RPOB_SOLBU
ID RPOB_SOLBU Reviewed; 1070 AA.
AC Q2MIJ5;
DT 30-MAY-2006, integrated into UniProtKB/Swiss-Prot.
DT 07-FEB-2006, sequence version 1.
DT 03-AUG-2022, entry version 64.
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 Solanum bulbocastanum (Wild potato).
OG Plastid; Chloroplast.
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC asterids; lamiids; Solanales; Solanaceae; Solanoideae; Solaneae; Solanum.
OX NCBI_TaxID=147425;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. PT29;
RX PubMed=16575560; DOI=10.1007/s00122-006-0254-x;
RA Daniell H., Lee S.-B., Grevich J., Saski C., Quesada-Vargas T., Guda C.,
RA Tomkins J., Jansen R.K.;
RT "Complete chloroplast genome sequences of Solanum bulbocastanum, Solanum
RT lycopersicum and comparative analyses with other Solanaceae genomes.";
RL Theor. Appl. Genet. 112:1503-1518(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; DQ347958; ABC56205.1; -; Genomic_DNA.
DR RefSeq; YP_538840.1; NC_007943.1.
DR AlphaFoldDB; Q2MIJ5; -.
DR SMR; Q2MIJ5; -.
DR GeneID; 3989543; -.
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..1070
FT /note="DNA-directed RNA polymerase subunit beta"
FT /id="PRO_0000237329"
SQ SEQUENCE 1070 AA; 120572 MW; F77E7CF697EFFC8F CRC64;
MLGDGNEGIS TIPGFNQIQF EGFCRFIDQG LTEELYKFPK IEDTDQEIEF QLFVETYQLV
EPLIKERDAV YESLTYSSEL YVSAGLIWKN SRDMQEQTIF IGNIPLMNSL GTSIVNGIYR
IVINQILQSP GIYYRSELDH NGISVYTGTI ISDWGGRSEL EIDRKARIWA RVSRKQKISI
LVLSSAMGLN LREILENVCY PEIFLSFLND KERKKIGSKE NSILEFYQQF ACVGGDPVFS
ESLCKELQKK FFQQRCELGR IGRRNMNRKL NLDIPQNNTF LLPRDILAAA DHLIGLKFGM
GALDDMNHLK NKRIRSVADL LQDQFGLALV RLENVVRGTI CGAIRHKLIP TPQNLVTSPP
LTTTYESFFG LHPLSQVLDR TNPLTQIVHG RKLSYLGPGG LTGRTASFRI RDIHPSHYGR
ICPIDTSEGI NVGLIGSLSI HARIGHWGSL ESPFYEISER STGVRMLYLS PGSDEYYMVA
AGNSLALNRD IQEEQVVPAR YRQEFLTIAW EQVHLRSIFP FQYFSIGASL IPFIEHNDAN
RALMSSNMQR QAVPLSRSEK CIVGTGLERQ AALDSGALAI AEREGRIVYT NTDKILLAGN
GDILSIPLVI YQRSNKNTCM HQKLRVPRGK CIKKGQILAD GAATVGGELA LGKNVLVAYM
PWEGYNSEDA VLISERLVYE DIYTSFHIRK YEIHTHVTSQ GPEKVTNEIP HLEAHLLRNL
DKKGIVMLGS WVETGDILVG KLTPQVVKES SYAPEDRLLR AILGIQVSTS KETCLKLPIG
GRGRVIDVRW IQKRGGSSYN PETIRVYISQ KREIKVGDKV AGRHGNKGII SKILPRQDMP
YLQDGRSVDM VFNPLGVPSR MNVGQIFECS LGLAGSLLDR HYRIAPFDER YEQEASRKLV
FSELYEASKQ TANPWVFEPE YPGKSRIFDG RTGNPFEQPV IIGKPYILKL IHQVDDKIHG
RSSGHYALVT QQPLRGRAKQ GGQRVGEMEV WALEGFGVAH ILQEMLTYKS DHIRARQEVL
GTTIIGGTIP NPEDAPESFR LLVRELRSLA LELNHFLVSE KNFQINRKEA