ID   RPOB_AETGR              Reviewed;        1073 AA.
AC   A4QJJ1;
DT   11-SEP-2007, integrated into UniProtKB/Swiss-Prot.
DT   15-MAY-2007, sequence version 1.
DT   03-AUG-2022, entry version 55.
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   Aethionema grandiflorum (Persian stone-cress).
OG   Plastid; Chloroplast.
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   rosids; malvids; Brassicales; Brassicaceae; Aethionemeae; Aethionema.
OX   NCBI_TaxID=72657;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Hosouchi T., Tsuruoka H., Kotani H.;
RT   "Sequencing analysis of Aethionema grandiflorum 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; AP009367; BAF49846.1; -; Genomic_DNA.
DR   RefSeq; YP_001123022.1; NC_009266.1.
DR   AlphaFoldDB; A4QJJ1; -.
DR   SMR; A4QJJ1; -.
DR   GeneID; 4962267; -.
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..1073
FT                   /note="DNA-directed RNA polymerase subunit beta"
FT                   /id="PRO_0000300430"
SQ   SEQUENCE   1073 AA;  120945 MW;  8EBA69868E40BAB7 CRC64;
     MLGDGKEGTS TIPGFNQIQF EGFYRFIDQG LIEEVSKFPK IEDIDQEIEF QLFVETYQLV
     EPLRKERDAV YESLTYSSEL YVSAGLIWKT SRKMQEQRIF IGNIPLMNSL GTSIVNGIYR
     IVINQILQSP GIYYQSELDH NGISVYTGTI ISDWGGRLEL EIDKKARIWA RVSRKQKISI
     LVLSSAMGSN LREILENVCY PEIFLSFLTD KEKKKIGSKE NAILEFYQQF SCVGGDPIFS
     ESLCKELQKK FFHQRCELGR IGRRNINWRL NLTIPQNNIF LLPRDILAAA DHLIGMKFGM
     GTLDDMNHLK NKRIRSVADL LQDQFGLALA RLENVVKGTI CGAIKHKLIP TPQNLVTATP
     LTTTYESFFG LHPLSQVLDR TNPLTQIVHG RKLSYLGPGG LTGRTANFRI RDIHPSHYGR
     ICPIDTSEGI NVGLIGSLAI HARIGDWGSL ESPFYELFEK SKKARIRMLF LSPSQDEYYM
     IAAGNSLALN RGIQEEQAVP ARYRQEFLTI AWEEVHLRSI FPFQYFSIGA SLIPFIEHND
     ANRALMSSNM QRQAVPLSRS EKCIVGTGLE RQVALDSGVP AIAEQEGKIL YTDTKKIILS
     GNGDNTLGIP LIMYQRSNKN TCMHQKSQVR RGKCIKKGQI LADGAATVGG ELALGKNILV
     AYMPWEGYNF EDAVLISECL VYGDIYTSFH IRKYEIQTHV TTQGPERITK EIPHLEGHLL
     RNLDKNGIVM LGSWVETGDI LVGKLTPQVA KESSYAPEDR LLRAILGIQV STSKETCLKL
     PIGGRGRVID VGWVQKKGGS SYNPEKIRVY ISQKREIKVG DKVAGRHGNK GIISKILPRQ
     DMPYLQDGRP VDMVFNPLGV PSRMNVGQIF ECSLGLAGSL LDRHYRIAPF DERYEQEASR
     KLVFSELYEA SKQTANPWVF EPEYPGKSRI FDGRTGDPFE QPVIIGKPYI LKLIHQVDDK
     IHGRSSGHYA LVTQQPLRGR SKQGGQRVGE MEVWALEGFG VAHILQEMLT YKSDHIRARQ
     EVLGTTIVGG TIPKPEDAPE SFRLLVRELR SLALDLNHFL VSEKNFQINR KEV