RPOB_DEIRA
ID RPOB_DEIRA Reviewed; 1159 AA.
AC Q9RVV9;
DT 16-JAN-2004, integrated into UniProtKB/Swiss-Prot.
DT 11-SEP-2007, sequence version 2.
DT 03-AUG-2022, entry version 123.
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=DR_0912;
OS Deinococcus radiodurans (strain ATCC 13939 / DSM 20539 / JCM 16871 / LMG
OS 4051 / NBRC 15346 / NCIMB 9279 / R1 / VKM B-1422).
OC Bacteria; Deinococcus-Thermus; Deinococci; Deinococcales; Deinococcaceae;
OC Deinococcus.
OX NCBI_TaxID=243230;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 13939 / DSM 20539 / JCM 16871 / LMG 4051 / NBRC 15346 / NCIMB
RC 9279 / R1 / VKM B-1422;
RX PubMed=10567266; DOI=10.1126/science.286.5444.1571;
RA White O., Eisen J.A., Heidelberg J.F., Hickey E.K., Peterson J.D.,
RA Dodson R.J., Haft D.H., Gwinn M.L., Nelson W.C., Richardson D.L.,
RA Moffat K.S., Qin H., Jiang L., Pamphile W., Crosby M., Shen M.,
RA Vamathevan J.J., Lam P., McDonald L.A., Utterback T.R., Zalewski C.,
RA Makarova K.S., Aravind L., Daly M.J., Minton K.W., Fleischmann R.D.,
RA Ketchum K.A., Nelson K.E., Salzberg S.L., Smith H.O., Venter J.C.,
RA Fraser C.M.;
RT "Genome sequence of the radioresistant bacterium Deinococcus radiodurans
RT R1.";
RL Science 286:1571-1577(1999).
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 -!- SEQUENCE CAUTION:
CC Sequence=AAF10490.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AE000513; AAF10490.1; ALT_INIT; Genomic_DNA.
DR PIR; G75459; G75459.
DR RefSeq; NP_294636.1; NC_001263.1.
DR RefSeq; WP_027479684.1; NC_001263.1.
DR AlphaFoldDB; Q9RVV9; -.
DR SMR; Q9RVV9; -.
DR STRING; 243230.DR_0912; -.
DR EnsemblBacteria; AAF10490; AAF10490; DR_0912.
DR KEGG; dra:DR_0912; -.
DR PATRIC; fig|243230.17.peg.1099; -.
DR eggNOG; COG0085; Bacteria.
DR HOGENOM; CLU_000524_4_1_0; -.
DR InParanoid; Q9RVV9; -.
DR OMA; FMTWEGY; -.
DR OrthoDB; 9601at2; -.
DR Proteomes; UP000002524; Chromosome I.
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..1159
FT /note="DNA-directed RNA polymerase subunit beta"
FT /id="PRO_0000047891"
SQ SEQUENCE 1159 AA; 128735 MW; C68FF0DE7838FDB9 CRC64;
MTLSKTPPRI ERFGDITEVI PLPNLTEVQV NSFKAFLQDD KAPDQREDVG LQSAFREVFP
IDESEKGRST GMVLDFIEYR LGEPEYSPEE CREKDLTYEA PLYVKLELIH KDTGVIKGFK
PDSPPESWVF LGNLPLMTFD GSFIINGADR VVISQIHRSP GVYFTSSYKG IKKQYTAAII
PMPKRGPWIE LEFAGDVLEM KVNKRKFPVS LLLRVLGMDD ASIRALFTEF TPEVEPGEDK
SAGMGADEAL LRLFTVLRPG DPPKRDKAIQ YLFGLLADPR RYDLGEPGRF KMNTKLGVQR
QERTLLKFED GKFSDAGLVD TIRYLMALQQ GLETVPMVDE DGVVTDVPVA EDDIDHLGNR
RVRTVGELLA DQLRVGMGRM ARGVRERMLL GNPDAATPTK LVNNRPIVAA MREFFGRSQL
SQFKDQTNPL SDLRHKRRIS ALGPGGLTRE RAGFDVRDVH RTHYGRICPI ETPEGANIGL
ISSLSSYAKV NDLGFIMAPY RKVEDGKVTN QVEYMTADIE DRYTIAQANS PLNEDNTFAD
ERVLARRKGD PLLYTPDEVD YMDVSPKQIV SINTSLIPFL EHDDANRALM GSNMQSQAVP
LVRADSPAVG TGVERRVVTD SGTSVVSDVN GRVSYVDARA IQVTLSEDHR ELNMNAGNVR
TFELIRFTRS NQGTNLDQHP IVSVGDEVKV GQVIADGPAS ERGRLALGQN ITIAIMPFDG
FNFEDAICIN EDLVRQDFYT SVHIEKDEIE ARDTKLGPEK ITRDIPGLSE AALRDLDEDG
IVRVGAEVKP GDILVGKTSF KGESEPTPEE RLLRSIFGEK AREVKDTSLR VQSGQGGIVV
KTVRFRRGDE GVDLKPGVRE MVRVYVAQKR QLQVGDKVAN RHGNKGVVSK IVRPEDMPYL
EDGTPVDIVF NPLGVPSRMN LGQILETHLG EVARLTGQKF ETPVFDSVTE ATIKEMLEVA
AAERLQARKD DGFELDKREQ EVLDRAGKLG VIDAPGDDYE KGQMQLARTG KSILYDGRTG
EPISGPVVVG IMYVMKLYHM VEDKLHARST GPYSLITQQP LGGKAQFGGQ RFGEMEVWAL
EAYGAAHVLQ EMLTIKSDDI DGRDAAYQSI VKGEEVSGST IPESFKVLVK ELHSLGLDVE
VLDHGDKAVD IFEGMMPKR
