ID   RPOB_LOBMA              Reviewed;        1072 AA.
AC   A4QLI6;
DT   11-SEP-2007, integrated into UniProtKB/Swiss-Prot.
DT   15-MAY-2007, sequence version 1.
DT   03-AUG-2022, entry version 57.
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   Lobularia maritima (Sweet alyssum) (Alyssum maritimum).
OG   Plastid; Chloroplast.
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   rosids; malvids; Brassicales; Brassicaceae; Anastaticeae; Lobularia.
OX   NCBI_TaxID=226051;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Hosouchi T., Tsuruoka H., Kotani H.;
RT   "Sequencing analysis of Lobularia maritima 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; AP009375; BAF50541.1; -; Genomic_DNA.
DR   RefSeq; YP_001123717.1; NC_009274.1.
DR   AlphaFoldDB; A4QLI6; -.
DR   SMR; A4QLI6; -.
DR   GeneID; 4964888; -.
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_0000300447"
SQ   SEQUENCE   1072 AA;  121059 MW;  42D44EB621468CB6 CRC64;
     MLGDGKEGTS TIPGFNQIQF EGFYRFIDQG LIEELSKFPK IEDIDHEIEF QLFVETYQLV
     EPLIKERDAV YESLTYSSEL YVSAGLIWKT SRNMQEQRIF IGNIPLMNSL GTSIVNGIYR
     IVINQILQSP GIYYQSELDH NGISVYTGTI ISDWGGRLEL EIDKKARIWA RVSRKQKISI
     LVLSSAMGSN LREILENVCY PEIFLSFLTD KEKKKIGSKE NAILEFYKQF SCVGGDPIFS
     ESLCKELQKK FFHQRCELGR IGRRNINWRL NLNIPQNNIF LLPRDILAAA DHLIGMKFGM
     GTLDDMNHLK NKRIRSVADL LQDQLGLALA RLENVVKGTI GGAIRHKLIP TPQNLVTSTP
     LTTTYESFFG LHPLSQVLDR TNPLTQIVHG RKLSYLGPGG LTGRTANFRI RDIHPSHYGR
     ICPIDTSEGI NVGLIGSLSI HARIGDWGSL ESPFYELFEK SKKARIRMLF LSPSQDEYYM
     IAAGNSLALN RGIQEEQAVP ARYRQEFLTI AWEEVHLRSI LPFQYFSIGA SLIPFIEHND
     ANRALMSSNM QRQAVPLSRS EKCIVGTGLE RQVALDSGVP AIAEHEGKIL YTDTEKIILS
     GNGDTFSIPL IMYQRSNKNT CMHQKPQVRR GKYIKKGQIL ADGAATVGGE LSLGKNILVA
     YMPWEGYNFE DAVLISESLV YDDIYTSFHI RKYEIQTHVT TQGPERITKE IPHLEGRLLR
     NLDKNGIVML GSWVETGDIL VGKLTPQVAK ESSYAPEDRL LRAILGIQVS TSKETCLKLP
     IGGRGRVIDV RWVQKKGGSS YNPEKIRVYI SQKREIKVGD KVAGRHGNKG IISKILPRQD
     MPYLQDGRPV DMVFNPLGVP SRMNVGQIFE CSLGLAGSLL DRHYRIAPFD ERYEQEASRK
     LVFSELYQAS KQTANPWVFE PEYPGKSRIF DGRTGDPFEQ PVIIGKPYIL KLIHQVDDKI
     HGRSSGHYAL VTQQPLRGRS KQGGQRVGEM EVWALEGFGV AHILQEMLTY KSDHIRARQE
     VLATTIIGGT IPKPEDAPES FRLLVRELRS LALELNHFLV SEKNFQINRK AV