ID   RPOB_CLOPE              Reviewed;        1234 AA.
AC   P0C2E7; Q93R88;
DT   23-JAN-2007, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-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}; OrderedLocusNames=CPE2413;
OS   Clostridium perfringens (strain 13 / Type A).
OC   Bacteria; Firmicutes; Clostridia; Eubacteriales; Clostridiaceae;
OC   Clostridium.
OX   NCBI_TaxID=195102;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=13 / Type A;
RX   PubMed=11792842; DOI=10.1073/pnas.022493799;
RA   Shimizu T., Ohtani K., Hirakawa H., Ohshima K., Yamashita A., Shiba T.,
RA   Ogasawara N., Hattori M., Kuhara S., Hayashi H.;
RT   "Complete genome sequence of Clostridium perfringens, an anaerobic flesh-
RT   eater.";
RL   Proc. Natl. Acad. Sci. U.S.A. 99:996-1001(2002).
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; BA000016; BAB82119.1; -; Genomic_DNA.
DR   RefSeq; WP_003460611.1; NC_003366.1.
DR   AlphaFoldDB; P0C2E7; -.
DR   SMR; P0C2E7; -.
DR   STRING; 195102.gene:10491730; -.
DR   PRIDE; P0C2E7; -.
DR   EnsemblBacteria; BAB82119; BAB82119; BAB82119.
DR   GeneID; 29570169; -.
DR   KEGG; cpe:CPE2413; -.
DR   HOGENOM; CLU_000524_4_1_9; -.
DR   OMA; FMTWEGY; -.
DR   Proteomes; UP000000818; 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; Reference proteome;
KW   Transcription; Transferase.
FT   CHAIN           1..1234
FT                   /note="DNA-directed RNA polymerase subunit beta"
FT                   /id="PRO_0000047885"
SQ   SEQUENCE   1234 AA;  138550 MW;  13F7884F93104023 CRC64;
     MVHPVQVGKR TRMSFAKVKD VAEMPNLIEI QLDSYKWFLD AGLYEVFDDI NPISNFTGNL
     VLEFVGYTLD MDNIKYSVEE CKERDTTYAA PLKVAVRLQN KETGEIKEQE VFMGDFPLMT
     EQGTFIINGA ERVIVSQLVR SPGVYYNYNV DKTGKKLFSA TVIPNRGAWL EYETDSNDVI
     YVRIDKTRKL PISILGRAMG FGSDQELLEY FGEEERFKAT IEKDNTKTKE EALLEIYKRL
     RPGEPPTVDS AISLIDSLFF DAKRYDLSRV GRYKFNKKLA IGLRIANQIA AEDIVDKLTG
     EVLVAKGEKI SRANAEEIQN RGINSVDVLV EDRVIRIIGN HFVDIHKCVD FDISDLNIRE
     LVHYPTLREI LDNYSDEETI KEEIKKNMTR LIPKHIIKDD IFATISYQIG LAYNIGYVDD
     IDHLGNRRLR SVGELLQNQF RIGLSRMERV VKERMTIQDQ EAITPQQLIN IRPVAAAIKE
     FFGSSQLSQF MDQTNPLSEL THKRRLSALG PGGLSRERAG FEVRDVHHSH YGRMCPIETP
     EGPNIGLINS LATYAKVNEY GFIETPYRVV DKAEGRVTGE IRYFTADEED QYLVAQANEP
     LDENGCFIDK KVTVRDKGEV LVVPSKDVDL MDVSPRQLVS VATAMIPFLE NDDASRALMG
     SNMQRQAVPL LKPYAPIVGT GIEYKAAVDS GVLPKAKNAG EVVYVSANEV RVKRELDGGV
     DTYRLLKFKR SNQGTCINQR PIVAKGDWVL KGEVLADGPS TDLGEIALGK NIRMGFITWE
     GYNYEDAMLI SEELVREDVF TSIHIEEYEC EARDTKLGPE EITRDIPNVS EDALKDIDER
     GIIRIGAEVR SGDILVGKVT PKGETELTAE ERLLRAIFGE KAREVRDTSL RVPHGEAGII
     VDVKVFTREN GDDLSPGVNE LVRCYIAQKR KISVGDKMAG RHGNKGVISR VLPEEDMPFL
     PDGRPLQICL NPLGVPSRMN IGQVLEVHLG WAASALGWHI ATPVFDGATE TDIEDCLEKA
     GYNRNGKTVL RDGRTGEEFD NEVTVGIMYI LKLAHLVDDK IHARSTGPYS LVTQQPLGGK
     AQFGGQRFGE MEVWALEAYG AAHTLQEILT VKSDDVVGRV KTYEAIVKGE NIPEPGVPES
     FKVLIKELQA LCLDVKVLND NNQEVKFKEL AEDDDEIEVL EVNMEGTEDS TTEEAKEEKG
     EAYIPAEEID EEIDYENIDL LDFTSDLDIE DDFN