RPOB_PLAOC
ID RPOB_PLAOC Reviewed; 1070 AA.
AC Q09G54;
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 Platanus occidentalis (Sycamore) (American plane tree).
OG Plastid; Chloroplast.
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; Proteales; Platanaceae; Platanus.
OX NCBI_TaxID=4403;
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; DQ923116; ABI49770.1; -; Genomic_DNA.
DR RefSeq; YP_740557.1; NC_008335.1.
DR AlphaFoldDB; Q09G54; -.
DR SMR; Q09G54; -.
DR GeneID; 4271289; -.
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_0000300452"
SQ SEQUENCE 1070 AA; 120663 MW; 8F5B73B0FCB33BA6 CRC64;
MRRDGNEGMS TIPGFNQIQF EGFCRFIDQG LTEELYKFPK IEDTDQEIEF QLFVETYQLV
EPLIKERDAV YESLTYSSEV YVPAGLIWKP GRDMQEQTIF IGNIPLMNSL GTSIVNGIYR
IVINQILQSP GIYYRSESDH NGISVYTGTI ISDWGGRSEL EIDRKARIWA RVSRKQKISI
LVPSSAMGSN LREILDNVCY PEIFLSFLND KEKKKIGSKE NAILEFYQQF ACVGGDPVFS
ESLCKELQKK FFQQRCELGR IGRRNMNRRL NLDIPQNNTF LLPRDVLAAA DHLIGMKFGM
GTLDDMNHLK NKRIRSVADL LQDQFGLALI RLENVVRGTI CGAIKHKLIP TPQNLVTSTP
LTTTYESFFG LHPLSQVLDR TNPLTQMVHG RKLSYLGPGG LTGRTASFRI RDIHSSHYGR
ICPIDTSEGI NVGLIGSLAI YARIGHWGSL ESPFYEISDR SKEVQMLYLS PSRDEYYMVA
AGNSLALNQS IPEEQVVPAR YRQEFLTIAW EQVHFRSIFP FQYFSIGASL IPFIEHNDAN
RALMSSNMQR QAVPLSQSEK CIVGTGLERQ AALDSGVSTI AEHEGKIIYT DTDKIILLGN
GDTLSIPLVM YQRSNKNTCM YQKPQVRRGK FIKKGQIVAD GAATVGGELA LGKNVLVAYM
PWEGYNSEDA VLISERLVYG DIYTSFHIRK YEIQTHVTSQ GPERITNEIP HLEAHLLRNL
DRNGIVMLGS WVETGDILVG KLTPQMAKES SYAPEDRLLR AILGIQVSTS KETCLKLPIG
GRGRVIDVRW IQKKGGSSYN PETICVYISQ KREIKVGDKV AGRHGNKGII SKILPRQDMP
YLQDGTPIDM VFNPLGVPSR MNVGQIFECS LGLAGDLLDR HYRIAPFDER YEQEASRKLV
FSELYKASKQ TANPWVFEPE YPGKSRIFDG RTGDPFEQPV LIGKSYILKL IHQVDDKIHG
RSSGHYALVT QQPLRGRAKQ GGQRVGEMEV WALEGFGVAH ILQEMLTYKS DHIRARQEVL
GTTIVGGTIP SPEDAPESFR LLVRELRSLA LELNHFLVSE KNFQINRKEA