RPOB_BARVE
ID RPOB_BARVE Reviewed; 1072 AA.
AC A4QK97;
DT 11-SEP-2007, integrated into UniProtKB/Swiss-Prot.
DT 15-MAY-2007, sequence version 1.
DT 03-AUG-2022, entry version 58.
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};
OS Barbarea verna (Early yellowrocket) (Erysimum vernum).
OG Plastid; Chloroplast.
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; malvids; Brassicales; Brassicaceae; Cardamineae; Barbarea.
OX NCBI_TaxID=50458;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Hosouchi T., Tsuruoka H., Kotani H.;
RT "Sequencing analysis of Barbarea verna chloroplast DNA.";
RL Submitted (MAR-2007) 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_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; AP009370; BAF50102.1; -; Genomic_DNA.
DR RefSeq; YP_001123278.1; NC_009269.1.
DR AlphaFoldDB; A4QK97; -.
DR SMR; A4QK97; -.
DR GeneID; 4961892; -.
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; 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 Transcription; Transferase.
FT CHAIN 1..1072
FT /note="DNA-directed RNA polymerase subunit beta"
FT /id="PRO_0000300433"
SQ SEQUENCE 1072 AA; 121054 MW; 0A62B1F8B5896A4E CRC64;
MLGDGKEGTS TIPGFNQIQF EGFYRFIDQG LIEELSKFPK IEDIDHEIEF QLFMETYQLV
EPLIKERDAV YESLTYSSEL YVSAGLIWKT SRNMQEQRIF IGNIPLMNSL GTSIVNGIYR
IVINQILQSP GIYYQSELDH NGISVYTGTI ISDWGGRLEL EIDKKARIWA RVSRKQKISI
LVLSSAMGSN LREILENVCY PEIFLSFLTD KEKKKIGSKE NAILEFYQQF SCVGGDPIFS
ESLCKELQKK FFHQRCELGR IGRRNINWRL NLNIPQNNIF LLPRDILAAA 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 IMYERSNKNT 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