ID   RPOB_NASOF              Reviewed;        1072 AA.
AC   A4QLS5;
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   Nasturtium officinale (Watercress) (Rorippa nasturtium-aquaticum).
OG   Plastid; Chloroplast.
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   rosids; malvids; Brassicales; Brassicaceae; Cardamineae; Nasturtium.
OX   NCBI_TaxID=65948;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Hosouchi T., Tsuruoka H., Kotani H.;
RT   "Sequencing analysis of Nasturtium officinale 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; AP009376; BAF50630.1; -; Genomic_DNA.
DR   RefSeq; YP_001123806.1; NC_009275.1.
DR   AlphaFoldDB; A4QLS5; -.
DR   SMR; A4QLS5; -.
DR   GeneID; 4962116; -.
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_0000300449"
SQ   SEQUENCE   1072 AA;  121076 MW;  432F2238671211B1 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 LQDQLGLALS RLENVVKGTI SGAIRHKLIP TPQNLVTSTP
     LTTTYESFFG LHPLSQVLDR TNPLTQIVHG RKLSYLGPGG LTGRTANFRI RDIHPSHYGR
     ICPIDTSEGI NVGLIGSLSI HARIGDWGSL ESPFYELFEK SKKARIRMLF LSPSQDEYFM
     IAAGNSLALN RGIQEEQAVP ARYRQEFLTI AWEEVHLRSI FPFQYFSIGA SLIPFIEHND
     ANRALMSSNM QRQAVPLSRS EKCIVGTGLE RQVALDSGVP AIAEHEGKIL YTDTEKIVFS
     GNGDTLSIPL IMYERSNKNT CMHQKPQVRR GKCIKKGQIL ADGAATVGGE LALGKNILVA
     YMPWEGYNFE DAVLISECLV YGDIYTSFHI RKYEIQTHVT TQGPERITKE IPHLEGRLLR
     HLDKNGIVML GSWVETGDIL VGKLTPQVAK ESSYAPEDRL LRAILGIQVS TSKETCLKLP
     IGGRGRVIDV RWVQKKGGSS YNPEIIRVYI SQKREIKVGD KVAGRHGNKG IISKILPRQD
     MPYLQDGRPV DMVFNPLGVP SRMNVGQIFE CSLGLAGSLL DRHYRIAPFD ERYEQEASRK
     LVFSELYKAS KQTANPWVFE PEYPGKSRIF DGRTGDPFEQ PVIIGKPYIL KLIHQVDDKI
     HGRSSGHYAL VTQQPLRGRS KQGGQRVGEM EVWALEGFGV AHILQEMLTY KSDHIRARQE
     VLGTTIIGGT IPKPEDAPES FRLLVRELRS LALELNHFLV SEKNFQINRK EV