RPOB_OLEA2
ID RPOB_OLEA2 Reviewed; 1375 AA.
AC Q30X05;
DT 21-FEB-2006, integrated into UniProtKB/Swiss-Prot.
DT 06-DEC-2005, sequence version 1.
DT 03-AUG-2022, entry version 95.
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=Dde_2997;
OS Oleidesulfovibrio alaskensis (strain ATCC BAA-1058 / DSM 17464 / G20)
OS (Desulfovibrio alaskensis).
OC Bacteria; Proteobacteria; Deltaproteobacteria; Desulfovibrionales;
OC Desulfovibrionaceae; Oleidesulfovibrio.
OX NCBI_TaxID=207559;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-1058 / DSM 17464 / G20;
RX PubMed=21685289; DOI=10.1128/jb.05400-11;
RA Hauser L.J., Land M.L., Brown S.D., Larimer F., Keller K.L.,
RA Rapp-Giles B.J., Price M.N., Lin M., Bruce D.C., Detter J.C., Tapia R.,
RA Han C.S., Goodwin L.A., Cheng J.F., Pitluck S., Copeland A., Lucas S.,
RA Nolan M., Lapidus A.L., Palumbo A.V., Wall J.D.;
RT "Complete genome sequence and updated annotation of Desulfovibrio
RT alaskensis G20.";
RL J. Bacteriol. 193:4268-4269(2011).
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; CP000112; ABB39791.1; -; Genomic_DNA.
DR RefSeq; WP_011368764.1; NC_007519.1.
DR AlphaFoldDB; Q30X05; -.
DR SMR; Q30X05; -.
DR STRING; 207559.Dde_2997; -.
DR PRIDE; Q30X05; -.
DR EnsemblBacteria; ABB39791; ABB39791; Dde_2997.
DR KEGG; dde:Dde_2997; -.
DR eggNOG; COG0085; Bacteria.
DR HOGENOM; CLU_000524_4_0_7; -.
DR OMA; FMTWEGY; -.
DR OrthoDB; 9601at2; -.
DR Proteomes; UP000002710; 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..1375
FT /note="DNA-directed RNA polymerase subunit beta"
FT /id="PRO_0000224052"
SQ SEQUENCE 1375 AA; 154037 MW; A74C362B17BC97E0 CRC64;
MGQLTKKFGK IEVTLPIPHL LNLQVDSYKK FLQEGAAALA PDEGLEGVFR SVFPIEDFNR
TASLEYVSYE IGEPKYDQAE CISKGLTYEA PIRIKVRLVV YDVDEDSENR TIRDIKEQDI
YFGTLPLMTE KGTFIINGTE RVIVNQLQRS PGIIFEHDAG KTHSSRKVLY SCRVIPMRGS
WLDFDYDHKD ILYVRIDRRR KMPATILFKA MGMSRSDILE YFYKKEYYTL EDDGRLMWEL
DKDLYRKDVA YADVADGEGK VIAKAGKPYT KRSWRLMLEA GIPAVEVAPD YIAGMFLAED
IVDEATGEVL AEAADEITLD LIDRLRECSI KRVPVLHTKG SDTSSSIRDT LLLDKTADQE
QARVEIYRRL RPSSPPTPEI ASTFFENLFR NPDYYDLSPV GRYKLNQRLG LTTTQERVLT
DEDILTAIRV LNHLKDTHGP ADDIDHLGNR RVRPVGELVE NQYRIGLVRM ERAIKERMSL
QEVSTLMPHD LINPKPVQAV LKEFFGTSQL SQFMDQTNAL SEVTHKRRLS ALGPGGLTRE
RAGFEVRDVH TSHYGRICPI ETPEGPNIGL IVSLTTYAKV NDFGFIETPY RVVRDGQVTD
EVKYLDASSE HGEVVAQANA RLDGDHRFVD EFVTTRVRGD VIMSPREEVT LMDISPSQMV
SISAALIPFL EHDDANRALM GSNMQRQAVP LLRSTKPIVG TGMEADVARD SGACIIAEAD
GVVRYADADR IVVSYEGDLY PRTGGVRSYD LQKYHKSNQS SCFGQKPLVS RGQVIRKGDV
LADGPGIEDG ELALGKNLVV AFMPWCGYNF EDSILISERC VKEDVFTSVH IEEFEVVARD
TKLGPEEITR DIPNVGEDML RNLDGSGIIR IGANVKPDDI LVGKITPKGE TQLTPEEKLL
RAIFGEKARD VKNTSLKVPP GIEGTVIDVK LFNRRSGEKD ERTRNIEDYE LARLDQKEKD
HIRALTETTR EKLAPVVVGK QLAYGLAGQK KGEVIAEAGQ TLTAEMLEGL PVKKLSGLFK
SKDTNEAVQQ ALESYDRQIE FINAMYESKR EKVTEGDDLP PGVIKMAKVH IAVKRKLNVG
DKMAGRHGNK GVVSCILPQE DMPFFADGRP VDIVLNPLGV PSRMNIGQIM ETHLGWAAKE
MGRKLALMLE HGQDLASVRE QVKTVFASDA ISSEVDNMDD ETFVRSVRRL RDGIVTKTPV
FDGATEEQIW SWMEQAGLAN DGKTELYDGR TGVRFHNRVT TGVMYILKLH HLVDEKIHAR
STGPYSLVTQ QPLGGKAQFG GQRLGEMEVW ALEAYGAAYL LQEFLTVKSD DVTGRVKMYE
KVVKGDNFLE AGLPESFNVL VKELMSLGLD VTLHQEEGKK RTKRAGMTFG DGTSY