RPOB_JASNU
ID RPOB_JASNU Reviewed; 1064 AA.
AC Q06RD9;
DT 06-FEB-2007, integrated into UniProtKB/Swiss-Prot.
DT 31-OCT-2006, sequence version 1.
DT 03-AUG-2022, entry version 57.
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}; ORFNames=JNC0253;
OS Jasminum nudiflorum (Winter jasmine).
OG Plastid; Chloroplast.
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC asterids; lamiids; Lamiales; Oleaceae; Jasmineae; Jasminum.
OX NCBI_TaxID=126431;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=17329229; DOI=10.1093/molbev/msm036;
RA Lee H.-L., Jansen R.K., Chumley T.W., Kim K.-J.;
RT "Gene relocations within chloroplast genomes of Jasminum and Menodora
RT (Oleaceae) are due to multiple, overlapping inversions.";
RL Mol. Biol. Evol. 24:1161-1180(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; DQ673255; ABG74620.1; -; Genomic_DNA.
DR RefSeq; YP_778482.1; NC_008407.1.
DR AlphaFoldDB; Q06RD9; -.
DR SMR; Q06RD9; -.
DR PRIDE; Q06RD9; -.
DR GeneID; 4319744; -.
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; -; 2.
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..1064
FT /note="DNA-directed RNA polymerase subunit beta"
FT /id="PRO_0000276590"
SQ SEQUENCE 1064 AA; 120285 MW; D99D39D1585ED013 CRC64;
MLGDGNEGMS TIPGLNQIQF EGFCRFIDQG LTEELSKFPK IEDTDQEIEF QLFMERYQLV
EPLRKERDAV YESLTYSSEF YVSAGLIWKT SRDMQEQTIL IGNIPLMNSL GTSIVKGIYR
IVINQILQSP GIYYRSELDH NEISVYTGTI ISDWGGRSEL EIDRKARIWA RVSRKQKISI
LVLSSAMGSN LKEILDNVFY PEIFLSFLKD KERKKIGSKE NAILEFYQQF ACVGGDPVFS
ESLCKELQTK FFQQRCELGR IGRRNMNRRL NLDIPQNNTF LLPRDILAAA DHLIEQKFGM
GTLDDMNHLK NKRIRSVADL LQDQLGLALV RLEDEVRETI CGPIRHKWRT TPHPQNLVTS
TPLTTTYESF FGSHPLSQVL DQTNPLTQIV HGRKWSYLDP GGLTGRTASF RIRDIHPSHY
GRICPIDTSE GINVGLIGSL AIHAKIGHWG SLESPFYEIS ERSTGVQMLY LSPGRDEYYT
VAAGNSLALN QDIQEEEVVP ARYRQEFLTI AWEQVHFRSI LPFQYFSIGA SLIPFIEHND
ANRALMSSNM QRQAVPLSRP EKCIVGTGLE RQVALDSGAL AIAEREGKIV STDTEKILFS
GNGDTLSIPL VMYQSSNKNT CMHQKPQVQR GKCIKKGQIL ADGAATVGGE LALGKNVLVA
YMPWEGYNSE DAVLISERLV YEDIYTSFHI RKYEIQTAGT ERITNEIPHL EAHLLRNLDK
NGIVMLGSWV ETGAILVGKL TPEVVKESPA NRLVYDIVGI QVSTSKDTCL KLPIGGRGRV
IDVRWIQKRG DNDNPETIRI YISQKREIKV GDKVAGRHGN KGIISKILPR QDMPYLQDGR
PVDMVFNPLG VPSRMNVGQI FECSLGLAGG LLDRHYRIVP FDERYEQEAS RKLVFSELYE
ASKQTTNPWV FEPEYPGKSR IFDGRSGNPF EQPILIGKPY ILKLIHQVDD KIHGRSVGNY
THITQQPLRG RAKGGGQRVG EMEVWALEGF GVAHILQEML TYKSDHIRAR QKIPGTTMIG
GTIPNPEDAP ESFRVLVREL RSLALELNHF LVSEKNFQIN RKEA