ID   RPOB_PINKO              Reviewed;        1075 AA.
AC   Q85X54;
DT   16-JAN-2004, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2003, sequence version 1.
DT   03-AUG-2022, entry version 77.
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 koraiensis (Korean pine).
OG   Plastid; Chloroplast.
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Pinopsida; Pinidae; Conifers I; Pinales; Pinaceae; Pinus;
OC   Pinus subgen. Strobus.
OX   NCBI_TaxID=88728;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=KangWon16;
RA   Noh E.W., Lee J.S., Choi Y.I., Han M.S., Yi Y.S., Han S.U.;
RT   "Complete nucleotide sequence of Pinus koraiensis.";
RL   Submitted (FEB-2003) to the EMBL/GenBank/DDBJ databases.
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; AY228468; AAO74009.1; -; Genomic_DNA.
DR   RefSeq; NP_817162.1; NC_004677.2.
DR   AlphaFoldDB; Q85X54; -.
DR   SMR; Q85X54; -.
DR   PRIDE; Q85X54; -.
DR   GeneID; 806901; -.
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_0000048040"
FT   REGION          966..986
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1075 AA;  122369 MW;  D45B1ABAF671A118 CRC64;
     MRLDENEGAF TIPEFGKIQF EGFCRFIDQG LMEELHNFPK IEDTDKEIEF SLFGNEYELA
     EPFIKERDAV YQSLTYYSEL YVPARSIRRN SRKIQKQTVF LGNIPLMNSH GTFVVNGIYR
     IVVNQILISP GIYYRSELDH NRINYIYTGT LISDWGRRSK LEIDVGERIW ARVSRKRKIS
     IPVLLSAMGL NLEEILDNTH YPKRFLFLLK KKERWEREEY LWSREKAILE FYKKLYCVSG
     DLVFSESLCK ELQEKFFRQR CELGKIGRRN LNQKLNLDIP ENEIFSLPQD VLAAVDYLIG
     VKFGMGTLDD IDHLRNRRIR SVADLLQNQF RLTLGHLEDT VRRTIHGATK RRSTPQNLVT
     STLFKNTFQD FFGSHPLSQF LDQTNPLTEI AHGRKLSHLG PGGLTGRTAS FRTRDIHPSY
     YGRICPIDTS EGMNAGLVSS LSIHAKIGDC GSLQSPFYKI SERSREEHMV YLLPGEDEDE
     YYRIATGNSL ALNQGIQEEQ ITPARYRQEF IVIAWEQIHF RSIFPFQYFS VGVSLIPFLE
     HNDANRALMG SNMQRQAVPL FRPEKCIAGT GLEGQAALDS GSVAIATQEG RIEYIDAVNI
     TSSINGDTVR TESVIYQRSN TNTCTHQKPQ VRQGECVKKG QILADGATTV GGELSLGKNV
     LVAYMPWEGY NFEDAILISE RLVYEDIYTS FHIVRYRIEI CMTSQGPERI TREIPHLDAH
     SLRHLDENGL VMLGSWIETG DVLVGKLTPQ TTEESLCTPE GRLLQTIFGI EVSTARESCL
     RAPIGGKGRV IDVRWINRVD DSGDNAETVH VYISQKRKIQ VGDKVAGRHG NKGIISIILP
     RQDMPYLQNG IPVDMVLNPL GVPSRMNVGQ IFECLPGLAG NLMNKHYRIT PFDEKYEREA
     SRKLVFPELY KASEQTANPW VFEPDHPGKH RLIDGRTGAV FEQPVTIGKA YMSKLSHQVD
     EKIHARSSGP YARVTQQPLR GKSKRGGQRI GEMEVWALEG FGVAYILQEM LTLKSDHIRT
     RNEVLGAIIT GGPIPKPDTA PESFRLLIRE LRSLALELNH AIISEKDFQI DREEV