RPOB_PELTS
ID RPOB_PELTS Reviewed; 1224 AA.
AC A5D5I2;
DT 20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT 12-JUN-2007, sequence version 1.
DT 03-AUG-2022, entry version 83.
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=PTH_0312;
OS Pelotomaculum thermopropionicum (strain DSM 13744 / JCM 10971 / SI).
OC Bacteria; Firmicutes; Clostridia; Eubacteriales; Desulfotomaculaceae;
OC Pelotomaculum.
OX NCBI_TaxID=370438;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 13744 / JCM 10971 / SI;
RX PubMed=18218977; DOI=10.1101/gr.7136508;
RA Kosaka T., Kato S., Shimoyama T., Ishii S., Abe T., Watanabe K.;
RT "The genome of Pelotomaculum thermopropionicum reveals niche-associated
RT evolution in anaerobic microbiota.";
RL Genome Res. 18:442-448(2008).
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; AP009389; BAF58493.1; -; Genomic_DNA.
DR AlphaFoldDB; A5D5I2; -.
DR SMR; A5D5I2; -.
DR STRING; 370438.PTH_0312; -.
DR PRIDE; A5D5I2; -.
DR EnsemblBacteria; BAF58493; BAF58493; PTH_0312.
DR KEGG; pth:PTH_0312; -.
DR eggNOG; COG0085; Bacteria.
DR HOGENOM; CLU_000524_4_1_9; -.
DR OMA; FMTWEGY; -.
DR Proteomes; UP000006556; 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; Reference proteome;
KW Transcription; Transferase.
FT CHAIN 1..1224
FT /note="DNA-directed RNA polymerase subunit beta"
FT /id="PRO_1000086375"
SQ SEQUENCE 1224 AA; 137444 MW; 510689DA108A5E25 CRC64;
MAYPEKVGAR VRYNFGRLRE VLDLPNLIEV QRNSYKWFLE EGLREVFQDI SPIQDFTGNL
VLEFLDYTLG EPKYTVEECK ERDVTYAAPL RVKVRLINKE TGEVKEQDVF MGDFPLMTEK
GTFIINGAER VIVSQLVRSP GVYFDETIDP SGKKLYTATI IPNRGAWLEF ETDVNDHIFV
RIDRTRKIPA TVLVRALGYG TKAQVAELFN EDKNILETLA RDNTDSEEEA LVEIYKRLRP
GEPPTVDSAR SLLTSLFFDP KRYDLANVGR YKIQKKLKHG VLYRYGPNPD GKTVFDPYLK
KEVPQKREFI RELTKEDIIE TIRYLLKLMN GEGQVDDIDH LGNRRLRSVG ELLQNQFRIG
LSRMERVVRE RMTIQDVDVI TPQVLINIRP VVAAIKEFFG SSQLSQFMDQ TNPLAELTHK
RRLSALGPGG LSRERAGFEV RDVHHSHYGR MCPIETPEGP NIGLIGSLST YARINEFGFI
ETPYRKVDKE NRRVTDEIVY LTADEEEGYV IAQANAPLDE EGRFIEPRVN ARSPEIVVVP
ADRVDYMDVS PKQVFSIATA LIPFLEHDDA NRALMGANMQ RQAVPLLKAQ APLVGTGIEY
KAARDSGVVV IAKESGTVEK VTSTHIEIRN DRGYLDRYKL LKFTRSNQGT CVNQKPIVKK
GERVEAGQVI ADGPSTDYGE LALGRNVLVA FMPWEGYNYE DAILVSEKTV KEDYFTSIHI
EEYECDARDT KLGPEEITRD IPNVGEEILK DLDDRGIIRV GAEVRPGDIL VGKVTPKGET
ELTAEERLLR AIFGEKAREV RDTSLRVPHG ESGKVVDVKV FSRDNGDELP PGVNQLVRVY
IAQKRKISEG DKMAGRHGNK GVIARILPEE DMPFLPDGTP IEIVLNPLGV PSRMNIGQVL
EAHLGWAAKV LGYYVSTPVF NGASEESIFE ALKEAAFKES GLRSFMEKAG LNEEELIGAV
ETAEKRAGSR EALIKEVEGA ESSGETIMAA IERTGLTAGM VNRLEEAGMT KKEILGAMKK
LLFARSGKMT LYDGRTGEPF DSPITVGYVY MLKLAHLVDD KIHARSTGPY SLVTQQPLGG
KAQFGGQRFG EMEVWALEAY GAAYTLQEIL TVKSDDVVGR VKTYEAIVKG ENVPEPGVPE
SFKVLIKELQ SLGLDVKVLS EDDQEIEIRE VEEDIGETAK ELGIDLQEGE LPEVEEADYS
EDVEDEDMFN EEFFNEDFDL EDDE
