ID   RPOB_PEDPA              Reviewed;        1202 AA.
AC   Q03EA9;
DT   11-SEP-2007, integrated into UniProtKB/Swiss-Prot.
DT   14-NOV-2006, sequence version 1.
DT   03-AUG-2022, entry version 86.
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=PEPE_1426;
OS   Pediococcus pentosaceus (strain ATCC 25745 / CCUG 21536 / LMG 10740 /
OS   183-1w).
OC   Bacteria; Firmicutes; Bacilli; Lactobacillales; Lactobacillaceae;
OC   Pediococcus.
OX   NCBI_TaxID=278197;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 25745 / CCUG 21536 / LMG 10740 / 183-1w;
RX   PubMed=17030793; DOI=10.1073/pnas.0607117103;
RA   Makarova K.S., Slesarev A., Wolf Y.I., Sorokin A., Mirkin B., Koonin E.V.,
RA   Pavlov A., Pavlova N., Karamychev V., Polouchine N., Shakhova V.,
RA   Grigoriev I., Lou Y., Rohksar D., Lucas S., Huang K., Goodstein D.M.,
RA   Hawkins T., Plengvidhya V., Welker D., Hughes J., Goh Y., Benson A.,
RA   Baldwin K., Lee J.-H., Diaz-Muniz I., Dosti B., Smeianov V., Wechter W.,
RA   Barabote R., Lorca G., Altermann E., Barrangou R., Ganesan B., Xie Y.,
RA   Rawsthorne H., Tamir D., Parker C., Breidt F., Broadbent J.R., Hutkins R.,
RA   O'Sullivan D., Steele J., Unlu G., Saier M.H. Jr., Klaenhammer T.,
RA   Richardson P., Kozyavkin S., Weimer B.C., Mills D.A.;
RT   "Comparative genomics of the lactic acid bacteria.";
RL   Proc. Natl. Acad. Sci. U.S.A. 103:15611-15616(2006).
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}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; CP000422; ABJ68463.1; -; Genomic_DNA.
DR   RefSeq; WP_002833322.1; NC_008525.1.
DR   AlphaFoldDB; Q03EA9; -.
DR   SMR; Q03EA9; -.
DR   STRING; 278197.PEPE_1426; -.
DR   EnsemblBacteria; ABJ68463; ABJ68463; PEPE_1426.
DR   GeneID; 33061584; -.
DR   KEGG; ppe:PEPE_1426; -.
DR   eggNOG; COG0085; Bacteria.
DR   HOGENOM; CLU_000524_4_1_9; -.
DR   OMA; FMTWEGY; -.
DR   OrthoDB; 9601at2; -.
DR   Proteomes; UP000000773; 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..1202
FT                   /note="DNA-directed RNA polymerase subunit beta"
FT                   /id="PRO_0000300365"
FT   REGION          1151..1202
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1163..1180
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1181..1202
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1202 AA;  134620 MW;  3399DD4143FCDA7C CRC64;
     MAGHLVKYGK HRTRRSYARI KEVLDLPNLI EIQSDSYQWF LDEGLREMFN DIMPIEDFAG
     KLSLEFVDYQ LLEPKYTVDE AREHEANYSA PLHVTLRLTN HETGEIKSQD VFFGDFPLMT
     EQGTFIINGA ERVIVSQLVR SPGVYYNLDT DKNNRKIWGT TVIPNRGAWL EYETDAKEIS
     YVRIDRTRKI PMTELVRALG FGSDEEIIDI FGGSDSLDFT LDKDVHKNPE DSRVAESLKD
     IYERLRPGEP KTADSSRSLL TARFFDPKRY DMAPVGRYKV NKKLSLKTRL LGQTLAETLA
     DPDTGEVIAQ KGEMVNKDVM KKLAVFLDRP DFKMVTYQPS EEAVVTEPMT IQVIKVQDPN
     DPERTLNMIG NGNIDAKLKH ITPADIIASM NYFFLLQDGI GSTDDIDHLG NRRIRSVGEL
     LQNQFRIGLS RMERVVRERM SIQDAETVTP QQLINIRPVV AATKEFFGSS QLSQFMDQTN
     PLGELSHKRR LSALGPGGLT RDRAGYEVRD VHYTHYGRMC PIETPEGPNI GLINNLASYG
     KINRYGFIET PYRRVSWEDH KVTDRIDYLT ADEEDQFVIA QANSPLNDDG SFADDVVMAR
     HESDNIETSI ENVDYMDVSP KQVVAVATAC IPFLENDDSN RALMGANMQR QAVPLVDPHS
     PLIGTGIEYK AAHDSGVALL CQHAGVVEYV DAREVRVRRD DGALDTYKLM KFRRSNGGKN
     YNQRPIVRVN DKVDADEVLA DGPSMEQGEL ALGQNPLIAF MTWQGYNFED AIAINERLVR
     DDVYTSIHIE EYESEARDTK LGPEEMTREI PNIGEDALRN LDQDGIVRVG AEVEDGDILV
     GKVTPKGVTE LSAEERLLHA IFGEKAREVR DTSLRVPHGG GGIVQDVKIF TRENGDELSP
     GVNMMVRVYI AQKRKLQVGD KMAGRHGNKG TVSVVIPQED MPYMPDGTPI DIMLSPMGVP
     SRMNIGQVLE LHLGMAARNL GIHMTTPVFD GAQDKDIWEA VAEAGMDSDA KSVLYDGRTG
     EPFEQRVAVG VMHYMKLAHM VDDKIHARSI GPYSLVTQQP LGGKAQFGGQ RFGEMEVWAL
     EAYGAAYTLQ EILTYKSDDV VGRVKTYEAI VKGEPIPRPG VPESFRVLVK ELQALGLDMK
     VLGGDDQEVE LRDMDEEDDD VVNVDALSKY AEKQNEKTNA SAEEAKAPST ESAPVETKNN
     QN