RPOB_AMBTC
ID RPOB_AMBTC Reviewed; 1072 AA.
AC P60282;
DT 16-JAN-2004, integrated into UniProtKB/Swiss-Prot.
DT 11-SEP-2007, sequence version 2.
DT 03-AUG-2022, entry version 86.
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 Amborella trichopoda.
OG Plastid; Chloroplast.
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; Amborellales; Amborellaceae; Amborella.
OX NCBI_TaxID=13333;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=12832641; DOI=10.1093/molbev/msg159;
RA Goremykin V.V., Hirsch-Ernst K.I., Wolfl S., Hellwig F.H.;
RT "Analysis of the Amborella trichopoda chloroplast genome sequence suggests
RT that Amborella is not a basal angiosperm.";
RL Mol. Biol. Evol. 20:1499-1505(2003).
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=CAD45099.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AJ506156; CAD45099.1; ALT_INIT; Genomic_DNA.
DR RefSeq; NP_904091.2; NC_005086.1.
DR AlphaFoldDB; P60282; -.
DR SMR; P60282; -.
DR STRING; 13333.ERM98365; -.
DR GeneID; 2546588; -.
DR KEGG; atr:2546588; -.
DR eggNOG; KOG0214; Eukaryota.
DR OrthoDB; 944344at2759; -.
DR Proteomes; UP000017836; Chloroplast.
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 Reference proteome; Transcription; Transferase.
FT CHAIN 1..1072
FT /note="DNA-directed RNA polymerase subunit beta"
FT /id="PRO_0000048009"
SQ SEQUENCE 1072 AA; 120930 MW; 1DA229C8364DCADB CRC64;
MLRDGNEGMS TIPGFSQIQF EGFCRFVDQG LAEELHKFPK IEDTDQEIEF QLLVETYQLA
EPLIKERDAV YESLTHSSEL YVPAGLIWKV GRDMQEQTVF IGNIPLMNSL GTFIVNGIYR
IVINQILQSP GIYYSSELDH NGISVYTGTI ISDRGGRSEL EIDRKARIWA RVSRKQKISI
LVLPSAMGSN LREILDNVCY PEILLYFPNE KEKKKIGSKE NAILEFYQQF SCVGGDPVFS
ESLCKELQKR FFQQRCELGR IGRQNMNQRL NIDIPQNNTF LLPRDVLAAT DHLIGMKFGM
GTLDDMNHLK NKRIRSVADL LQDQFGLALV RLENVVRGTI CGAIRHKFIP TPQNLVTSTP
LTTTYESFFG LHPLSQVLDR TNPLTQIVHG RKSSYLGPGG LTGRTASFRI RDIHPSHYGR
ICPIDTSEGI NVGLIGSLAI HARIGDWGSI RSPFYEISER SKEEQMVYLS PRRDEYYMVM
VAAGNSLALN QDIQDEQVVP ARYRQEFVTI AWEHIDLRSI YPLQYFSIGA SLIPFIEHND
ANRALMSSNM QRQAVPLSRS EKCIVGTGLE RQAALDSGGS AIAQHEGKVI YTDTEKILLS
GNGDTISIPL LMYQRSNKNT CMHQKPQVHR DKYVKKGQVL ADGAATVGGE LALGKNVLVA
HMPWEGYNFE DAVLISERLV YGDIYTSFHI RKYEIQTHVT SHGPEKITNE IPHLEAHLLR
NLDRNGIVML GSWVETGDVL VGKLTPQTAK ESSYAPEDRL LRVILGIQVS TAKETCLKLP
IGGRGRVIDV RWIQKKGASS YNPEKIRVYI SQKREIKVGD KVAGRHGNKG IISKILPRQD
MPYLQDGTPV DMVFNPLGVP SRMNVGQIFE CSLGLAGDLL DRHYRITPFD ERYEQEASRK
LVFPELYEAS KRTANPWVFE PEYPGKSRIF DGRTGDPFEQ PVIIGKSYML KLIHQVDDKI
HGRSSGHYAL VTQQPLRGRA KQGGQRVGEM EVWALEGFGV AHILQEMLTY KSDHIRARQE
LLGTTIVGGT IPKPEGAPES FRLLVRELRS LALELKHFLV SEKNFQINRK EA