RPOB_AETCO
ID RPOB_AETCO Reviewed; 1073 AA.
AC A4QJA7;
DT 11-SEP-2007, integrated into UniProtKB/Swiss-Prot.
DT 15-MAY-2007, sequence version 1.
DT 03-AUG-2022, entry version 56.
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 Aethionema cordifolium (Lebanon stonecress).
OG Plastid; Chloroplast.
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; malvids; Brassicales; Brassicaceae; Aethionemeae; Aethionema.
OX NCBI_TaxID=434059;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Hosouchi T., Tsuruoka H., Kotani H.;
RT "Sequencing analysis of Aethionema coridifolium chloroplast DNA.";
RL Submitted (MAR-2007) 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}.
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DR EMBL; AP009366; BAF49762.1; -; Genomic_DNA.
DR RefSeq; YP_001122938.1; NC_009265.1.
DR AlphaFoldDB; A4QJA7; -.
DR SMR; A4QJA7; -.
DR PRIDE; A4QJA7; -.
DR GeneID; 4968618; -.
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..1073
FT /note="DNA-directed RNA polymerase subunit beta"
FT /id="PRO_0000300429"
SQ SEQUENCE 1073 AA; 121115 MW; B54A6E71CAF90913 CRC64;
MLGDGKEGTS TIPGFNQIQF EGFYRFIDQG LIEEVSKFPK IEDIDQEIEF QLFVETYQLV
EPLIKERDAV YESLTYSSEL YVSAGLIWKT SRNMQEQRIF IGNIPLMNSL GTSIVNGIYR
IVINQILQSP GIYYQSELDH NGISVYTGTI ISDWGGRLEL EIDKKARIWA RVSRKQKISI
LVLSSAMGLN LREILENVCY PEIFLSFLTD KEKKQIGSKE NAILEFYQQF SCVGGDPIFS
ESLCKELQKK FFHQRCELGR IGRRNINWRL NLTIPQNNIF LLPRDILAAA DHLIGMKFGM
GTLDDMNHLQ NKRIRSVADL LQDQFGLALA RLENVVKGTI CGAIKHKLIP TPQNLVTATP
LTTTYESFFG LHPLSQVLDR TNPLTQIVHG RKLSYLGPGG LTGRTANFRI RDIHPSHYGR
ICPIDTSEGI NVGLIGSLAI HARIGDWGSL ESPFYELFEK SKKARIRMLF LSPSQDEYYM
IAAGNSLALN RGIQEEQAVP ARYRQEFLTI AWEEVHLRSI FPFQYFSIGA SLIPFIEHND
ANRALMSSNM QRQAVPLSRS EKCIVGTGLE RQVALDSGVP AIAEQEGKIL YTDTKKIILS
GYGDNTLGIP LIRYQRSNKN TCMHQKPQVR RGKCIKKGQI LADGAATVGG ELALGKNILV
GYMPWEGYNF EDAVLISECL VYGNIYTSFH IRKYEIQTHV TTQGPERITK EIPHLEGRLL
RNLDKNGIVM LGSWVETGDI LVGKLTPQVA KESSYAPEDR LLRAILGIQV STSKETCLKL
PIGGRGRVID VRWVQKKGGS SYNPEKIRVY ISQKREIKVG DKVAGRHGNK GIISKILPRQ
DMPYLQDGRP VDMVFNPLGV PSRMNVGQIF ECSLGLAGSL LDRHYRIAPF DERYEQEASR
KLVFSELYEA SKQTANPWVF EPEYPGKSRI FDGRTGDPFE QPVIIGKPYI LKLIHQVDDK
IHGRSSGHYA LVTQQPLRGR SKQGGQRVGE MEVWALEGFG VAHILQEMLT YKSDHIRARQ
EVLGTTIIGG TIPKPEDAPE SFRLLVRELR SLALDLNHFL VSEKNFQINR KEV