RPOB_PHAAO
ID RPOB_PHAAO Reviewed; 1070 AA.
AC Q3BAP8;
DT 21-FEB-2006, integrated into UniProtKB/Swiss-Prot.
DT 11-SEP-2007, sequence version 2.
DT 03-AUG-2022, entry version 71.
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 Phalaenopsis aphrodite subsp. formosana (Moth orchid).
OG Plastid; Chloroplast.
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; Liliopsida; Asparagales; Orchidaceae;
OC Epidendroideae; Vandeae; Aeridinae; Phalaenopsis.
OX NCBI_TaxID=308872;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Taisugar TS-97;
RX PubMed=16207935; DOI=10.1093/molbev/msj029;
RA Chang C.-C., Lin H.-C., Lin I.-P., Chow T.-Y., Chen H.-H., Chen W.-H.,
RA Cheng C.-H., Lin C.-Y., Liu S.-M., Chang C.-C., Chaw S.-M.;
RT "The chloroplast genome of Phalaenopsis aphrodite (Orchidaceae):
RT comparative analysis of evolutionary rate with that of grasses and its
RT phylogenetic implications.";
RL Mol. Biol. Evol. 23:279-291(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}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAW82495.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AY916449; AAW82495.1; ALT_INIT; Genomic_DNA.
DR RefSeq; YP_358570.2; NC_007499.1.
DR AlphaFoldDB; Q3BAP8; -.
DR SMR; Q3BAP8; -.
DR GeneID; 3741670; -.
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_0000224131"
SQ SEQUENCE 1070 AA; 120926 MW; AF8E0071651AF194 CRC64;
MLQNGNEGMS TIPGFSQIQF EGFCRFINQG LTEEFHKFQK IEDRDQEIEF QLFVETYQLV
EPLITERDAV YESLTYSSEL YVPAVLIWKT GRNMQEQTVF IGNIPIMNSF GTSIVNGIYR
IVINQIVQSP GIYYRSELEH NGVSVYTSTI ISDWGGRSEL EIDRKARIWA RVSRKQKISI
LVLSSAMGSN IREILDNVCY PEIFLSFPND KEKKKIGSKE NAILEFYQQF ACVGGDPVFS
ESLCKELQKK FFQQRCELGK IGRQNLNRRL NLDIPQNNTF LLPRDLLAAV DHLIGMKLGM
GTLDDMSHLK NKRIRSVADL LQDQFGLALV RLENTVRGTI CGAIRHKLIP TPQNLVTSTS
LTTTYESFFG LHPLSQVLDR TNPLTQIVHG RKWSYLGPGG LTGRTASFRI RDIHPSHYGR
ICPIDTSEGI NVGLMGSLAI HVKVGYWGSI ESPFYGLSER SKEAQMVYLS PNRDEYYMVA
AGNSLALNRD IQEQQVVPAR YRQEFLTIAW EEIHLRSIFP FQYFSIGASL IPFIEHNDAN
RALMSSNMQR QAVPLSRSEK CIVGTGLEGQ TALDSGVSVI AECKGKIIYT DTQKIFLSSN
GDTLSIPLVM YQRSNKNTCM NQKTQVQRGK YIKKGQILAG GAATAGGELA LGKNVLVAYM
PWEGYNFEDA VLISERLVYK DIYTSFHIRK YEIQTHVTSQ GPERITKEIP HLEARLLRNL
DRNGIVMLGS WIETGDILVG KLTPQTASES SYAPEDRLLR AILGIQVSTS KETSLRLPIG
GRGRVIDVRW IHRRGVSNSN PERIRVYISQ KREIKVGDKV AGRHGNKGII SKILSRQDMP
YLQDGTPVDM VFNPLGVPSR MNVGQIFECS LGLAGDLLKK HYRIGPFDER YEQEASRKLV
FSELYEASKK TKNPWVFEPE YPGKSRIFDG RTGDLFEQPV LIGKSYILKL IHQVDDKIHG
RSSGHYALVT QQPLRGRAKQ GGQRVGEMEV WALEGFGVAH ILQEMLTYKS DHIRARQEVL
GAMIIGATVP NPESAPESFR LLVRELRSLS LELNHFLVSE KNFQMDRKEA