ID   RPOB_CYCTA              Reviewed;        1072 AA.
AC   A6H5F9;
DT   11-SEP-2007, integrated into UniProtKB/Swiss-Prot.
DT   24-JUL-2007, sequence version 1.
DT   03-AUG-2022, entry version 56.
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   Cycas taitungensis (Prince sago) (Cycas taiwaniana).
OG   Plastid; Chloroplast.
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Cycadidae; Cycadales; Cycadaceae; Cycas.
OX   NCBI_TaxID=54799;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=17383970; DOI=10.1093/molbev/msm059;
RA   Wu C.-S., Wang Y.-N., Liu S.-M., Chaw S.-M.;
RT   "Chloroplast genome (cpDNA) of Cycas taitungensis and 56 cp protein-coding
RT   genes of Gnetum parvifolium: insights into cpDNA evolution and phylogeny of
RT   extant seed plants.";
RL   Mol. Biol. Evol. 24:1366-1379(2007).
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; AP009339; BAF64925.1; -; Genomic_DNA.
DR   RefSeq; YP_001312184.1; NC_009618.1.
DR   AlphaFoldDB; A6H5F9; -.
DR   SMR; A6H5F9; -.
DR   PRIDE; A6H5F9; -.
DR   GeneID; 5309613; -.
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; 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.
PE   3: Inferred from homology;
KW   Chloroplast; DNA-directed RNA polymerase; Nucleotidyltransferase; Plastid;
KW   Transcription; Transferase.
FT   CHAIN           1..1072
FT                   /note="DNA-directed RNA polymerase subunit beta"
FT                   /id="PRO_0000300439"
SQ   SEQUENCE   1072 AA;  120437 MW;  6461C9CB817B8739 CRC64;
     MLLDENKGTS TIPEFGKIQF EGFCRFIDQG LIEELQNFPK IEDTDQEIES QLFGNKYELA
     EPLIKERNAV YQSLTYSSEL YVPARLIQRN SRKIQKQTVL IGNLPLMNSQ GTFVVNGISR
     IVVNQILRSP GIYYSSEPDQ SGITLYTSTI ISDWGGRSKL EIDGKTRIWA RVSKKRKISI
     PILLSAMGSN LGEILDNVCY PKIFLSLLTE RQEQKEYLRS KKNAILEFYK KLYCVSGDLV
     FSESLCKELR KKFLQQRCEL GKIGRRNPNQ KLNLDIPENE IFSLPQDVLA AVDYSIRVKF
     GMGTLDDMDH LKNRRIRSVA DLLQNQFGLA LGRLENAVRR TIRRATKRKC LPTPNNLVTS
     TPLTTTFQDF FGSHPLSQFL DQTNPLTEIV HRRKLSYLGP GGLTGRTASS RIRDIHPSHY
     GRICPIETSE GMNAGLVASL AIRARIGHCG SLQSPFHKIS ERSEEEHMVY LSSGEDEYYR
     IATGNYLALN QGIREEQVTP ARYRQEFLAI AWEQIHFRSI FPFQYFSVGV SLIPFLEHND
     ANRALMGSNM QRQAVPLFQP EKCIVGTGLE GQAAPDSGSA AIATQGGRIT YIDAGKITSS
     VDGDTVGTEL VTYQRSNNNT CMHQKPRVRR GEYVKKGQIL ADGAATVGGE LSLGKNILVA
     HMPWEGYNFE DAILISERLV YEDIYTSFHI ERYGIVTCMT SQGPERITKE IPHLDAHLLR
     HLDGNGLVML GSWVETGDVL VGKLTPQPAE ESLRAPEGRL LQAIFGIQVS SARESCLRVP
     IGGRGRVIDV RWIHKEENFG DNAEVVHVYI FQKRKIQVGD KVAGRLGNKG IISKILPRQD
     MPYLQDGTSV DMVLNPLGVL SRMNVGQIFE CLPGLAGNLM NRHYRITPFD ERYEREASRK
     PVFPELYGAS EQTANPWVFE PNHPGKNRLI DGRTGDTLEQ PVTTGKAYMP KLIHQVDDKI
     HARSSGPYAL VTQQPLRGKS KRGGQRVGEM EVWALEGFGV AYILQEMLTL KSDHIGARHE
     VLGAIITGGP IPRPGTAPES FRLLVRELRS LAPELDHAII YENDFQIDRK EV