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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
 
 
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