RPOB_CERDE
ID RPOB_CERDE Reviewed; 1070 AA.
AC A8SE86;
DT 08-APR-2008, integrated into UniProtKB/Swiss-Prot.
DT 15-JAN-2008, sequence version 1.
DT 03-AUG-2022, entry version 54.
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 Ceratophyllum demersum (Rigid hornwort) (Coontail).
OG Plastid; Chloroplast.
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; Ceratophyllales; Ceratophyllaceae;
OC Ceratophyllum.
OX NCBI_TaxID=4428;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=18048334; DOI=10.1073/pnas.0708072104;
RA Moore M.J., Bell C.D., Soltis P.S., Soltis D.E.;
RT "Using plastid genome-scale data to resolve enigmatic relationships among
RT basal angiosperms.";
RL Proc. Natl. Acad. Sci. U.S.A. 104:19363-19368(2007).
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; EF614270; ABQ81442.1; -; Genomic_DNA.
DR RefSeq; YP_001542439.1; NC_009962.1.
DR AlphaFoldDB; A8SE86; -.
DR SMR; A8SE86; -.
DR GeneID; 5729428; -.
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_0000329198"
SQ SEQUENCE 1070 AA; 120554 MW; 80AB8769A647239E CRC64;
MLRDRNEGMS TIPGFSQIQF EGFCRFLDQG LTEELHKFPK IEDTDQEIEF QLFVETYQLA
EPLIKEKDAI YESLTYSSEL YVPAGLIWKN GRDMQEQTVF IGNIPLMNSL GTSIVNGIYR
IVINQILQSP GIYYRSELDH NGISVYTGTI ISDWGGRSEL EIDRKARIWA RVSRKQKISI
LVLSSAMGSN LREILDNVCY PEIFLSFLND KDRKKIGSKE NAILEFYQQF ACVGGDPVFS
ESLCKELQKK FFQQRCELGR IGRRNMNQRL NLNIPQNNTF LLPRDVLAAA DHLIGMKFGM
GTLDDMNHLK NKRIRSVADL LQDQFGLALV RLENAIRGTI SGAIKHKLIP TPQNLVTSTP
LTTTFESFFG LHPLSQVLDR TNPLTQIVHG RKSSYLGPGG VTGRTASFRI RDIHPSHYGR
ICPIDTSEGI NVGLIGSLAI HAKIGFWGSI ETPFYEISEK SKEAQIVYLP PSRDEYSMVA
AGNSLALNRG IQEEQVVPAR YRQEFLTIAW EKIHLRSIFP FQYFSIGASL IPFIEHNDAN
RALMSSNMQR QAVPLFRSEK CIVGTGLERQ VALDSGVSAI AEHEGKILYT DTDKIVLSAN
GDTISIPLVM YQRSNKNTCM HQKPQVQRNK CIKKGQILAD GAATVGGELA LGKNVLVAYM
PWEGYNSEDA VLISERMVYE DIFTSFHIRK YEIQTHVTSQ GPERITNEIP HLEAHLLRNL
DRNGIVRLGS WIETGDILVG KLTPQTAKES SYAPEDRLLR AILGVQVSTA KETCLKLPIG
GRGRVIDVRW IQKKGGSSYN PETIRVYISQ KREIKVGDKV AGRHGNKGII SKILARQDMP
YLQDGTPIDM VFNPLGVPSR MNVGQIFECS LGLAGDLLDR HYRIAPFDER YEQEASRKLV
FPELYEASKQ TSNPWVFEPE YPGKSRIFDG RTGDPFEQPV IIGKSYILKL IHQVDDKIHG
RSSGHYALVT QQPLRGRAKQ GGQRVGEMEV WALEGFGVAH ISQEMLTYKS DHIRARQEVL
GTTIIGGTIP NPEDAPESFR LLVRELRSLA LELNHFLISD KNFQINRKEA