RPOB_BORDL
ID RPOB_BORDL Reviewed; 1155 AA.
AC B5RLU9;
DT 14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT 04-NOV-2008, sequence version 1.
DT 03-AUG-2022, entry version 77.
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=BDU_383;
OS Borrelia duttonii (strain Ly).
OC Bacteria; Spirochaetes; Spirochaetales; Borreliaceae; Borrelia.
OX NCBI_TaxID=412419;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Ly;
RX PubMed=18787695; DOI=10.1371/journal.pgen.1000185;
RA Lescot M., Audic S., Robert C., Nguyen T.T., Blanc G., Cutler S.J.,
RA Wincker P., Couloux A., Claverie J.-M., Raoult D., Drancourt M.;
RT "The genome of Borrelia recurrentis, the agent of deadly louse-borne
RT relapsing fever, is a degraded subset of tick-borne Borrelia duttonii.";
RL PLoS Genet. 4:E1000185-E1000185(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; CP000976; ACH93335.1; -; Genomic_DNA.
DR RefSeq; WP_012538146.1; NC_011229.1.
DR AlphaFoldDB; B5RLU9; -.
DR SMR; B5RLU9; -.
DR STRING; 412419.BDU_383; -.
DR EnsemblBacteria; ACH93335; ACH93335; BDU_383.
DR KEGG; bdu:BDU_383; -.
DR eggNOG; COG0085; Bacteria.
DR HOGENOM; CLU_000524_4_3_12; -.
DR OMA; FMTWEGY; -.
DR Proteomes; UP000000611; 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; Transcription;
KW Transferase.
FT CHAIN 1..1155
FT /note="DNA-directed RNA polymerase subunit beta"
FT /id="PRO_1000141663"
SQ SEQUENCE 1155 AA; 130073 MW; 6EAD90ABCAD2D543 CRC64;
MIKRVHLGQG KAEEILNLPN LIEIQLNSYE KFLQLERLKN NKPLLNEGLE SVFRDVFPMK
SSNGEVALEY EKYYIEYDSI SFTEKECKRK GQSYEAVLKI RLNLQFLTTG EIRQKDVYMG
TIPLMTDRGT FIVNGAERVI VSQIHRSPGV VFYKEKDLYY ARIIPYRGSW LEFEIDSKKD
YLYVKIDRKK RILVTLFLRA LGLDTREKII ETFYKIRKIE VNDDTKREIT GQYLATNITI
KENMTYRAGD KITLQDIEDF LQNGVKEINL IDFDGYDSVP GKHFISSDVI LNCFEKEDAY
FALKDGFKEL SRESVMLAVY SVLLPGEPIS IDNAENDLRT VFFSEKRYDL GHVGRYKLSK
KFGLDDLTTS VLTMTDIVNT ISHLLRIYDG HDVLDDIDHL GNRRVRSVGE LLTNIYKGAM
SRVEKIAKDR MSNKEVFNLK PQELISVKPV VSAVKEFFAT SQLSQFMDQV NPLAELTHKR
RLNALGPGGL SRDRAGFEVR DVHYTHYGRM CPIETPEGPN IGLIVSLATY SKVNDYGFLE
TPYRKVIDGK VTDDIEYLSA IDEEKKCIAQ ANASVSSDGN YTDDLVSVRI SGDYTTMMPK
NIDYMDVSPR QLISVSSALI PFLEHNDANR ALMGSNMQRQ AVPLLFPQPP IVGTGMERIV
AKDSGVVIKA KRPGRVVLAT NKKIVIKPDN ATSERDLDEY ELYKYERTNQ DTSFNHSVLV
KNGQIVNKDE IIADGPATRY GELALGNNLL VGFIPWNGFN YEDAILISER IVKEDLYTSI
HIKEFSIEVR ETKLGPEKVT ADIPNVSGKI LSKLDENGIV RIGTYVKPGD ILIGKVTPKS
EGDITPEFKL LTSIFGEKAK DVKNNSLKVP HGTEGTVIDV QRITKDDVGN LPPGVDEILK
VYIAKKRKLK EGDKMAGRHG NKGVVAKILP VEDMPYLADG TPLDICLNPL GVPSRMNIGQ
LMESQLGLAG KYLGEYYDVP VFESATNECI QEKLKKAGFN ETSKAVLYDG YTGEPFENEV
MVGVIYMLKL HHLVDDKMHA RSTGPYSLVS QQPLGGKAQF GGQRLGEMEV WALEAYGAAH
TLQELLTVKS DDMSGRVKIY ENIVKGIPTN VSGIPESFNV LMQELRGLGF DLSIYDDNGN
QIPLTEKEEE LINKT