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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
 
 
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