ID   RPOB_ZYGCR              Reviewed;        1063 AA.
AC   Q32RG0;
DT   21-FEB-2006, integrated into UniProtKB/Swiss-Prot.
DT   06-DEC-2005, sequence version 1.
DT   03-AUG-2022, entry version 63.
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   Zygnema circumcarinatum (Green alga).
OG   Plastid; Chloroplast.
OC   Eukaryota; Viridiplantae; Streptophyta; Zygnemophyceae; Zygnematophycidae;
OC   Zygnematales; Zygnemataceae; Zygnema.
OX   NCBI_TaxID=35869;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=16236178; DOI=10.1186/1741-7007-3-22;
RA   Turmel M., Otis C., Lemieux C.;
RT   "The complete chloroplast DNA sequences of the charophycean green algae
RT   Staurastrum and Zygnema reveal that the chloroplast genome underwent
RT   extensive changes during the evolution of the Zygnematales.";
RL   BMC Biol. 3:22-22(2005).
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; AY958086; AAX45862.1; -; Genomic_DNA.
DR   RefSeq; YP_636566.1; NC_008117.1.
DR   AlphaFoldDB; Q32RG0; -.
DR   SMR; Q32RG0; -.
DR   GeneID; 4108182; -.
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; 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; 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..1063
FT                   /note="DNA-directed RNA polymerase subunit beta"
FT                   /id="PRO_0000224135"
SQ   SEQUENCE   1063 AA;  119295 MW;  F2A3B5E9F8E085FC CRC64;
     MLSINRNAGM FVLPDFKQIQ IDSFRHFLTD LLRLELQRFG TIKHANQQLE FKLLGELYRL
     EIPKFNEREA VYQSATYSSN LYAPAYLVDK KRGIIQKQTV FLGSIPLMSA RGTFVIRGVS
     RCIVSQLLRS PGIYYTLSVQ GVYTATIICN SGKSFKLELD RQGCLWVRVG RNSKAPLLLL
     LIALGLEMRY IPPMIVQRTK KLNQLLLCVE DAKIDLCKRL KLKQKTTQIE LGVTDPIYSL
     FLKPYELGRM GRLNLNKRLN LRVSEFEILL RSQDLIVASD YLVQVSNGIG SLDDIDDLKH
     KRVKWVSDLF CVQLNMALKK LNVAVHTNLN KMEARISRMS LKSVVSSNAI ATTFFRFVAS
     YQLSQFLDQT NPLSEIVHKR KLSLLGPGGL TPRTARFRVR DIHPSQYGRI CPVQTAEGQN
     AGVVNSFTIC AHIGDNGAIK TSLYKVCTNS MQGHVIDMLP GEDEYSTIAT ESCLVVANSS
     NQFQSIPAQH RREFVTLRWD EIGFRNTLPV HSFSVGVVLI PFLEHDDATR ALMGSNMQRQ
     AVPLLKLERP IVGTGIESQV ALDSGTVITA VQECKIHNVD ATQIAYVPKD SFELLYINLL
     NYERSNNATC LHQRPIVECG ETVQKGQLIA DGSATVDGEL ALGKNVLVAY MPWEGYNFED
     AVLINERLIY EDVYTSLHIE RYEAEARETN QAIETITKQI PHLNAHVLRH LDETGVVSLG
     AWVETGDVLV GKLTAKQSEG LLHTPESKLL QDILGVQAFG TQDTCLKVPT RGEGRVIDVR
     WITRDNHLLG HRKVIHVYIL QERKIQVGDK VAGRHGNKGV VSRILPRQDM PYLQDGTPVD
     MVLSPLGVPS RMNVGQVFEC LLGLAGGYLN QHYRIMPFDE RYGRESSRKL VFSELYKASQ
     TTNYPWIFEP DSPGKSRLFD GRTGEVFNQP VTVGRAYMFK LIHQVDDKIH ARSTGPYALV
     TQQPVRGRSR QGGQRVGEME VWAFQGFGAA CVLQELLTTK SDHATARAEA PNAIVTGNLV
     PKPIGTSDCL GVLIRELQCL GIQLDHTMLS QHNMIQYPNL NEE