RPOB_BORT9
ID RPOB_BORT9 Reviewed; 1155 AA.
AC A1QZH7;
DT 28-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT 14-APR-2009, sequence version 1.
DT 03-AUG-2022, entry version 76.
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=BT0389;
OS Borrelia turicatae (strain 91E135).
OC Bacteria; Spirochaetes; Spirochaetales; Borreliaceae; Borrelia.
OX NCBI_TaxID=314724;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=91E135;
RA Porcella S.F., Raffel S.J., Schrumpf M.E., Montgomery B., Smith T.,
RA Schwan T.G.;
RT "The genome sequence of Borrelia hermsii and Borrelia turicatae:
RT comparative analysis of two agents of endemic N. America relapsing fever.";
RL Submitted (DEC-2004) to the EMBL/GenBank/DDBJ databases.
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; CP000049; AAX17719.1; -; Genomic_DNA.
DR RefSeq; WP_011772338.1; NC_008710.1.
DR AlphaFoldDB; A1QZH7; -.
DR SMR; A1QZH7; -.
DR STRING; 314724.BT0389; -.
DR PRIDE; A1QZH7; -.
DR KEGG; btu:BT0389; -.
DR eggNOG; COG0085; Bacteria.
DR HOGENOM; CLU_000524_4_1_12; -.
DR OMA; FMTWEGY; -.
DR OrthoDB; 9601at2; -.
DR Proteomes; UP000001205; 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; -; 2.
DR Gene3D; 2.40.50.150; -; 1.
DR Gene3D; 3.90.1110.10; -; 2.
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; Transcription;
KW Transferase.
FT CHAIN 1..1155
FT /note="DNA-directed RNA polymerase subunit beta"
FT /id="PRO_1000165791"
SQ SEQUENCE 1155 AA; 130066 MW; 6FB1A898AE1601F1 CRC64;
MIKRVHLGQG KAEEILDLPN LIEIQLNSYE KFLQLDRLKN NKPLLNEGLE SVFRDVFPMK
SSNGEVALEY EKYYVEYDSL SFTEKECKRK GQSYEAVLKI RLNLQFLTTG EIRQKDVYMG
TIPLMTDRGT FIVNGAERVI VSQIHRSPGV VFYKEKDLYY ARIIPYRGSW LEFEIDSKKD
YLYVKIDRKK RILVTLFLRA LGLDTREKII ETFYKIKKIE VNEDTKREIT GQYLAVNITI
KENMTYRAGD KITLQDIEDF LQNGVKEIDL IDFDGYDSVP GKHFISSDVI LNCFEKEDAY
FSLKDGFKEL SRESVMLAVY SVLLPGEPIS IDNAENDLRT VFFSEKRYDL GHVGRYKLSK
KFGLNDLTTS VLTMTDIVNT ISHLLRIYDG HDVLDDIDHL GNRRVRSVGE LLTNIYKGAM
SRVEKIAKDR MSNKEVFNLK PQELISVKPI VSAVKEFFAT SQLSQFMDQV NPLAELTHKR
RLNALGPGGL SRDRAGFEVR DVHYTHYGRM CPIETPEGPN IGLIVSLATY AKVNDYGFLE
TPYRKVINGK VTDEIEYLSA IDEEKKCIAQ ANAAVNAESN YIDDLISVRV SGDYTTMIPK
NIDYMDVSPR QLISVSSALI PFLEHNDANR ALMGSNMQRQ AVPLLFPQPP IVGTGMERIV
AKDSGVVIKA KRSGTVVLAT SKRIVIRPDN ADDEHDLDEY ELAKYERTNQ DTSFNHSVLI
KEGQVVNKGE IIADGPATRY GELALGNNLL VGFIPWNGFN YEDAILISER IVKEDLYTSI
HIKEFSIEVR ETKLGPEKVT ADIPNVSGKI LNKLDENGIV RIGTYVKPGD ILIGKVTPKS
EGDITPEFKL LTSIFGEKAK DVKNNSLKVP HGTEGTVIDV QRITKNDVGN LPPGVDEILK
VYVAKKRRLK EGDKMAGRHG NKGVVAKILP VEDMPYLADG TPLDICLNPL GVPSRMNIGQ
LMESQLGLAG KYLSEYYDVP VFESATNECI QEKLKKAGFN ETSKAILYDG YTGEPFENEV
MVGIIYMLKL HHLVDDKMHA RSTGPYSLVS QQPLGGKAQF GGQRLGEMEV WALEAYGAAY
TLQELLTVKS DDMSGRVKIY ENIVKGIPTN VSGIPESFNV LMQELRGLGF DLSIYDDNGN
QIPLTEKEEE LINKT