ID   RPOB_CLOBB              Reviewed;        1249 AA.
AC   B2TIG8;
DT   14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT   01-JUL-2008, sequence version 1.
DT   03-AUG-2022, entry version 82.
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=CLL_A0231;
OS   Clostridium botulinum (strain Eklund 17B / Type B).
OC   Bacteria; Firmicutes; Clostridia; Eubacteriales; Clostridiaceae;
OC   Clostridium.
OX   NCBI_TaxID=935198;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Eklund 17B / Type B;
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 sequence of Clostridium botulinum strain Eklund.";
RL   Submitted (APR-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; CP001056; ACD21931.1; -; Genomic_DNA.
DR   RefSeq; WP_012422821.1; NC_018648.1.
DR   AlphaFoldDB; B2TIG8; -.
DR   SMR; B2TIG8; -.
DR   PRIDE; B2TIG8; -.
DR   EnsemblBacteria; ACD21931; ACD21931; CLL_A0231.
DR   KEGG; cbk:CLL_A0231; -.
DR   PATRIC; fig|935198.13.peg.205; -.
DR   HOGENOM; CLU_000524_4_1_9; -.
DR   OMA; FMTWEGY; -.
DR   OrthoDB; 9601at2; -.
DR   Proteomes; UP000001195; 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; 2.40.270.10; -; 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; 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..1249
FT                   /note="DNA-directed RNA polymerase subunit beta"
FT                   /id="PRO_1000141678"
SQ   SEQUENCE   1249 AA;  140671 MW;  38B31AA097643AA3 CRC64;
     MVHPVQVGKR TRMSFGKVKD VTEMPNLIEV QLDSYQWFLR EGLHEVFEDI NPITNFTGNL
     VLEFVDYKLD MDNIKYSVEE CKERDATYAA PLKVSVRLQN NETGEIKEQE VFMGDFPLMT
     EQGTFIINGA ERVIVSQLVR SPGVYYNYSI DKTGKKLYSA TVIPNRGAWL EYETDSNDII
     YVRIDKTRKL PITILARAMG FGSDQELLDF FGEDERFRAS IEKDNTKTRE EGLLEIYKRL
     RPGEPPTVDS AISLIDSLFF DAKRYDLSRV GRYKFNKKLA LNLRIANQIA AMDVINPSTG
     EIMVEKGQKI SRLLAEDIQN AGIKSVDILV DDKLVRVISN NFVDITKQVP FDVSDLQIKE
     LVHYPTLREI LDNYSDETTI KEEIKKNLSR LIPKHIIKDD IFATISYELG LPYGIGYVDD
     IDHLGNRRLR SVGELLQNQF RIGLSRMERV VKERMTIQDQ ESITPQMLIN IRPVAAAIKE
     FFGSSQLSQF MDQTNPLSEL THKRRLSALG PGGLSRERAG FEVRDVHHSH YGRMCPIETP
     EGPNIGLINS LATFARVNEY GFIETPYRIV DKENARATEE IRYFTADEED QCLIAQAKEP
     LDENGYFVDK KVTVRYLEDV LVVPATDVDL MDVSARQIVS VATAMIPFLE NDDASRALMG
     SNMQRQAVPL LKPQAPIVGT GIEFKAAVDS GVLPKARNAG 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 NEIEECLEKA
     GYNANGKTVL YDGRTGEPFD NLVTVGIMYI LKLAHLVDDK IHARSTGPYS LVTQQPLGGK
     AQFGGQRFGE MEVWALEAYG AAHTLQEILT VKSDDVVGRV KTYEAIVKGE NIPEPGVPES
     FKVLIKELQA LCLDVKVLNE NHQEVSLKEY TDDEIADLEV NIEGSEESVP VVPVVESNIE
     EVEVEVEVEV ETETEDGYRE DLDEIEYDEN FEIETLETDL ELDDFNDEH