ID   RPOB_CLOD6              Reviewed;        1238 AA.
AC   Q18CF1;
DT   11-SEP-2007, integrated into UniProtKB/Swiss-Prot.
DT   25-JUL-2006, sequence version 1.
DT   03-AUG-2022, entry version 99.
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=CD630_00660;
OS   Clostridioides difficile (strain 630) (Peptoclostridium difficile).
OC   Bacteria; Firmicutes; Clostridia; Eubacteriales; Peptostreptococcaceae;
OC   Clostridioides.
OX   NCBI_TaxID=272563;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=630;
RX   PubMed=16804543; DOI=10.1038/ng1830;
RA   Sebaihia M., Wren B.W., Mullany P., Fairweather N.F., Minton N.,
RA   Stabler R., Thomson N.R., Roberts A.P., Cerdeno-Tarraga A.M., Wang H.,
RA   Holden M.T.G., Wright A., Churcher C., Quail M.A., Baker S., Bason N.,
RA   Brooks K., Chillingworth T., Cronin A., Davis P., Dowd L., Fraser A.,
RA   Feltwell T., Hance Z., Holroyd S., Jagels K., Moule S., Mungall K.,
RA   Price C., Rabbinowitsch E., Sharp S., Simmonds M., Stevens K., Unwin L.,
RA   Whithead S., Dupuy B., Dougan G., Barrell B., Parkhill J.;
RT   "The multidrug-resistant human pathogen Clostridium difficile has a highly
RT   mobile, mosaic genome.";
RL   Nat. Genet. 38:779-786(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; AM180355; CAJ66881.1; -; Genomic_DNA.
DR   RefSeq; WP_003436174.1; NC_009089.1.
DR   RefSeq; YP_001086530.1; NC_009089.1.
DR   PDB; 7L7B; EM; 3.26 A; C=2-1238.
DR   PDBsum; 7L7B; -.
DR   AlphaFoldDB; Q18CF1; -.
DR   SMR; Q18CF1; -.
DR   STRING; 272563.CD630_00660; -.
DR   ChEMBL; CHEMBL2363852; -.
DR   DrugCentral; Q18CF1; -.
DR   EnsemblBacteria; CAJ66881; CAJ66881; CD630_00660.
DR   GeneID; 66352564; -.
DR   KEGG; cdf:CD630_00660; -.
DR   PATRIC; fig|272563.8.peg.77; -.
DR   eggNOG; COG0085; Bacteria.
DR   OMA; FMTWEGY; -.
DR   PhylomeDB; Q18CF1; -.
DR   BioCyc; PDIF272563:G12WB-120-MON; -.
DR   PRO; PR:Q18CF1; -.
DR   Proteomes; UP000001978; 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; 1.
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   1: Evidence at protein level;
KW   3D-structure; DNA-directed RNA polymerase; Nucleotidyltransferase;
KW   Reference proteome; Transcription; Transferase.
FT   CHAIN           1..1238
FT                   /note="DNA-directed RNA polymerase subunit beta"
FT                   /id="PRO_0000300300"
SQ   SEQUENCE   1238 AA;  139323 MW;  DFB1A1C7CDAE170D CRC64;
     MPHPVTIGKR TRMSFSKIKE IADVPNLIEI QVDSYEWFLK EGLKEVFDDI SPIEDYTGNL
     ILEFVDYSLD DKPKYDIEEC KERDATYCAP LKVKVRLINK ETGEIKEQEV FMGDFPLMTE
     RGTFVINGAE RVIVSQLVRS PGVYYAEERD KTGKRLISST VIPNRGAWLE YETDSNDVIS
     VRVDRTRKQP VTVLLRALGI GTDAEIIDLL GEDERLSATL EKDNTKTVEE GLVEIYKKLR
     PGEPPTVESA SSLLNALFFD PKRYDLAKVG RYKFNKKLAL CYRIMNKISA EDIINPETGE
     VFVKAGEKIS YDLAKAIQNA GINVVNLLMD DDKKVRVIGN NFVDIKSHID FDIDDLNIKE
     KVHYPTLKEI LDGYSDEEEI KEAIKSRIKE LIPKHILLDD IIASISYEFN IFYNIGNIDD
     IDHLGNRRIR SVGELLQNQV RIGLSRMERV IKERMTVQDM EAITPQALVN IRPVSAAIKE
     FFGSSQLSQF MDQTNPLSEL THKRRLSALG PGGLSRERAG FEVRDVHHSH YGRMCPIETP
     EGPNIGLINS LGTYAKINEF GFIESPYRKF DKETSTVTDE IHYLTADEED LFVRAQANEP
     LTEDGKFVNH RVVCRTVNGA VEMVPESRVD YMDISPKQVV SVATAMIPFL ENDDANRALM
     GANMQRQAVP LVRREAPIIG TGIEYRAAKD SGAVVVARNS GIAERVTADE IIIKREDGNR
     DRYNLLKFKR SNSGTCINQT PIINKGDQII KGDVIADGPA TDLGEVALGR NCLIAFMTWE
     GYNYEDAILI NERLVKEDRL STIHIEEYEC EARDTKLGPE EITRDIPNVG DSAIKNLDDR
     GIIRIGAEVD SGDILVGKVT PKGETELTAE ERLLRAIFGE KAREVRDTSL KVPHGESGII
     VDVKVFTREN GDDLSPGVNE LVRCYIAKKR KIKVGDKMAG RHGNKGVISR VLPEEDMPFM
     ENGTPLDIIL NPQGIPSRMN IGQVLEVHLG LAAKTLGWYV ATSVFDGANE YDIMDALEEA
     GYPRDGKLTL YDGRTGESFD NRITVGYMYY LKLHHLVDEK LHARSTGPYS LVTQQPLGGK
     AQFGGQRFGE MEVWALEAYG AAHILQEILT VKSDDVVGRV RTYEAIVKGE NIPEPGIPES
     FKVLIKELQS LCLDVKVLTD EDQEIEVRES VDEDDTIGEF ELDVVNHMGE VEESNIIEEI
     EDDFAENAED EDIENLEEFT EDDLFEEEID FDSDDFDM