ID   RPOB_LEMMI              Reviewed;        1072 AA.
AC   A9L988;
DT   08-APR-2008, integrated into UniProtKB/Swiss-Prot.
DT   05-FEB-2008, sequence version 1.
DT   03-AUG-2022, entry version 56.
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   Lemna minor (Common duckweed).
OG   Plastid; Chloroplast.
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; Liliopsida; Araceae; Lemnoideae; Lemna.
OX   NCBI_TaxID=4472;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=18463914; DOI=10.1007/s00239-008-9091-7;
RA   Mardanov A.V., Ravin N.V., Kuznetsov B.B., Samigullin T.H., Antonov A.S.,
RA   Kolganova T.V., Skyabin K.G.;
RT   "Complete sequence of the Duckweed (Lemna minor) chloroplast genome:
RT   structural organization and phylogenetic relationships to other
RT   angiosperms.";
RL   J. Mol. Evol. 66:555-564(2008).
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; DQ400350; ABD48487.1; -; Genomic_DNA.
DR   RefSeq; YP_001595500.1; NC_010109.1.
DR   AlphaFoldDB; A9L988; -.
DR   SMR; A9L988; -.
DR   PRIDE; A9L988; -.
DR   GeneID; 5787576; -.
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; -; 1.
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_0000329201"
SQ   SEQUENCE   1072 AA;  121219 MW;  77C057E707B0C85E CRC64;
     MLRDGNEGMF TIPGFSQIQF EGFCRFINQG LMEEFNKFPK IEDTDQEIEF KLFVETYQLA
     EPLIKERDAV YESLTYSSEL YVLAGLIWKT NRDMKEQTVF IGNIPLMNSL GTFIVNGIYR
     IVINQILQSP GIYYRSELDH NGISVYTSTI ISDWGGRSEL EIDRKARIWA RVSRKQKISI
     LVLLSAMGLN LREILDNVCY PEIFLSFLND KEKKKIGSKE NAILEFYQQF ACVGGDPVFS
     ESLCKELQKK FFQQRCELGR IGRRNINQRL NLDIPHNNTF LLPRDVLAAA DHLIGMKFGM
     GTLDDMNHLK NKRIRSVADL LQDQFGLALV RLENAVRGTI SGAIRHKLIP TPQNLVTSTS
     LTTTYESFFG LHPLSQVLDR TNPLTQIVHG RKLSYLGPGG VTGRTASFRI RDIHPSHYGR
     ICPIDTSEGI NVGLIGSLAI HVRIGHWGSI ETPFYEISER SKEKEARMIY LSPSRDEYYM
     IAAGNSLALN RGIQEEQVVP ARYRQEFLTI AWEQVHLRSI FPFQYFSIGA SLIPFIEHND
     ANRALMSSNM QRQAVPLSRS EKCIVGTGLE RQAALDSGVS VIAEHEGKVI STDTHQIVFS
     GNGNTLNIPL VMYQRSNKNT CMHQKPQVQR GKYVKKGQIL ADGAATVGGE LALGKNVLVA
     YMPWEGYNFE DAVLISERLV YSDIYTSFHI RKYEIQTHMT SQGPERITNE IPHLEAHLLR
     NLDRNGIVML GSWVETGDIL VGKLTPQIAN ESSYAPEDRL LRAILGIQVS TAKETSLKLP
     IGGRGRVIDV RWIQKKGGSS YNPEIIRVYI LQKREIKVGD KVAGRHGNKG IISKILPRQD
     MPYLQDGTPV DMVFNPLGVP SRMNVGQIFE CSLGLAGDLL NRHYRIAPFD ERYEQEASRK
     LVFSELYEAS KQTKNPWVFE PEYPGKSKIF DGRTGDPFEQ AVLIGKSYIL KLIHQVDDKI
     HGRSSGHYAL VTQQPLRGRA KQGGQRVGEM EVWALEGFGV AHILQEMLTY KSDHIRARQE
     VLGTTIIGGT IVNPEDAPES FRLLVRELRS LALELNHFLV SEKNFQINRK EA