
DR PRO; PR:P50546; -.
DR Proteomes; UP000006548; Chloroplast.
DR ExpressionAtlas; P50546; baseline and differential.
DR Genevisible; P50546; AT.
DR GO; GO:0009507; C:chloroplast; IDA:TAIR.
DR GO; GO:0042644; C:chloroplast nucleoid; HDA:TAIR.
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; TAS:TAIR.
DR GO; GO:0003729; F:mRNA binding; IDA:TAIR.
DR GO; GO:0032549; F:ribonucleoside binding; IEA:InterPro.
DR GO; GO:0006354; P:DNA-templated transcription, elongation; TAS:TAIR.
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; 3.
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..1072
FT /note="DNA-directed RNA polymerase subunit beta"
FT /id="PRO_0000048011"
FT CONFLICT 286
FT /note="V -> I (in Ref. 1; CAA74024)"
FT /evidence="ECO:0000305"
FT CONFLICT 341
FT /note="S -> G (in Ref. 1; CAA74024)"
FT /evidence="ECO:0000305"
FT CONFLICT 346
FT /note="H -> Y (in Ref. 1; CAA74024 and 3; CAA58965)"
FT /evidence="ECO:0000305"
FT CONFLICT 599
FT /note="F -> L (in Ref. 1; CAA74024 and 3; CAA58965)"
FT /evidence="ECO:0000305"
FT CONFLICT 927
FT /note="S -> T (in Ref. 1; CAA74024)"
FT /evidence="ECO:0000305"
FT CONFLICT 958..959
FT /note="DK -> VI (in Ref. 1; CAA74024)"
FT /evidence="ECO:0000305"
FT CONFLICT 1038
FT /note="P -> Q (in Ref. 1; CAA74024)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1072 AA; 121059 MW; DD84376968E64F8A CRC64;
MLGDEKEGTS AIPGFNQIQF EGFYRFIDQG LIEELAKFPK IEDIDHEIEF QLFVETYQLV
EPLIKERDAV YESLTYSSEL YVSAGLIWKT SRNMQEQRIF IGNIPLMNSL GTSIVNGIYR
IVINQILQSP GIYYQSELDH NGISVYTGTI ISDWGGRLEL EIDKKARIWA RVSRKQKISI
LVLSSAMGLN LREILENVCY PEIFLSFLTD KEKKKIGSKE NAILEFYQQF SCVGGDPIFS
ESLCKELQKK FFHQRCELGR IGRRNINWRL NLNIPQNNIF LLPRDVLAAA DHLIGMKFGM
GTLDDMNHLK NKRIRSVADL LQDQLGLALA RLENVVKGTI SGAIRHKLIP TPQNLVTSTP
LTTTYESFFG LHPLSQVLDR TNPLTQIVHG RKLSYLGPGG LTGRTANFRI RDIHPSHYGR
ICPIDTSEGI NVGLIGSLSI HARIGDWGSL ESPFYELFEK SKKARIRMLF LSPSQDEYYM
IAAGNSLALN RGIQEEQAVP ARYRQEFLTI AWEEVHLRSI FPFQYFSIGA SLIPFIEHND
ANRALMSSNM QRQAVPLSRS EKCIVGTGLE RQVALDSGVP AIAEHEGKIL YTDTEKIVFS
GNGDTLSIPL IMYQRSNKNT CMHQKPQVRR GKCIKKGQIL ADGAATVGGE LALGKNILVA
YMPWEGYNFE DAVLISECLV YGDIYTSFHI RKYEIQTHVT TQGPERITKE IPHLEGRLLR
NLDKNGIVML GSWVETGDIL VGKLTPQVAK ESSYAPEDRL LRAILGIQVS TSKETCLKLP
IGGRGRVIDV RWVQKKGGSS YNPEIIRVYI SQKREIKVGD KVAGRHGNKG IISKILPRQD
MPYLQDGRPV DMVFNPLGVP SRMNVGQIFE CSLGLAGSLL DRHYRIAPFD ERYEQEASRK
LVFSELYEAS KQTANPWVFE PEYPGKSRIF DGRTGDPFEQ PVIIGKPYIL KLIHQVDDKI
HGRSSGHYAL VTQQPLRGRS KQGGQRVGEM EVWALEGFGV AHILQEMLTY KSDHIRARQE
VLGTTIIGGT IPKPEDAPES FRLLVRELRS LALELNHFLV SEKNFQINRK EV
