ID   RPOB_LOTJA              Reviewed;        1070 AA.
AC   Q9BBS9;
DT   10-OCT-2002, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2001, sequence version 1.
DT   03-AUG-2022, entry version 94.
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   Lotus japonicus (Lotus corniculatus var. japonicus).
OG   Plastid; Chloroplast.
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   rosids; fabids; Fabales; Fabaceae; Papilionoideae; 50 kb inversion clade;
OC   NPAAA clade; Hologalegina; robinioid clade; Loteae; Lotus.
OX   NCBI_TaxID=34305;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. Miyakojima MG-20;
RX   PubMed=11214967; DOI=10.1093/dnares/7.6.323;
RA   Kato T., Kaneko T., Sato S., Nakamura Y., Tabata S.;
RT   "Complete structure of the chloroplast genome of a legume, Lotus
RT   japonicus.";
RL   DNA Res. 7:323-330(2000).
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; AP002983; BAB33194.1; -; Genomic_DNA.
DR   RefSeq; NP_084796.1; NC_002694.1.
DR   AlphaFoldDB; Q9BBS9; -.
DR   SMR; Q9BBS9; -.
DR   GeneID; 802853; -.
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_0000048028"
SQ   SEQUENCE   1070 AA;  120893 MW;  7126BD99B0B5C063 CRC64;
     MLGVGNEGMS TLPGLNQIQF EGFCRFIDRG LTEELFKFPK IEDTDQEIEF QLFVETYQLV
     EPSIKEKDAV YESLTYSSEL YVSAGLIWKN SKNIQEQTIF IGNIPLMNSL GTSIVNGIYR
     IVINQILQSP GIYYQSELDH KGISVYTGTI ISDWGGRLEL EIDRKARIWA RVSRKQKISI
     LVLSSAMGSN LNEILENVCY PEIFLSFLND KEEKKIGSKE SAILEFYRQF ACVGGDPVFP
     ESLCRELQKK FFQQRCELGE IGRRNMNRRL NLDIPQNNTF LLPRDILTAA DHLIGMKFRM
     GTLDDMNHLK NKRIRSVADL LQDQFGLALV RLENMVRGTI CGAIRYKLIP TPQNLVTSTP
     LTTTYESFFG LHPLSQVLDR TNPLTQIVHG RKLSYLGPGG LTGRTASFRI RDIHSSHYGR
     ICPIDTSEGI NVGLIGSLAI HARIGRWGSI ESPFFEISER SKRIHMLYLS PSRDEYYMIA
     TGNYLALNQG NQEEQIVPAR YRQEFLTIAW EQVHLRSIFS FQYFSIGASL IPFIEHNDAN
     RALMSSNMQR QAVPLSQSEK CIVGTGLERQ VALDSGTLAI AEHEGKIIYK DTNKIVLFGS
     GETLSVPLVI YRRSNKNTCM HQKSQVQRGK CIKRGQILAD GAATVGGELS LGKNVLVAYM
     PWEGYNSEDA VLISDRLVYE DIYTSFHIRK YEIQTHVTSN GPERITNKIP HLEVHLLRNL
     DKNGLVILGS WVEAGDILVG KLTPQMAKES SYAPEDRLLR AILGIQVSTS KETCLKLPIG
     GRGRVIDVRW LHKKGGSGYN PETIHIYILQ KREIKVGDKV AGRHGNKGIV SKILARQDMP
     YLQDGRPVDM VFNPLGVPSR MNVGQIFECS LGLAGDVLDR HYRIAPFDER YEQEASRKLV
     FSELYQASKQ TSNPWIFEPE YPGKSRIFDG RTGTPFEQPV IIGNPYILKL IHQVDDKIHG
     RSSGHYALVT QQPLKGRAKQ GGQRVGEMEV WALEGFGVAH ILQEMLTYKS DHIKARQEVL
     GTTIIGGTIS KPVDAPESFR LLVRELRSLA LELNHFLVSE KNFRIHRKEV