RPOB_DRIGR
ID RPOB_DRIGR Reviewed; 1071 AA.
AC Q06H05;
DT 06-FEB-2007, integrated into UniProtKB/Swiss-Prot.
DT 31-OCT-2006, sequence version 1.
DT 03-AUG-2022, entry version 60.
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 Drimys granadensis.
OG Plastid; Chloroplast.
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; Magnoliidae; Canellales; Winteraceae; Drimys.
OX NCBI_TaxID=224735;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=17020608; DOI=10.1186/1471-2148-6-77;
RA Cai Z., Penaflor C., Kuehl J.V., Leebens-Mack J., Carlson J.E.,
RA dePamphilis C.W., Boore J.L., Jansen R.K.;
RT "Complete plastid genome sequences of Drimys, Liriodendron, and Piper:
RT implications for the phylogenetic relationships of magnoliids.";
RL BMC Evol. Biol. 6:77-77(2006).
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; DQ887676; ABH88289.1; -; Genomic_DNA.
DR RefSeq; YP_784378.1; NC_008456.1.
DR AlphaFoldDB; Q06H05; -.
DR SMR; Q06H05; -.
DR GeneID; 4363553; -.
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..1071
FT /note="DNA-directed RNA polymerase subunit beta"
FT /id="PRO_0000276587"
SQ SEQUENCE 1071 AA; 120597 MW; 91419F808F6A1FB4 CRC64;
MLRDGNEGMF TIPGFSQIQF EGFFRFIDQG LTEELHKFPK IEDTDQEIEF QLFVDTYRLV
EPLIKERDAV YESLTYSSEL YVPAGLIWKT GRDMQEQTIF IGNIPLMNSL GTSIVNGIYR
IVINQILQSP GIYYRSELDH NGISVYTGSI ISDWGGRSEL EIDRKARIWA RVSRKQKISI
LVPSSAMGSN LREILDNVCY PEIFLSFPNE KEKKKIGSRE NAILEFYQQF ACVGGDPVFS
ESLCKELQKK FFQQRCELGR IGRRNMNWRL NLDIPQNNLF LLPRDVLAAA DHLIGMKFGM
GTLDDMNHLK NKRIRSVADL LQDQFGLALV RLENVVRGTI CGAIRHKLIP TPHNLVTSTP
LTTTYESFFG LHPLSQVLDR TNPLTQIVHG RKSSYLGPGG LTGRTASFRI RDIHPSHYGR
ICPIDTSEGI NVGLIGSLAI HARIGYLGSI ESPFYEISQR SKEVQTVYLS PNRDEYYMVA
AGNSLALNQG IQEEQVVPAR YRQEFLTIAW EQIHLRSIFP FQYFSIGASL IPFIEHNDAN
RALMSSNMQR QAVPLSRSEK CIVGTGLERQ AALDSGVSAI AEQDGKIIYT DTDKIVLSGN
GDTAISIPLV IYQRSNKNTC MHQKPQVPRG KCLKKGQILA DGAATVGGEL ALGKNVLVSY
MPWEGYNFED AVLISERLVY GDIYTSFHIR KYEIQTHVTS QGPERITNEI PHLEAHLLRN
LDINGIVMLG SWIETGDILV GKLTPQTAKE SSYAPEDRLL RAILGIQVST AKETCLKLPI
GGRGRVIDVR WIQKGGGSSY NPEMIRVYIS QKREIKVGDK VAGRHGNKGI ISKILPRQDM
PYLQDGTPVD MVFNPLGVPS RMNVGQIFEC SLGLAGDLLD RHYRIAPFDE RYEQEASRKL
VFPELYEASK QTANPWVFEP EYPGKSRIFD GRTGDPFEQP VIIGKSYILK LIHQVDDKIH
GRSSGHYALV TQQPLRGRAK QGGQRVGEME VWALEGFGVA HISQEMLTYK SDHIRARQEV
LGTTIIGGTI PNPEDAPESF RLLVRELRSL ALELNHFLVS EKNFQIHRKE A