RPOB_CLOBM
ID RPOB_CLOBM Reviewed; 1239 AA.
AC B1KSN3;
DT 14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT 29-APR-2008, sequence version 1.
DT 03-AUG-2022, entry version 80.
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=CLK_2932;
OS Clostridium botulinum (strain Loch Maree / Type A3).
OC Bacteria; Firmicutes; Clostridia; Eubacteriales; Clostridiaceae;
OC Clostridium.
OX NCBI_TaxID=498214;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Loch Maree / Type A3;
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; CP000962; ACA56498.1; -; Genomic_DNA.
DR RefSeq; WP_012344363.1; NC_010520.1.
DR AlphaFoldDB; B1KSN3; -.
DR SMR; B1KSN3; -.
DR EnsemblBacteria; ACA56498; ACA56498; CLK_2932.
DR KEGG; cbl:CLK_2932; -.
DR HOGENOM; CLU_000524_4_3_9; -.
DR OMA; FMTWEGY; -.
DR Proteomes; UP000000722; 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; -; 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..1239
FT /note="DNA-directed RNA polymerase subunit beta"
FT /id="PRO_1000141680"
FT REGION 1182..1239
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1239 AA; 139848 MW; 3D2D26C86C07220B 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 CGVNEVYIKI DDKSFKVIGN HFVDIHSLIS FDISDLNIKE
YVFYPVLKEI LDNYADEESI KEEIRKNIYR LIPKHIIRED IYATINYELG LSYDIGYKDD
IDHLGNRRLR SVGELLQNQF RIGLSRMERV VKERMTIQDQ EVITPQALIN IRPVAASIKE
FFGSSQLSQF MDQTNPLSEL THKRRLSALG PGGLSRERAG FEVRDVHHSH YGRMCPIETP
EGPNIGLINS LATFAKVNEY GFIETPYRRI DPKNKRATND IVYMTADEED LYVIARSDEP
IDENGYFMDD KVTVRAKEEV LVVPVSEVEY MDISPRQLVS VATAMIPFLE NDDASRALMG
SNMQRQAVPL LKPQAPIVGT GIEYKAATDS GVLPKAKNAG TVAYVSADEI RVRRDSDGGI
DKYKLLKFKR SNQGTCINQR PIVSKGEVVA KETLLADGPS TDLGEIALGK NILMGFITWE
GYNYEDAMLI SEQLVREDVF 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 VDEDVDELEV NIEGAENQLE DKEEKEEEKE
ENYKEDSDEY DDLREEDVEP DLEELSLDDL DLDDFGDEH
