ID   RPOB_ACOGR              Reviewed;        1071 AA.
AC   Q5QA72;
DT   21-JUN-2005, integrated into UniProtKB/Swiss-Prot.
DT   04-JAN-2005, sequence version 1.
DT   03-AUG-2022, entry version 65.
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   Acorus gramineus (Dwarf sweet flag).
OG   Plastid; Chloroplast.
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; Liliopsida; Acoraceae; Acorus.
OX   NCBI_TaxID=55184;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=15453916; DOI=10.1186/1471-2148-4-35;
RA   Stefanovic S., Rice D.W., Palmer J.D.;
RT   "Long branch attraction, taxon sampling, and the earliest angiosperms:
RT   Amborella or monocots?";
RL   BMC Evol. Biol. 4:35-35(2004).
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; AY757819; AAV74361.1; -; Genomic_DNA.
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..1071
FT                   /note="DNA-directed RNA polymerase subunit beta"
FT                   /id="PRO_0000048007"
SQ   SEQUENCE   1071 AA;  120968 MW;  55FECADB637488C3 CRC64;
     MPRDGNEGMF TIPGFSQIQF EGFCRFVDQG LMEEFHKFPK IEDTDQEIEF QLFVERYQLV
     EPLIKERDAV YESLTYSSEL YVPAGLIWKT GRDMQEQTIF IGNIPLMNSL GTFIVNGIYR
     IVINQILQSP GIYYRSELDH NGISVYTSTI ISDWGGRSEL EIDRKSRIWA RVSRKQKISI
     LVLSSAMGSN LREILDNVCY PEIFLSFLND REKKKIGSKE NAILEFYQQF ACVGGDPVFS
     ESLCKELQKK FFQQRCELGR IGRRNMNRRL NLDIPQSNTF LLPRDVLAAA DHLIGMKFGM
     GTLDDMNHLK NKRIRSVADL LQDQFGLALV RLENAVRGTI CGAIRHKLIL TPQNLVSSTS
     LTTTYESFFG LHPLSQVLDR TNPLTQIVHG RKLSYLGPGG LTGRTASFRI RDIHPSHYGR
     ICPIDTSEGI NVGLIGSLAI HARIGHWGSI ESPFYEVYQR SKETKMVFLS PSRDEYYTVA
     TGNSLALNRG GIQEEQIVPA RYRQEFLTIA WEQIHLRSIF PFQYFSIGAS LIPFIEHNDA
     NRALMSSNMQ RQAVPLSRSX XXXXXXXXXX XAALDSGVSA IAECEGKIIY TDTHKIVLSG
     HGDTISIPLV MYQRSNKNTC MHQNPQVRRG KCIKKGQILA DGAATVGGEL ALGKNVLVAY
     MPWEGYNFED AVLISERLVY EDIYTSFHIR KYEIQTHVTS QGPERITHEI PHLEAHLLRN
     LDRNGIVALG SWVETGDILV GKLTPQTANE SSYAPEDRLL RAILGIQVST AKETCLKLPI
     GGRGRVIDVR WIQKKGGSSY NPETIRVYIS QKREIKVGDK VAGRHGNKGI ISKILSRQDM
     PYLQDGTPVD MVFNPLGVPS RMNVGQIFEC SLGLAGDLLD RHYRIAPFDE RYEQEASRKL
     VFSELYEASK QTANPWVFEP EYPGKSRIFD GRTGDPFEQP VLIGKSYILK LIHQVDDKIH
     GRSSGHYALV TQQPLRGRAK QGGQRVGEME VWALEGFGVA HILQEMLTYK SDHIRARQEV
     LGTTIIGGTI PTPEDAPESF RLLVRELRSL ALELNHFLVS EKNFQINRKE A