RPOB_POPAL
ID RPOB_POPAL Reviewed; 1070 AA.
AC Q14FG5;
DT 06-FEB-2007, integrated into UniProtKB/Swiss-Prot.
DT 22-AUG-2006, sequence version 1.
DT 03-AUG-2022, entry version 65.
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 Populus alba (White poplar).
OG Plastid; Chloroplast.
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; fabids; Malpighiales; Salicaceae; Saliceae; Populus.
OX NCBI_TaxID=43335;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Okumura S., Yamashita A., Kanamoto H., Hattori M., Takase H., Tomizawa K.;
RT "Complete structure of the chloroplast genome of Populus alba.";
RL Submitted (MAR-2005) to the EMBL/GenBank/DDBJ databases.
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; AP008956; BAE97197.1; -; Genomic_DNA.
DR RefSeq; YP_665550.1; NC_008235.1.
DR AlphaFoldDB; Q14FG5; -.
DR SMR; Q14FG5; -.
DR GeneID; 4178254; -.
DR KEGG; palz:4178254; -.
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_0000276596"
SQ SEQUENCE 1070 AA; 120521 MW; 16F79B3FA3C3E548 CRC64;
MLGDGNGGMS TIPGFNQIQF EGFCRFIDQG LAEELYKFPK IEDRDQEIEF QLFVETYQLV
EPSIKERDAV YESLTYSSEL YVSGGLIWKN SRDMQEQTIF IGNIPLMNSL GTSIVNGIYR
IVINQILQSP GIYYRSELNH NGISVYTGTI ISDWGGRVEL EIDKKARIWA RVSRKQKISI
LVLSSAMGLN LREILENVCY PEIFLSFLSD KEKKKIGSRE NAILEFYQQF TCVGGGPVFS
ESLCKELQKK FFQQRCELGR IGRLNMNQRL NLDIPHNNTF LLPRDILAAA DHLIGMKFGM
GTLDDMNHLK NKRIRSVADL LQDQFGLALI RLENVVRGTI CGAIRHKLIP TPQNLVTSTP
LTTTYESFFG LHPLSQVLDR TNPLTQIVHG RKSSYLGPGG LTGRTASFRI RDIHPSHYGR
ICPIDTSEGI NVGLIGSLTI HAKIGHLGSL ESPFYEISAR SKKVRMLYLS PNRDEYYMIA
AGNCLALNRG AREEQVVPAR YRQEFLTIAW EQVRLRSFFP FQYFSIGASL IPFIEHNDAN
RALMSSNMQR QAVPLARSEK CIVGTGLERQ VALDSGVPAI AEHEGKIIYT DIDKIILSGN
GYTVSIPLVM YQRSNKNTCM HQKTQVQRGK CIKRGQVLAD GAATVGGELA LGKNILVAYM
PWEGYNFEDA VLISERLVYE DVYTSFHIRK YEIQTHVTSQ GPERITNEIP HLEAHLLRNL
DKNGIVMLGS WVETGDILIG KLTPQLAKES SYAPEDRLLR AILGIQVSTS KETCLKLPTG
GRGRVIDVRW IQKKGGSSYN PETIRVYILQ KREIKVGDKV AGRHGNKGII SKILPRQDMP
YLQDGGPVDM VFNPLGVPSR MNVGQIFECS LGLAGSLLAR HYRVAPFDER YEQEASRKLV
FSELYEAGKQ TANPWVFEPE CPGKSRIFDG RTGDPFEQPV IIGKPYILKL IHQVADKIHG
RSSGHYALVT QQPLRGRAKQ GGQRVGEMEV WALEGFGVSH ILQEMLTYKS DHIRARQEVL
GTTISGRTIP KPEDAPESFR LLVRELRSLA LELKHFLISE KNFQINRKEV