ID   RPOB_CLOBA              Reviewed;        1241 AA.
AC   B2UYA3;
DT   14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT   01-JUL-2008, sequence version 1.
DT   03-AUG-2022, entry version 76.
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=CLH_0230;
OS   Clostridium botulinum (strain Alaska E43 / Type E3).
OC   Bacteria; Firmicutes; Clostridia; Eubacteriales; Clostridiaceae;
OC   Clostridium.
OX   NCBI_TaxID=508767;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Alaska E43 / Type E3;
RA   Brinkac L.M., Brown J.L., Bruce D., Detter C., Munk C., Smith L.A.,
RA   Smith T.J., Sutton G., Brettin T.S.;
RT   "Complete genome sequence of Clostridium botulinum E3 str. Alaska E43.";
RL   Submitted (MAY-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; CP001078; ACD51529.1; -; Genomic_DNA.
DR   RefSeq; WP_003373711.1; NC_010723.1.
DR   AlphaFoldDB; B2UYA3; -.
DR   SMR; B2UYA3; -.
DR   KEGG; cbt:CLH_0230; -.
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; -; 2.
DR   Gene3D; 2.40.50.150; -; 1.
DR   Gene3D; 3.90.1110.10; -; 2.
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..1241
FT                   /note="DNA-directed RNA polymerase subunit beta"
FT                   /id="PRO_1000141677"
SQ   SEQUENCE   1241 AA;  139570 MW;  E738B75094C5AA31 CRC64;
     MVHPVQVGKR TRMSFGKVKD VTEMPNLIEV QLDSYQWFLR EGLHEVFDDI NPITNFTGNL
     VLEFVDYKLD MDNIKYSVEE CKERDATYAA PLKVSVRLQN NETGEIKEQE VFMGDFPLMT
     DQGTFIINGA ERVIVSQLVR SPGVYYNYSI DKTGKKLYSA TVIPNRGAWL EYETDSNDII
     YVRIDKTRKL PITILARAMG FGSDQELLDF FGEDERFRAS IEKDNTKTRE EGLLEIYKRL
     RPGEPPTVDS AISLIDSLFF DAKRYDLSRV GRYKFNKKLA LNLRIANQIA AMDVINPSTG
     EIMVEKGQKI SRLLSEDIQN AGIKSVDILV DDKLVRVISN NFVDITKQVP FDVSDLQIKE
     LVHYPTLKEI LDNYSDEATI KEEIKKNLSR LIPKHIIKDD IFATISYELG LPYGIGYVDD
     IDHLGNRRLR SVGELLQNQF RIGLSRMERV VKERMTIQDQ ESITPQMLIN IRPVAAAIKE
     FFGSSQLSQF MDQTNPLSEL THKRRLSALG PGGLSRERAG FEVRDVHHSH YGRMCPIETP
     EGPNIGLINS LATFARVNEY GFIETPYRII DKENARATEE IRYFTADEED QCLIAQAKEP
     LDENGYFVDK KVTVRYLEDV LVVPATDVDL MDVSARQIVS VATAMIPFLE NDDASRALMG
     SNMQRQAVPL LKPQAPIVGT GIEFKAAVDS GVLPKAKNAG VVTFVSANEI RVKRDSDGGT
     DNYRLLKFKR SNQSSCINQR PIVNKGEIVF KNQVLADGPS TDLGEIALGK NIRMGFITWE
     GYNYEDAMLI SEELVREDVF TSMHIEEYEC EARDTKLGPE EITRDIPNVS EDALKDIDDR
     GIIRIGAEVR SGDILVGKVT PKGETELTAE ERLLRAIFGE KAREVRDTSL RVPHGEAGII
     VDIKVFTREN GDELNPGVNE LVRCYIVQKR KISVGDKMAG RHGNKGVISR ILPEEDMPFL
     PDGRPLQICL NPLGVPSRMN IGQVLEVHLG WAASKLGWHI STPVFDGATE NEIEACLEKA
     GYNANGKTVL YDGRTGEPFD NPVTVGIMYI LKLAHLVDDK IHARSTGPYS LVTQQPLGGK
     AQFGGQRFGE MEVWALEAYG AAHTLQEILT VKSDDVVGRV KTYEAIVKGE NIPEPGVPES
     FKVLIKELQA LCLDVKVLNE NHQEVSLKEY TDDEIADLEV NIEGSEESTP VVPVVESNIE
     EVEVEAEDGY REDLDEIEYD ENFEIETLET DLELDDFNDE H