ID   RPOB_MESVI              Reviewed;        1080 AA.
AC   Q9MUS5;
DT   27-APR-2001, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2000, sequence version 1.
DT   03-AUG-2022, entry version 94.
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   Mesostigma viride (Green alga).
OG   Plastid; Chloroplast.
OC   Eukaryota; Viridiplantae; Streptophyta; Mesostigmatophyceae;
OC   Mesostigmatales; Mesostigmataceae; Mesostigma.
OX   NCBI_TaxID=41882;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NIES-296 / KY-14 / CCMP 2046;
RX   PubMed=10688199; DOI=10.1038/35001059;
RA   Lemieux C., Otis C., Turmel M.;
RT   "Ancestral chloroplast genome in Mesostigma viride reveals an early branch
RT   of green plant evolution.";
RL   Nature 403:649-652(2000).
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; AF166114; AAF43826.1; -; Genomic_DNA.
DR   RefSeq; NP_038385.1; NC_002186.1.
DR   AlphaFoldDB; Q9MUS5; -.
DR   SMR; Q9MUS5; -.
DR   PRIDE; Q9MUS5; -.
DR   GeneID; 800856; -.
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; IPR019462; DNA-dir_RNA_pol_bsu_external_1.
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; 1.
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; PF10385; RNA_pol_Rpb2_45; 1.
DR   Pfam; PF00562; RNA_pol_Rpb2_6; 1.
DR   Pfam; PF04560; RNA_pol_Rpb2_7; 1.
DR   TIGRFAMs; TIGR02013; rpoB; 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..1080
FT                   /note="DNA-directed RNA polymerase subunit beta"
FT                   /id="PRO_0000048031"
SQ   SEQUENCE   1080 AA;  121911 MW;  6FECC1BDB547422A CRC64;
     MMIIEEYTPV PNTAFDFKIP DLIEMQLSSF RIFLKKGLIE ELKDFSVISN SKKNLELRFF
     PEKYKLKRPK YNERTSIRRA STYTCQLYVP AKLTNKRTGE IQEQDVFLGE IPLMTGRGSF
     IINGSSRVIV NQIVRSPGIY YKREIDKKGR KTHSATIISN RGAWLRIETD KNGLIWARIG
     KIRKVSIMIV FKAMGLTKNE IFDALKYPQF LKKTIQETDP YLENDIQHDD DFENESTSTL
     LSTREILESR FFQSKYYDLG KVGRYKINKK LQLNIPENIR VLTVQDILAA VDYLINLEFN
     IGTLDDIDHL KNRRVRSVGE LIQNQVRVGL GRLERMIYKR MGESSPDSLT LTSLVNPKPL
     VGAIREFFGS SQLSQFMDQT NPLSEITHKR RLSCLGPGGL SRERAGLAVR DIHPSHYGRI
     CPIETPEGPN AGLIGSLATH SRVNEYGFLE SPFYITKNRK VIKSELPIYL APDQEDQFKV
     APGDLLLSCY SSIENNYVPV RYKQEFTTSK AEEVDYVGIS PTQAISIATS LIPFLEHDDA
     NRALMGSNMQ RQAVPLLKPN RPIVGTGFEE QVALDSGTVV ICRHKGIVIS VDSKTILVRS
     LRMNAKGIQH SHIDRYYLQK YNRSNQDTCI NQKPVVSQGE WVQKGDILAD GSATVNGELT
     LGQNILVAYM PWEGYNFEDA ILISEKLVYE DIYTSIHIEK YEVDARKTKL GPEKITREIP
     NVNDHLLRNL DDNGIVIPGA RVESGDILVG KVTPKEDLDQ HPEGKLLRAI FGEKARDVRD
     SSLRVPNGVS GTVVNVRRLT GKELPSGVIM MVHVSISQKR KIQVGDKMAG RHGNKGIISK
     ILPRQDMPYL QDGTPVDMVL NPLGVPSRMN VGQVFECLLG LAGEYLSENY KLMPFDEMYG
     KETSRGLVYS KLYEARQKTG YPWLFNIQSP GKSKLFDGRT GESFDQPVTI GKAYMLKLVH
     LVDDKIHARS TGPYSLVTQQ PLGGRAKHGG QRLGEMEVWA LEGFGAAYTL QELLTIKSDD
     MKGRNDALNA IIKGRPIPKP GTPESFKVLI RELQSLCLDI GVYKVHKSNK NQEIDLMQNF