RPOB_KINRD
ID RPOB_KINRD Reviewed; 1171 AA.
AC A6W5T0;
DT 08-APR-2008, integrated into UniProtKB/Swiss-Prot.
DT 21-AUG-2007, sequence version 1.
DT 03-AUG-2022, entry version 86.
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=Krad_0680;
OS Kineococcus radiotolerans (strain ATCC BAA-149 / DSM 14245 / SRS30216).
OC Bacteria; Actinobacteria; Kineosporiales; Kineosporiaceae; Kineococcus.
OX NCBI_TaxID=266940;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-149 / DSM 14245 / SRS30216;
RX PubMed=19057647; DOI=10.1371/journal.pone.0003878;
RA Bagwell C.E., Bhat S., Hawkins G.M., Smith B.W., Biswas T., Hoover T.R.,
RA Saunders E., Han C.S., Tsodikov O.V., Shimkets L.J.;
RT "Survival in nuclear waste, extreme resistance, and potential applications
RT gleaned from the genome sequence of Kineococcus radiotolerans SRS30216.";
RL PLoS ONE 3:e3878-e3878(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}.
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DR EMBL; CP000750; ABS02169.1; -; Genomic_DNA.
DR AlphaFoldDB; A6W5T0; -.
DR SMR; A6W5T0; -.
DR STRING; 266940.Krad_0680; -.
DR PRIDE; A6W5T0; -.
DR EnsemblBacteria; ABS02169; ABS02169; Krad_0680.
DR KEGG; kra:Krad_0680; -.
DR eggNOG; COG0085; Bacteria.
DR HOGENOM; CLU_000524_4_3_11; -.
DR OMA; FMTWEGY; -.
DR Proteomes; UP000001116; 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; 1.
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..1171
FT /note="DNA-directed RNA polymerase subunit beta"
FT /id="PRO_0000329181"
SQ SEQUENCE 1171 AA; 129224 MW; 986A971F90A4A62F CRC64;
MEGPLLAASL PASAPNSTYI GNQSPRTVSG RYSFGKIHEP LEVPDLLALQ TDSFDWLLGN
KRWQDRVEAS TNGGLAVPTT SGLEEIFEEI SPIEDFSGSM SLSFRDHRFE PPKYSLDDCK
ERDLTYSAPL FVTAEFINGN TGEIKSQTVF MGDFPLMTDR GTFVINGTER VVVSQLVRSP
GIYFERVPDK TSDRDTWTAK IIPSRGAWLE FEIDKRDTVG VRVDRKRKQS VTVLMKALGW
SESQIREEFA DYESMISTLE KDHTSGVEDA LLDIYRKLRP GEPPTQEAAR NLLDNLYFNP
KRYDLAKVGR YKVNKKLGTE EPLSDSVLSV DDIVRTIKYL VKLHAGEVTM PGVKNGQPVD
VRVEVDDIDH FGNRRLRSVG ELIQNQVRTG LSRMERVVRE RMTTQDVEAI TPQTLINIRP
VVASIKEFFG TSQLSQFMDQ TNPLAGLTHK RRLSALGPGG LSRERAGMEV RDVHPSHYGR
MCPIETPEGP NIGLIGSLSS YGRINPFGFI ETPYRKIVDG VVSDEVEYLT ADEEDAFVIA
QANAPLDADS RFAEARVLVR AKGGETEFVP RDEVDYMDVA ARQMVSVATA MIPFLEHDDA
NRALMGANMQ RQAVPLVKSE APLIGTGMEF RAAVDAGDVV VATKAGVATD VSADMITTSN
DDGTSTTYKV AKFRRSNHGT AYNQQVVINE GDRVEVGTVL ADGPSTDGGE MALGRNLMVA
FMPWEGHNYE DAIILSQRLV QDDVLSSIHI EEHEVDARDT KLGPEEITRD IPNVAEEVLA
DLDERGIIRI GAEVRDGDLL VGKVTPKGET ELTPEERLLR AIFGEKAREV RDTSLKVPHG
ETGTVIGVKV FDRDEGDELP PGVNQLVRVY VANKRKITDG DKLAGRHGNK GVISKILPVE
DMPFLEDGTP VDVILNPLGV PSRMNVGQVL ELHLGWIASR GWKIEGQPDW AKLIPEEIRE
APAGSRIATP VFDGAREEEI TGLLSSTIPT RDGDRLVGGD GKARLFDGRS GEPFPDPVAV
GYMYILKLHH LVDDKIHARS TGPYSMITQQ PLGGKAQFGG QRFGEMEVWA LEAYGAAYAL
QELLTIKSDD VLGRVKVYEA IVKGENIPEP GIPESFKVLI KEMQSLCLNV EVLSSDGMAI
EMRDSDEDVF RAAEELGIDL ARREPSSVEE V