ID   RPOB_EUCGG              Reviewed;        1072 AA.
AC   Q49L06;
DT   21-FEB-2006, integrated into UniProtKB/Swiss-Prot.
DT   13-SEP-2005, sequence version 1.
DT   03-AUG-2022, entry version 66.
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   Eucalyptus globulus subsp. globulus (Tasmanian blue gum).
OG   Plastid; Chloroplast.
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   rosids; malvids; Myrtales; Myrtaceae; Myrtoideae; Eucalypteae; Eucalyptus.
OX   NCBI_TaxID=71271;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=16303753; DOI=10.1093/dnares/dsi006;
RA   Steane D.A.;
RT   "Complete nucleotide sequence of the chloroplast genome from the Tasmanian
RT   blue gum, Eucalyptus globulus (Myrtaceae).";
RL   DNA Res. 12:215-220(2005).
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; AY780259; AAX21021.1; -; Genomic_DNA.
DR   RefSeq; YP_636291.1; NC_008115.1.
DR   AlphaFoldDB; Q49L06; -.
DR   SMR; Q49L06; -.
DR   GeneID; 4108362; -.
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..1072
FT                   /note="DNA-directed RNA polymerase subunit beta"
FT                   /id="PRO_0000224128"
SQ   SEQUENCE   1072 AA;  120816 MW;  2A5AFBD4DCE1C8BE CRC64;
     MLGDGNEGMS TIPGFNQIQF EGFCRFIDQG LTEELIKFPK IEDTDQEIEF QLFVETYQLV
     EPLIKERDAV YESLTYSSEL YVSAGLIWKT SRDMQEQTLF IGNIPLMNSL GTSIVNGIYR
     IVINQILQSP GIYYRSELDH NGISVYTGTI ISDWGGRLEL EIDRKARIWA RVSRKQKISI
     LVLSSAMGSN LREILENVCY PEIFLSFLND KEKKKIGSKE NAILEFYQQF ACVGGDPVFS
     ESLCKELQKK FFQQRCELGR IGRRNMNRRL NLDIPQNNTF LLPRDILAAA DHLIGMKFGM
     GTLDDMNHLK NKRIRSVADL LQDQFGLALV RLENVVKGTI CGAIRHKLIP TPQNLVTSTP
     LTTTYESFFG LHPLSQVLDR TNPLTQIVHG RKLSYLGPGG LTGRTASFRI RDIHPSHYGR
     ICPIDTSEGI NVGLIGSLAI HARIGQGGSL ESPFYEISER SKSKKVRMLY LSPSRDEYYM
     IAAGNSLALN QRIQEEQVVP ARYRQEFLTI AWEQVNLRSI FPFQYFSIGA SLIPFIEHND
     ANRALMSSNM QRQAVPLSRS EKCIVGTGLE RQAALDSGVT AIAEHEGKII YTNTDKIILL
     GNGDTLSIPL VMYQRSNKNT CMHQKPQVPR GKCIKKGQIL ADGAATVGGE LALGKNVLVA
     YLPWEGYNFE DAVLISERLV YEDIYTSFHI RKYEIQTHVT SQGPERITNE IPHLEAHLLR
     NLDKNGIVML GSWVEAGDVL VGKLTPQTAK ESSYAPEDRL LRAILGIQVS TSKETCLKLP
     IGGRGRVIDV RWIQKKGGSN YNPETICVYI LQKREIKVGD KVAGRHGNKG IISKILPRQD
     MPYLQDGRPV DMVFNPLGVP SRMNVGQIFE CSLGLAGDLL DRHYRIAPFD ERYEQEASRK
     LVFSELYEAS QQTANPWVFE PEYPGKSRIF DGRTGDPFEQ PVIIGKPYIL KLIHQVDDKI
     HGRSSGHYAL VTQQPLRGRA KQGGQRVGEM EVWALEGFGV AHILQEMLTY KSDHIRARQE
     VLGTTIIGGT IPKPKDAPES FRLLVRELRS LSLELNHFLV SEKNFQINRK EA