ID   RPOB_CALFG              Reviewed;        1060 AA.
AC   Q7YJX8;
DT   16-JAN-2004, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2003, sequence version 1.
DT   03-AUG-2022, entry version 78.
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   Calycanthus floridus var. glaucus (Eastern sweetshrub) (Calycanthus
OS   fertilis var. ferax).
OG   Plastid; Chloroplast.
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; Magnoliidae; Laurales; Calycanthaceae;
OC   Calycanthus.
OX   NCBI_TaxID=212734;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Goremykin V., Hirsch-Ernst K.I., Woelfl S., Hellwig F.H.;
RT   "The chloroplast genome of the 'basal' angiosperm Calycanthus fertilis
RT   -- structural and phylogenetic analyses.";
RL   Plant Syst. Evol. 242:119-135(2003).
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; AJ428413; CAD28713.1; -; Genomic_DNA.
DR   RefSeq; NP_862746.2; NC_004993.1.
DR   AlphaFoldDB; Q7YJX8; -.
DR   SMR; Q7YJX8; -.
DR   GeneID; 2598032; -.
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..1060
FT                   /note="DNA-directed RNA polymerase subunit beta"
FT                   /id="PRO_0000048014"
SQ   SEQUENCE   1060 AA;  119316 MW;  4BB014230CD20AA1 CRC64;
     MPTIPGFSQI QFEGFCRFID QGLTEELHKF PKIEDTDQEI EFQLFVETYQ LVEPLIKERD
     AVYESLTYSS ELYVSAGLIW KTGRDMQEQT IFIGNIPLMN SLGNSIVSGI YRIVINQILQ
     SPGIYYRSEL DHNGISVYTG TIISDWGGRP ELEIDRKARI WARVSRKQKI SILVPSSAMG
     SNLREILDNV CYPEIFLSFP NDKEKKKIGS RENAILEFYK QFACVGGDPV FSESLCKELQ
     KKFFQQRCEL GRIGRRNMNR RLNIDIPQNN TFLLPRDVLA VVDHLIGMKF GMGTLDDMNH
     LKNKRIRSVA DLLQDQFGLA LVRLENAVRG TICGAIRHKL IPTPHNLVTS TPLTTTYESF
     FGLHPLSQVL DRTNPLTQIV HGRKSSYLGP GGLTGRTASF RIRDIHPSHY GRICPIDTSE
     GINVGLIGSL AIHARIGHWG SIESPFYEIS EKSKEIVYLP PSRDEYYMVA AGNSLALNRG
     IQEEQVVPAR YRQEFLTIAW EQIHLRSIFP FQYFSIGASL IPFIEHNDAN RALMSSNMQR
     QAVPLSRSEK CIVGTGLEGQ AALDSGVSAI AEHEGKIIYT DTDKIVLSGN RDTISIPLVM
     YQRSNKNTCM HQKPRVPRGK CIKKGQILAD GAATVGGELA LGKNVLVAHM PWEGYNSEDA
     VLISERLIYG DIYTSFHIRK YEIQTHVTSQ GPERITNEIP HLEAHLLRNL DKNGIVMLGS
     WIERGDILVG KLTPQAAKES SYAPEDRLLR AILGIQVSTA KETCLKLPIG GRGRVIDVRW
     IQKKGGSSYN PETIRVSILQ KREIKVGDKV AGRHGNKGIV SKILPRQDMP YLQDGTPVDM
     VFNPLGVPSR MNVGQMFECS LGLAGYLLDK HYRIAPFDER YEQEASRKLV FPELYSASKQ
     TVNPWVFEPE YPGKSRIFDG RTGDPFEQPV IIGKSYILKL IHQVDDKIHG RSSGHYALVT
     QQPLRGRAKQ GGQRVGEMEV WALEGFGVAH ISQEMLTYKS DHIRARQEVL GATIIGGTIP
     KPEDAPESFR LLVRELRSLA LELNHFLVSE KNFQINRKEA