ID   RPOB_CLOBH              Reviewed;        1232 AA.
AC   A5I7L4; A7G8U6;
DT   08-APR-2008, integrated into UniProtKB/Swiss-Prot.
DT   26-JUN-2007, sequence version 1.
DT   03-AUG-2022, entry version 90.
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};
GN   OrderedLocusNames=CBO3488, CLC_3433;
OS   Clostridium botulinum (strain Hall / ATCC 3502 / NCTC 13319 / Type A).
OC   Bacteria; Firmicutes; Clostridia; Eubacteriales; Clostridiaceae;
OC   Clostridium.
OX   NCBI_TaxID=441771;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Hall / ATCC 3502 / NCTC 13319 / Type A;
RX   PubMed=17519437; DOI=10.1101/gr.6282807;
RA   Sebaihia M., Peck M.W., Minton N.P., Thomson N.R., Holden M.T.G.,
RA   Mitchell W.J., Carter A.T., Bentley S.D., Mason D.R., Crossman L.,
RA   Paul C.J., Ivens A., Wells-Bennik M.H.J., Davis I.J., Cerdeno-Tarraga A.M.,
RA   Churcher C., Quail M.A., Chillingworth T., Feltwell T., Fraser A.,
RA   Goodhead I., Hance Z., Jagels K., Larke N., Maddison M., Moule S.,
RA   Mungall K., Norbertczak H., Rabbinowitsch E., Sanders M., Simmonds M.,
RA   White B., Whithead S., Parkhill J.;
RT   "Genome sequence of a proteolytic (Group I) Clostridium botulinum strain
RT   Hall A and comparative analysis of the clostridial genomes.";
RL   Genome Res. 17:1082-1092(2007).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Hall / ATCC 3502 / NCTC 13319 / Type A;
RX   PubMed=18060065; DOI=10.1371/journal.pone.0001271;
RA   Smith T.J., Hill K.K., Foley B.T., Detter J.C., Munk A.C., Bruce D.C.,
RA   Doggett N.A., Smith L.A., Marks J.D., Xie G., Brettin T.S.;
RT   "Analysis of the neurotoxin complex genes in Clostridium botulinum A1-A4
RT   and B1 strains: BoNT/A3, /Ba4 and /B1 clusters are located within
RT   plasmids.";
RL   PLoS ONE 2:E1271-E1271(2007).
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; AM412317; CAL85049.1; -; Genomic_DNA.
DR   EMBL; CP000727; ABS36887.1; -; Genomic_DNA.
DR   RefSeq; YP_001255970.1; NC_009495.1.
DR   RefSeq; YP_001389211.1; NC_009698.1.
DR   AlphaFoldDB; A5I7L4; -.
DR   SMR; A5I7L4; -.
DR   KEGG; cbh:CLC_3433; -.
DR   KEGG; cbo:CBO3488; -.
DR   PATRIC; fig|413999.7.peg.3465; -.
DR   HOGENOM; CLU_000524_4_1_9; -.
DR   OMA; FMTWEGY; -.
DR   PRO; PR:A5I7L4; -.
DR   Proteomes; UP000001986; 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..1232
FT                   /note="DNA-directed RNA polymerase subunit beta"
FT                   /id="PRO_0000329171"
FT   REGION          1170..1232
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1195..1232
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   CONFLICT        160
FT                   /note="A -> T (in Ref. 2; ABS36887)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   1232 AA;  138933 MW;  C7A892458422A89C CRC64;
     MVHPVQVGKR TRMSFSRLKE VGQMPNLIEV QLDSYDWFLK EGLQEVFDDI NPIQDYTGNL
     NLEFVGYKLD LDSIKYSVEE CKERDSTYAA PLKVKVRLLN KETGEIKEQE VFMGDFPLMT
     EQGTFIINGA ERVIVSQLVR SPGVYYDMTV DKTGSKLFSA TVIPNRGAWL EYETDSNNII
     YVRIDKTRKL PITILARALG YGTDAEIIEF FGEDERLKAT IEKDNTKTRE EALLEIYKRL
     RPGEPPTVDS AESLIESLFF DAKRYDLSRV GRYKFNKKLA IHLRITNQIA DQDIVNPQTG
     EILVQKGEKI DKDKAIEIQN CGINEVYIKI DDKSFKVIGN HFVDIHSLVP FDISDLNIKE
     YVFYPVLKEI LDNYADEESI KEEIRKNIYR LIPKHIIRED IYATINYELA LSYDIGYKDD
     IDHLGNRRLR SVGELLQNQF RIGLSRMERV VKERMTIQDQ EVITPQALIN IRPVAASIKE
     FFGSSQLSQF MDQTNPLSEL THKRRLSALG PGGLSRERAG FEVRDVHHSH YGRMCPIETP
     EGPNIGLINS LATFAKVNEY GFIETPYRRI DPKNKRATND IVYMTADEED LYVIARSDEP
     IDENGYFIDD KVTVRAKEEV LVVPVSEVEY MDISPRQLVS VATAMIPFLE NDDASRALMG
     SNMQRQAVPL LKPQAPIVGT GIEYKAATDS GVLPKAKNAG TVVYVSADEI RVRRDSDGGI
     DKYKLLKFKR SNQGTCINQR PIVSKGEVVA KETLLADGPS TDLGEIALGK NILMGFITWE
     GYNYEDAMLI SEQLVKEDVF TSIHIEEYEA EARDTKLGPE EITRDIPNVG EEALKDIDER
     GIIRIGAEVR SGDILVGKVT PKGETELTAE ERLLRAIFGE KAREVRDTSL RVPHGEAGII
     VDVKIFTREN GDELPPGVNK LVRCYIAQKR KISVGDKMAG RHGNKGVISR VLPEEDMPFL
     PDGRPLQICL NPLGVPSRMN IGQVLEVHLG LAASKLGWHI ATPVFDGAIE SDIVDCLRKA
     GYSEDGKTVL YDGRTGEPFD NRVTVGYMYI LKLAHLVDDK IHARSTGPYS LVTQQPLGGK
     AQFGGQRFGE MEVWALEAYG AAHTLQEILT VKSDDVVGRV KTYEAIVKGE NIPEPGVPES
     FKVLIKELQA LCLDVKVLND DNQEIKLKES VDEDADELEV NIEGTENQPE EKEEKEKEDS
     DEYDDLREED VEPDLEELSL DDLDLDDFGD EH