ID   RPOB_PINTH              Reviewed;        1075 AA.
AC   P41607;
DT   01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1995, sequence version 1.
DT   03-AUG-2022, entry version 103.
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   Pinus thunbergii (Japanese black pine) (Pinus thunbergiana).
OG   Plastid; Chloroplast.
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Pinopsida; Pinidae; Conifers I; Pinales; Pinaceae; Pinus;
OC   Pinus subgen. Pinus.
OX   NCBI_TaxID=3350;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=7937893; DOI=10.1073/pnas.91.21.9794;
RA   Wakasugi T., Tsudzuki J., Ito S., Nakashima K., Tsudzuki T., Sugiura M.;
RT   "Loss of all ndh genes as determined by sequencing the entire chloroplast
RT   genome of the black pine Pinus thunbergii.";
RL   Proc. Natl. Acad. Sci. U.S.A. 91:9794-9798(1994).
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; D17510; BAA04326.1; -; Genomic_DNA.
DR   PIR; T07448; T07448.
DR   RefSeq; NP_042369.1; NC_001631.1.
DR   AlphaFoldDB; P41607; -.
DR   SMR; P41607; -.
DR   PRIDE; P41607; -.
DR   GeneID; 809068; -.
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; 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..1075
FT                   /note="DNA-directed RNA polymerase subunit beta"
FT                   /id="PRO_0000048041"
SQ   SEQUENCE   1075 AA;  122471 MW;  00677BC6D8F26ACA CRC64;
     MRLDENEGAF TIPEFGKIQF EGFCRFIDQG LMEELHNFPK IEDIDKEIEF RLFGNEYELA
     EPFIKERDAV YQSLTYYSEL YVPARSIRRN SRKIQKQTVF LGNIPLMNSH GTFVVNGIYR
     VVVNQILISP GIYYRSELDH NRINYIYTGT LISDWGRRSK LEIDVGERIW ARVSRKQKIS
     IPVLLSAMGL NLEEILDNTR YPERFLFLLK KKGRWEREEY LWSREKAILE FYKKLYCISG
     DLVFSESLCK ELQKKFFRKR CELGKIGRRN LNQKLNLDIP ENEIFSLPQD VLAAVDYLIG
     VKFGMGTLDD IDHLRNRRIR SVADLLQNQF RLALGRLEDA VKRTIRRATK RRSTPQNLVT
     STLLKNTFQD FFGSHPLSQF LDQTNPLTEI AHGRKLSHLG PGGLTGRTAS FRTRDIHPSY
     YGRICPIDTS EGMNAGLVAS LSIHAKIGDC GSLQSPFYKI SERSREEHMV YLLPGEDEDE
     YYRIATGNSL ALNQGIQEEQ ITPARYRQEF IVIAWEQIHF RSIFPFQYFS VGVSLIPFLE
     HNDANRALMG SNMQRQAVPL FRPEKCIAGT GLEGQAALDS GSVAIATQEG RIEYIDAVNI
     TSSVNGDTVR TESVIYQRSN TNTCTHQKPQ IHQGECVKKG QILADGATTV GGELSLGKNV
     LVAYMPWEGY NFEDAILISE RLVYEDIYTS FHIVRYRIEI CMTSQGPERI TREIPHLDAH
     LLRHLDENGL VMLGSWIETG DVLVGKLTPQ TIEESLCTPE GRLLQTIFGI EVSTARENCL
     RAPIGGRGRV IDVRWINRVD DSGDNAETVH VYISQKRKIQ VGDKVSGRHG NKGIISIVLP
     RQDMPYLQNG IPVDMVLNPL GVPSRMNVGQ IFECLPGLAG NPMNKHYRIT PFDEKYEREA
     SRKLVFPELY KASEQTANPW VFEPDHPGKH RLIDGRTGDV FEQPVTIGKA YMSKLSHQVD
     EKIHARSSGP YARVTQQPLR GKSKRGGQRI GEMEVWALEG FGVAYILQEM LTLKSDHIRT
     RNEVLGAIIT GGPIPKPDTA PESFRLLIRE LRSLALELNH AIISEKNFQI DREEV