ID   RPOB_IPOPU              Reviewed;        1067 AA.
AC   A7Y3B9;
DT   08-APR-2008, integrated into UniProtKB/Swiss-Prot.
DT   23-OCT-2007, sequence version 1.
DT   03-AUG-2022, entry version 55.
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   Ipomoea purpurea (Common morning glory) (Pharbitis purpurea).
OG   Plastid; Chloroplast.
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   asterids; lamiids; Solanales; Convolvulaceae; Ipomoeeae; Ipomoea.
OX   NCBI_TaxID=4121;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=17956636; DOI=10.1186/1471-2229-7-57;
RA   McNeal J.R., Kuehl J.V., Boore J.L., dePamphilis C.W.;
RT   "Complete plastid genome sequences suggest strong selection for retention
RT   of photosynthetic genes in the parasitic plant genus Cuscuta.";
RL   BMC Plant Biol. 7:57-57(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; EU118126; ABV02340.1; -; Genomic_DNA.
DR   RefSeq; YP_001468300.1; NC_009808.1.
DR   AlphaFoldDB; A7Y3B9; -.
DR   SMR; A7Y3B9; -.
DR   PRIDE; A7Y3B9; -.
DR   GeneID; 5601337; -.
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..1067
FT                   /note="DNA-directed RNA polymerase subunit beta"
FT                   /id="PRO_0000329200"
SQ   SEQUENCE   1067 AA;  120407 MW;  04C1A5D8BCF7CE55 CRC64;
     MEGGGMTTIP GFNQIQFEGF CRFIDQGLTE ELSKFPKIED IDQEIEFQLF VETYQLVEPL
     IKERDAVYDS LTYSSELYVS ARLIWKTSRD MQEQTIFIGS IPLMNSQGTS IVNGIYRIVI
     NQILQSPGIY YRSELDHNGI SVYTGTIISD WGGRSELEID RKARIWARVS RKQKISILVL
     SSAMGSNLRE ILENVCYPEI FLSFLSDKEK KKIGSKENAI LEFYQQFACV DGDPIFSESL
     WKELQKKFFQ QRCELGRIGR RNMNRRLNLD IPQNNTFLLP RDLLAAADHL IGLKFGMGTL
     DDMNHLQNKR IRSVADLLQD QFGLALVRLE NAVRGTICGA IRHKLIPTPQ NLVTSTPLTT
     TYESFFGLHP LSQVLDRTNP LTQIVHGRKF SSLGPGGLTG RTASFRIRDI HPSHYGRICP
     IDTSEGINVG LIGSLAIHAR IGHWGSLESP FYEISERSTG VRMLYLSPGR DEYYMVAAGN
     SLALNQDIQE DQVVPARYRQ EFLTIAWEQV HLRSIFPFQY FSIGASLIPF IEHNDANRAL
     MSSNMQRQAV PLSRSEKCIV GTGVERQAAL DSGALVIAER EGRVVYTDTD KILFSGDGET
     LSIPLVMYKR SNKNTCMHQK PQVQRGKCIK KGQILADGAA TVEGELALGK NVLVAYMPWE
     GYNSEDAVLI SERLVYEDIY TSFHIKKYEI QTHVTSQGPE KVTNEIPHLE AHFIRNLDKN
     GIVKQGSWVE TGDVLVGKLT PQVVKESSYA PEDRLLRAIL GIQVSTSKET CLKVPIGGRG
     RVIDVRWIQK KGGSSYNPEM IRVYILQKRE IKVGDKVAGR HGNKGIISKI LPRQDMPYLQ
     DGRSVDLVFN PLGVPSRMNL GQIFECSLGL AGSLLDRHYR IAPFDERYEQ EASRKVVFSE
     LYEASKQTAN PWAFEPEYPG KSRIFDGRTG NPFEQPVLIG KPYILKLIHQ VDDKIHGRSS
     GHYALVTQQP LRGRAKQGGQ RVGEMEVWAL EGFGVAHILQ EMLTYKSDHI RARQEVLGTT
     IVGGTIPNPK DAPESFRLLV RELRSLALEL NHFLVSEKNF QIHRKEA