RPOB_SILLA
ID RPOB_SILLA Reviewed; 1070 AA.
AC Q589C0;
DT 21-JUN-2005, integrated into UniProtKB/Swiss-Prot.
DT 10-MAY-2005, sequence version 1.
DT 03-AUG-2022, entry version 70.
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 Silene latifolia (White campion) (Bladder campion).
OG Plastid; Chloroplast.
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC Caryophyllales; Caryophyllaceae; Sileneae; Silene;
OC Silene subgen. Behenantha; Silene sect. Melandrium.
OX NCBI_TaxID=37657;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA Kejnovsky E., Kubat Z., Hobza R., Lengerova M., Sato S., Tabata S.,
RA Fukui K., Matsunaga S., Vyskot B.;
RT "A partial chloroplast genome of Silene latifolia.";
RL Submitted (AUG-2004) 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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AB189069; BAD93457.1; -; Genomic_DNA.
DR AlphaFoldDB; Q589C0; -.
DR SMR; Q589C0; -.
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_0000048047"
SQ SEQUENCE 1070 AA; 120652 MW; FE291F0C11E603D7 CRC64;
MLREGNELMS TIPGFNQIQF EGFCQFIDQG LPEELYKFPK IEDTDQEIEF QLFVETYQLV
EPVIKEKDAV YKSLTYSSEL YVSAGLIWKT GREIQEQTIL IGNIPLMNSL GTFLVNGIYR
IVINQILQSP GIYYRSELDH NGISVYTGTI ISDWGGRSEL EIDRKARIWA RVSRKQKISI
LVLSSAMGSN LKEILDNVCY PEIFLSFLND KDKKNFGSKE NAILEFYQQF ACVGGDPVFS
ESLCKELQKK FFQQKCELGR IGRRNMNRRL NLDIPQNNTF LLPRDILAAT DHLIGMKFGM
GTLDDMNHLK NKRIRSVADL LQDQFGLALV RLENVVRGTI CGAIRHKLIP TPQNLVTSTP
LTTTYESFFG LHPLSQVLDR TNPLTQIVHG RKLSYLGPGG LTGRTASFRI RDIHPSHYGR
ICPIDTSEGI NVGLIGSLAI HARIGLLGSL ESPFYKISER SAMVQMLFLS PSIDEYYMVS
TGNSLALNQG IQEEQVVPAR YRQEFLTIAW EQVHLRSIFP FQYFSIGASL IPFIEHNDAN
RALMSSNMQR QAVPLSQSEK CIVGTGLERQ AALDSGILAI AEHEGKILYT DTDKIIFSGN
GDIQSIPLVM YQRSNKNTCM HQNPRIPRGK CIKKGQILAD GAATVGGELA LGKNILVAYM
PWEGYNFEDA VLISERLVYE DIYTSFHIRK YDIQTYVTSQ GPERVTSEIP HLEAHLLRNL
DKNGIVRLGS WVETGDILVG KLTPQMAKES SYAPEDRLLR AILGIQVSTS KETCLKLPIG
GRGRVIDVRW IQKKGGSSYN PETIHVYILQ KREIKVGDKV AGRHGNKGII SKILPRQDMP
YLQDGRPVDM VFNPLGVPSR MNVGQIFECS LGLAGGLLDR HYRIAPFDER YEQEASRKLV
FSELYQASKQ TSEPWIFEPE YPGKSRIFDG RTGDLFEQPV IIGNPYILKL IHQVDDKIHG
RSSGHYALVT QQPLRGRAKQ GGQRVGEMEV WALEGFGVAH ILQEMLTYKS DHIKARQDVL
GTTIIGGTIP NPEDAPESFR LLIRELRSLA LELNHFLVSE KTFQINRMEA