RPOB_CLOBL
ID RPOB_CLOBL Reviewed; 1234 AA.
AC A7GJ82;
DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT 11-SEP-2007, sequence version 1.
DT 03-AUG-2022, entry version 77.
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=CLI_3671;
OS Clostridium botulinum (strain Langeland / NCTC 10281 / Type F).
OC Bacteria; Firmicutes; Clostridia; Eubacteriales; Clostridiaceae;
OC Clostridium.
OX NCBI_TaxID=441772;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Langeland / NCTC 10281 / Type F;
RA Brinkac L.M., Daugherty S., Dodson R.J., Madupu R., Brown J.L., Bruce D.,
RA Detter C., Munk C., Smith L.A., Smith T.J., White O., Brettin T.S.;
RL Submitted (JUN-2007) 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; CP000728; ABS40506.1; -; Genomic_DNA.
DR RefSeq; WP_012101135.1; NC_009699.1.
DR AlphaFoldDB; A7GJ82; -.
DR SMR; A7GJ82; -.
DR EnsemblBacteria; ABS40506; ABS40506; CLI_3671.
DR KEGG; cbf:CLI_3671; -.
DR HOGENOM; CLU_000524_4_1_9; -.
DR OMA; FMTWEGY; -.
DR Proteomes; UP000002410; 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; Transcription;
KW Transferase.
FT CHAIN 1..1234
FT /note="DNA-directed RNA polymerase subunit beta"
FT /id="PRO_1000051969"
FT REGION 1169..1234
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1174..1234
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1234 AA; 139177 MW; 873B3DDB330BA5F2 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 IYATINYELG 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 EKEEKEEEKE
DSDEYDDLRE EDVEPDLEEL SLDDLDLDDF GDEH
