ID   RPOB_LACCB              Reviewed;        1199 AA.
AC   B3WAM8;
DT   14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT   02-SEP-2008, sequence version 1.
DT   03-AUG-2022, entry version 78.
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=LCABL_26820;
OS   Lacticaseibacillus casei (strain BL23) (Lactobacillus casei).
OC   Bacteria; Firmicutes; Bacilli; Lactobacillales; Lactobacillaceae;
OC   Lacticaseibacillus.
OX   NCBI_TaxID=543734;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=BL23;
RA   Maze A., Boel G., Bourand A., Loux V., Gibrat J.F., Zuniga M., Hartke A.,
RA   Deutscher J.;
RT   "Lactobacillus casei BL23 complete genome sequence.";
RL   Submitted (JUN-2008) 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: 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; FM177140; CAQ67747.1; -; Genomic_DNA.
DR   RefSeq; WP_012491990.1; NC_010999.1.
DR   AlphaFoldDB; B3WAM8; -.
DR   SMR; B3WAM8; -.
DR   KEGG; lcb:LCABL_26820; -.
DR   HOGENOM; CLU_000524_4_1_9; -.
DR   OMA; FMTWEGY; -.
DR   OrthoDB; 9601at2; -.
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; Transcription;
KW   Transferase.
FT   CHAIN           1..1199
FT                   /note="DNA-directed RNA polymerase subunit beta"
FT                   /id="PRO_1000141704"
FT   REGION          1175..1199
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1199 AA;  133700 MW;  6AE78A267DA8A708 CRC64;
     MAGHLVNYGK HRTRRSYARI KEVLDLPNLI KIQTNSYQWF LDEGLKEMFD DIMPIDDFQG
     KLSLEFVGYQ LLEPKYTVEE ARQHDANYSA PLHVTLRLTN HETGEIKSQD VFFGDFPLMT
     KQGTFIINGA ERVIVSQLVR SPGVYFHSET DKNSRVTYGT TVIPNRGAWL EYETDAKDIA
     YVRIDRTRKI PLTELVRALG FGSDQDIINM FGDNDSLMLT LEKDVHKNTD DSRTDEALKD
     IYERLRPGEP KTADSSRSLL YARFFDPKRY DLASVGRYKV NKKLSLKTRL LNQVLAETLA
     DPDTGEVIAQ KGTKVDRQVM DKLAPYLDRD DFKTITYQPS DQGVVTDPIE LQSIKVYSQV
     TPDKEINLIG NGHIGKKVKH IVPADVLASM NYFLNLQEGL GSIDDIDHLG NRRIRSVGEL
     LQNQFRIGLS RMERVVRERM SIQDTATVTP QQLINIRPVV ASIKEFFGSS QLSQFMDQTN
     PLGELTHKRR LSALGPGGLT RDRAGYEVRD VHYTHYGRMC PIETPEGPNI GLINSLASYA
     VVNPYGFIET PYRRVSWDTH KVTDKIDYLT ADEEDNYIVA QANSPLNDDG SFVDETVLAR
     HKDNNIEISP DKVDYMDVSP KQVVAVATAC IPFLENDDSN RALMGANMQR QAVPLVNPHA
     PLVGTGMEYK AAHDSGTAVL ANNAGTVEYV DAKQIRVRRE DGALDAYNLM KFKRSNAGKN
     YNQRPIVTIG DHVDVDEIIA DGPAMQNGEL ALGQNPIIAF MTWNMYNYED AIVLSERLVK
     DDVYTSIHIE EYESEARDTK LGPEEVTREI PNVGEEALKD LDEFGVVRVG AEVRDGDILV
     GKVTPKGVTE LSAEERLLHA IFGEKAREVR DTSLRVPHGG GGIIQDVKIF TREAGDELSP
     GVNMMVRVYI TQKRKIQVGD KMAGRHGNKG TVSVVVPEED MPYLPDGTPV DICLSPMGVP
     SRMNIGQVLE LHLGMAARNL GIHVATPVFD GANDKDLWAT VKEAGMASDG KSVLYDGRTG
     EPFENRVSVG IMYYMKLSHM VDDKIHARSI GPYSLVTQQP LGGKAQFGGQ RFGEMEVWAL
     EAYGAAYTLQ EILTYKSDDV VGRVKTYEAI VKGEPIPKPG VPESFRVLVK ELQALGLDMK
     VLGADKKEIE LRDMDDDEDD IVSVDALAKF AAQQEEKKAH EAAAQATDGK SANSTDDKK