RPOB_CALS8
ID RPOB_CALS8 Reviewed; 1229 AA.
AC A4XI30;
DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT 29-MAY-2007, sequence version 1.
DT 03-AUG-2022, entry version 82.
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=Csac_0951;
OS Caldicellulosiruptor saccharolyticus (strain ATCC 43494 / DSM 8903 / Tp8T
OS 6331).
OC Bacteria; Firmicutes; Clostridia; Thermoanaerobacterales;
OC Thermoanaerobacterales Family III. Incertae Sedis; Caldicellulosiruptor.
OX NCBI_TaxID=351627;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 43494 / DSM 8903 / Tp8T 6331;
RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S.,
RA Kiss H., Brettin T., Bruce D., Han C., Schmutz J., Larimer F., Land M.,
RA Hauser L., Kyrpides N., Lykidis A., van de Werken H.J.G., Verhaart M.R.A.,
RA VanFossen A.L., Lewis D.L., Nichols J.D., Goorissen H.P., van Niel E.W.J.,
RA Stams F.J.M., Willquist K.U., Ward D.E., van der Oost J., Kelly R.M.,
RA Kengen S.M.W., Richardson P.;
RT "Genome sequence of the thermophilic hydrogen-producing bacterium
RT Caldicellulosiruptor saccharolyticus DSM 8903.";
RL Submitted (APR-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; CP000679; ABP66565.1; -; Genomic_DNA.
DR AlphaFoldDB; A4XI30; -.
DR SMR; A4XI30; -.
DR STRING; 351627.Csac_0951; -.
DR PRIDE; A4XI30; -.
DR EnsemblBacteria; ABP66565; ABP66565; Csac_0951.
DR KEGG; csc:Csac_0951; -.
DR eggNOG; COG0085; Bacteria.
DR HOGENOM; CLU_000524_4_0_9; -.
DR OMA; FMTWEGY; -.
DR Proteomes; UP000000256; 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..1229
FT /note="DNA-directed RNA polymerase subunit beta"
FT /id="PRO_1000051967"
FT REGION 1175..1229
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1215..1229
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1229 AA; 138333 MW; 8636187BDBD00EDA CRC64;
MALPRPVQYG KVQRMSYGKV KEVLDLPYLL EIQKKSFQWF LDEGLREVLR EISPIKDYTE
NLLLEFVDYY FDGPPKYSEQ ECKERDATYA RPLKVKVRLI NKETGEIKEQ DIYMGEFPIM
TETGTFIING AERVIVSQLI RSPGCYFASS IDKQGRKIFS GTIIPNRGAW LEFETDTSEL
LSVRLDRTRK VSLTTLLKAF GLYNQQLIFN KLGEDERLKA SLEKEANKGE IGNPVENALL
EIYRRLRPGE PPNVENAKNL LERMYFDPRG YDLAKVGRYK LNKKLSLWKR IFNKRAAEDI
VDKRTGEILV KEGEIISREA ALNIQDAGIN EVLVYVEDDK VFKVVGNNTV KLDRYVDFDV
SDLNIKELVY LPVLNEILST TNDVNEIKQL IKERERELVP YCLTRDDVFA ATSYFLGLKY
GIGHIDDIDH LGNRRVRAVG ELLQNQFRIG LARMERVIRE RMTIQDIDSV TPQTLINIRP
VTAAIKEFFG SSPLSQFMDQ VNPLAALTNK RRLSALGPGG LSRDRAGFEV RDVHHSHYGR
MCPIETPEGP NIGLITSLAT YARVNEYGFL ETPYRKVDKK EARVTDEVVY LTADEEDTYK
IAQATEPVDE EGRFINQRIT VRFGEDIIEV DKHEVDLVDI SPKQIVSVST SLIPFLENDD
ANRALMGSNM QRQAVPLLTT ESPIIGTGVE YRAAVDSGVC VLAKKDGIVE KVSADEIVIQ
NHDGTKDVYH LLKFKRTNQG TCFNQRPIVR KGQEVKTGEV IADGPSTDHG ELALGKNVLV
AFMPWEGYNY EDAILISERL VKEDVYTSIH IEEYECEARD TKLGPEEITR DIPNIGEDAI
KDLDERGIIR IGAEVKSGDI LVGKVTPKGE TELTAEERLL RAIFGEKARE TRDTSLRVPH
GEGGIVVDVK VFSRDKGDEL PPGVNQLVRV YVAQKRKISV GDKMAGRHGN KGVISRILPV
EDMPFLPDGT PVDIVLNPLG VPSRMNIGQI LETHLGYAAK ALGWKVATPV FDGAKEEDIE
EALNLAGLSP NGKTILYDGR TGEPFDNEVT VGYMYMLKLV HLVDDKIHAR STGPYSLVTQ
QPLGGKAQFG GQRFGEMEVW ALEAYGAAYT LQELLTVKSD DVTGRVKTYE AIVKGENIPE
PGIPESFKVL VKELQSLCLD VKLLSEDNKE IELKESIDED EQPQGLGAFE RGLEEVENGE
EDDDKEKFYE DLMDASQEQD ESADDDIDE
