RPOB_NANDO
ID RPOB_NANDO Reviewed; 1070 AA.
AC Q09FW9;
DT 11-SEP-2007, integrated into UniProtKB/Swiss-Prot.
DT 17-OCT-2006, sequence version 1.
DT 03-AUG-2022, entry version 62.
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 Nandina domestica (Heavenly bamboo).
OG Plastid; Chloroplast.
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; Ranunculales; Berberidaceae; Nandinoideae;
OC Nandina.
OX NCBI_TaxID=41776;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16934154; DOI=10.1186/1471-2229-6-17;
RA Moore M.J., Dhingra A., Soltis P.S., Shaw R., Farmerie W.G., Folta K.M.,
RA Soltis D.E.;
RT "Rapid and accurate pyrosequencing of angiosperm plastid genomes.";
RL BMC Plant Biol. 6:17-17(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; DQ923117; ABI49855.1; -; Genomic_DNA.
DR RefSeq; YP_740642.1; NC_008336.1.
DR AlphaFoldDB; Q09FW9; -.
DR SMR; Q09FW9; -.
DR PRIDE; Q09FW9; -.
DR GeneID; 4271572; -.
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..1070
FT /note="DNA-directed RNA polymerase subunit beta"
FT /id="PRO_0000300448"
SQ SEQUENCE 1070 AA; 120216 MW; D35601DF7BBA7B0F CRC64;
MLRDANEGMS TIPGFSQIQF EGFCRFIDRG LMEELNKFPK IEDTDQEIEF QLFVETYQLV
EPLIKERDAV HESLTYCSEL YVPAGLIWKT GKDIQEQTIF IGNIPLMNSL GTSIVNGIYR
IVINQILQSP GIYYRSELDH NGISVYTGTI ISDWGGRSEL EIDRKARIWA RVSRKQKISI
LVPSSAMGSN LKEIIDNVCY PEIFLSFPND KEKKKIGSKE NAILEFYQQF ACVGGDPVFS
ESLCKELQKK FFQQRCELGR IGRRNMNRRL NLDIPHNITF LLPRDVLAAA DHLIGMKFGM
GTLDDMNHLK NKRIRSVADL LQDQFGLAMV RLENAVRGTI GGAIRQKLIP TPHNLVTSTP
LTTTYESFFG LHPLSQVLDR TNPLTQIVHG RKSSYLGPGG LTGRTASFRI RDIHPSHYGR
ICPIDTSEGI NVGLIGSLAI HARIGHWGSL ERPFYEISER SKGVRVIYLS PSIDEYYMVT
AGNSLALNHG IQEEQVVPAR YRQEFLTIAW EQIQLRSIFP FQYFSVGASL IPFIEHNDAN
RALMSSNMQR QAVPLSRSEK CIVGTGLERQ AALDSGVSAI AEHEGKIIYT DTDKIILSGN
GATLSIPLVM YQRSNKNTCM HQKPQVSRGK CIKKGQILAD GAATVGGELA LGKNVLVAYM
PWEGYNFEDA VLISERLVYG DIYTSFHIRK YEIQTHVTSQ GPERITNEIP HLEAHLLRNL
DRNGIVMLGS WVETGDILVG KLTPQVAKES SYAPEDRLLR AILGIQVSTA KETCLKLPIG
GRGRVIDVRW IHKKGGSSYN PETIRVYISQ KREIKVGDKV AGRHGNKGII SKILPRQDMP
YLQDGTPVDM VFNPLGVPSR MNVGQIFECS LGLAGGLLDR HYRIAPFDER YEQEASRKLV
FSELYEASKQ TANPWVFEPE YPGKSRIFDG RTGDPFAQPV IIGKSYILKL IHQVDDKIHG
RSSGHYALVT QQPLRGRAKQ GGQRVGEMEV WALEGFGVAH ILQEMLTYKS DHIRARQEVL
GTTIIGGTIP NPEDAPESFR LLVRELRSLA LELNHFLVSE KNFQINRKEA