ID   RPOB_LACPL              Reviewed;        1201 AA.
AC   Q88XZ3; F9UMJ8;
DT   16-JAN-2004, integrated into UniProtKB/Swiss-Prot.
DT   16-NOV-2011, sequence version 2.
DT   03-AUG-2022, entry version 105.
DE   RecName: Full=DNA-directed RNA polymerase subunit beta {ECO:0000255|HAMAP-Rule:MF_01321};
DE            Short=RNAP subunit beta {ECO:0000255|HAMAP-Rule:MF_01321};
DE            EC=2.7.7.6 {ECO:0000255|HAMAP-Rule:MF_01321};
DE   AltName: Full=RNA polymerase subunit beta {ECO:0000255|HAMAP-Rule:MF_01321};
DE   AltName: Full=Transcriptase subunit beta {ECO:0000255|HAMAP-Rule:MF_01321};
GN   Name=rpoB {ECO:0000255|HAMAP-Rule:MF_01321}; OrderedLocusNames=lp_1021;
OS   Lactiplantibacillus plantarum (strain ATCC BAA-793 / NCIMB 8826 / WCFS1)
OS   (Lactobacillus plantarum).
OC   Bacteria; Firmicutes; Bacilli; Lactobacillales; Lactobacillaceae;
OC   Lactiplantibacillus.
OX   NCBI_TaxID=220668;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-793 / NCIMB 8826 / WCFS1;
RX   PubMed=12566566; DOI=10.1073/pnas.0337704100;
RA   Kleerebezem M., Boekhorst J., van Kranenburg R., Molenaar D., Kuipers O.P.,
RA   Leer R., Tarchini R., Peters S.A., Sandbrink H.M., Fiers M.W.E.J.,
RA   Stiekema W., Klein Lankhorst R.M., Bron P.A., Hoffer S.M.,
RA   Nierop Groot M.N., Kerkhoven R., De Vries M., Ursing B., De Vos W.M.,
RA   Siezen R.J.;
RT   "Complete genome sequence of Lactobacillus plantarum WCFS1.";
RL   Proc. Natl. Acad. Sci. U.S.A. 100:1990-1995(2003).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND GENOME REANNOTATION.
RC   STRAIN=ATCC BAA-793 / NCIMB 8826 / WCFS1;
RX   PubMed=22156394; DOI=10.1128/jb.06275-11;
RA   Siezen R.J., Francke C., Renckens B., Boekhorst J., Wels M.,
RA   Kleerebezem M., van Hijum S.A.;
RT   "Complete resequencing and reannotation of the Lactobacillus plantarum
RT   WCFS1 genome.";
RL   J. Bacteriol. 194:195-196(2012).
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: The RNAP catalytic core consists of 2 alpha, 1 beta, 1 beta'
CC       and 1 omega subunit. When a sigma factor is associated with the core
CC       the holoenzyme is formed, which can initiate transcription.
CC       {ECO:0000255|HAMAP-Rule:MF_01321}.
CC   -!- SIMILARITY: Belongs to the RNA polymerase beta chain family.
CC       {ECO:0000255|HAMAP-Rule:MF_01321}.
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DR   EMBL; AL935263; CCC78437.1; -; Genomic_DNA.
DR   RefSeq; YP_004888951.1; NC_004567.2.
DR   AlphaFoldDB; Q88XZ3; -.
DR   SMR; Q88XZ3; -.
DR   STRING; 220668.lp_1021; -.
DR   EnsemblBacteria; CCC78437; CCC78437; lp_1021.
DR   KEGG; lpl:lp_1021; -.
DR   PATRIC; fig|220668.9.peg.863; -.
DR   eggNOG; COG0085; Bacteria.
DR   HOGENOM; CLU_000524_4_1_9; -.
DR   PhylomeDB; Q88XZ3; -.
DR   BioCyc; LPLA220668:G1GW0-880-MON; -.
DR   Proteomes; UP000000432; Chromosome.
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; IPR019462; DNA-dir_RNA_pol_bsu_external_1.
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; 1.
DR   Pfam; PF04563; RNA_pol_Rpb2_1; 1.
DR   Pfam; PF04561; RNA_pol_Rpb2_2; 2.
DR   Pfam; PF04565; RNA_pol_Rpb2_3; 1.
DR   Pfam; PF10385; RNA_pol_Rpb2_45; 1.
DR   Pfam; PF00562; RNA_pol_Rpb2_6; 1.
DR   Pfam; PF04560; RNA_pol_Rpb2_7; 1.
DR   TIGRFAMs; TIGR02013; rpoB; 1.
DR   PROSITE; PS01166; RNA_POL_BETA; 1.
PE   3: Inferred from homology;
KW   DNA-directed RNA polymerase; Nucleotidyltransferase; Reference proteome;
KW   Transcription; Transferase.
FT   CHAIN           1..1201
FT                   /note="DNA-directed RNA polymerase subunit beta"
FT                   /id="PRO_0000047908"
FT   REGION          1165..1201
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1170..1187
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1201 AA;  134502 MW;  9BA8E9F6AD987BD2 CRC64;
     MAGHLVKYGK HRTRRSYARI KEVLDLPNLI EIQTDSYQWF LDEGLREMFE DIMPIDDFAG
     KLSLEFVDYQ LLEPKYTVEE AREHDANYSA PLHVTLRLTN HETGEIKSQD VFFGDFPLMT
     EQGTFIINGA ERVIVSQLVR SPGVYFNEEL DKNGRPSYGT TVIPNRGAWL ELETDAKNVS
     YVRIDRTRKI PLTELVRALG YGSDDDIIDM LGETDSLMLT LEKDVHKNTD DSRVEESLKD
     IYERLRPGEP KTADSSRSLL TARFFDPKRY DFAPVGRYKV NKKLSMKTRL MDQTLAETLA
     DPDTGEVIAQ KDTVIDKNVM AKLSPYLERD DFKTVTYTPS DEAVVTNPMV LQVVKVYSQN
     DPEKVVNVIG NGNIDLKFKH IVPADIIASI NYFFNLQEGL GSTDDIDHLG NRRIRSVGEL
     LQNQFRIGLS RMERVVRERM SIQDAATVTP QQLINIRPVV ASIKEFFGSS QLSQFMDQTN
     PLGELTHKRR LSALGPGGLT RDRAGYEVRD VHYTHYGRMC PIETPEGPNI GLINSLSSYA
     KVNRSGFIET PYRRVDWTTH KVTDKIDYLA ADEEDQFVIA QANSPLNDDG SFVEDTVLAR
     NKEENLETPI ENVDYMDVSP KQVVAVATAC IPFLENDDSN RALMGANMQR QAVPLLDPHA
     PLIGTGIEYK AAHDSGIALI CRHEGTVEYV DAREVRVRRD DGSLDTYKLM KFRRSNGGKN
     YNQRPIVKVG DHVDNDEVLA DGPAMEGGEL ALGQNPLVAF MTWNGYNFED AIIINERLVR
     EDVYTSIHIE EYESEARDTK LGPEEMTREI PNVGEDALKN LDEDGIIRIG AEVKDGDILV
     GKVTPKGVTE LSAEERLLHA IFGEKAREVR DTSLRVPHGG GGIIQDVKIF TRENGDELSP
     GVNMMVRVYI AQKRKIQVGD KMAGRHGNKG TVSIVVPEED MPYMPDGTPI DIMLSPMGVP
     SRMNIGQVLE LHLGMAARKL GIHMATPVFD GAQDTDIWEA IREAGVDSDA KSIVYDGRTG
     EPFDKRVAVG VMHYMKLSHM VDDKIHARSI GPYSLVTQQP LGGKAQFGGQ RFGEMEVWAL
     EAYGAAYTLQ EILTYKSDDV VGRVKTYEAI VKGEPIPKPG VPESFRVLVK ELQALGLDMK
     VLDSEDKEIE LRDMDDDDDE VVNVDALSKF KQQQDEKAAD KAAKADAAKP SETTNAQQDN
     Q