RPOB_BORAP
ID RPOB_BORAP Reviewed; 1155 AA.
AC Q0SNB8; G0IS36;
DT 11-SEP-2007, integrated into UniProtKB/Swiss-Prot.
DT 05-SEP-2006, sequence version 1.
DT 03-AUG-2022, entry version 102.
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};
GN OrderedLocusNames=BAPKO_0404, BafPKo_0391;
OS Borreliella afzelii (strain PKo) (Borrelia afzelii).
OC Bacteria; Spirochaetes; Spirochaetales; Borreliaceae; Borreliella.
OX NCBI_TaxID=390236;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PKo;
RX PubMed=16914037; DOI=10.1186/1471-2164-7-211;
RA Gloeckner G., Schulte-Spechtel U., Schilhabel M., Felder M., Suehnel J.,
RA Wilske B., Platzer M.;
RT "Comparative genome analysis: selection pressure on the Borrelia vls
RT cassettes is essential for infectivity.";
RL BMC Genomics 7:211-211(2006).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PKo;
RX PubMed=22123755; DOI=10.1128/jb.05951-11;
RA Casjens S.R., Mongodin E.F., Qiu W.G., Dunn J.J., Luft B.J.,
RA Fraser-Liggett C.M., Schutzer S.E.;
RT "Whole-genome sequences of two Borrelia afzelii and two Borrelia garinii
RT Lyme disease agent isolates.";
RL J. Bacteriol. 193:6995-6996(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; CP000395; ABH01660.1; -; Genomic_DNA.
DR EMBL; CP002933; AEL69617.1; -; Genomic_DNA.
DR RefSeq; WP_011600996.1; NC_008277.1.
DR AlphaFoldDB; Q0SNB8; -.
DR SMR; Q0SNB8; -.
DR STRING; 390236.BafPKo_0391; -.
DR PRIDE; Q0SNB8; -.
DR EnsemblBacteria; AEL69617; AEL69617; BafPKo_0391.
DR KEGG; baf:BAPKO_0404; -.
DR KEGG; bafz:BafPKo_0391; -.
DR PATRIC; fig|390236.22.peg.384; -.
DR eggNOG; COG0085; Bacteria.
DR HOGENOM; CLU_000524_4_1_12; -.
DR OMA; FMTWEGY; -.
DR Proteomes; UP000005216; 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_0000300285"
FT CONFLICT 446
FT /note="S -> R (in Ref. 2; AEL69617)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1155 AA; 129869 MW; 133FC58FDB7DD5B4 CRC64;
MIKRVHLGQG RADEILDLPN LIEIQLNSYE KFLQLDKLKN KKPLLNEGLE SVFRNIFPIK
SGNGDVALEY ERYYIENDTL NFTEKECKRK GQSYEAVLKV RLNLQFLTTG EIRQKDVYMG
TIPLMTERGT FIINGAERVI VSQIHRSPGV VFYKEKDLYS ARIIPYRGSW LEFEIDSKKD
YLYVKIDRKK RILITLFLRA LGFDTREKII ETFYNIKKIK VEEGTKRDLP GQYLAKSINI
RENMYYRAGD KITLQDVEDF LQNGVNEIEL VDFDGYNDVS GKYFVSSNVI LNCLEKEDAF
FALKDGSKEL PKESVMLAVY GALFPGEPIS IDNAENDLKT IFFSERRYDL GRVGRYKLSK
KFGSDDLSTS VLTMDDIVNT ISHLLRIYEG HDILDDIDHL GNRRVRSVGE LLTNIYKGAM
SRVEKIAKDR MSNKEVFNLK PQELISVKPI VSAVKEFFAT SQLSQFMDQV NPLAELTHKR
RLNALGPGGL SRDRAGFEVR DVHYTHYGRM CPIETPEGPN IGLIVSLATY SRVNDYGFLE
TPYRKVVNGE VTNELEYLSA IDEEKKCIAQ ANAAFNSDGK YLEDLVSVRI SGDYTTTNPK
NIDYMDVSPR QLISVSSALI PFLEHNDANR ALMGSNMQRQ AVPLLFPKPP IVGTGMESVV
AKDSGVVVKA KRSGEVILAT SNKIVVKPFE SENVKDLDEY HIVKYERTNQ DTCFNQSVLV
KEGQKVERGE IIADGPATRY GELALGNNLL LGVIPWNGFN YEDAILISDR IVKEDLYTSI
HIKEFSIEVR ETKLGPEKVT GDIPNVSEKI LNKLDENGII RIGTYVKPGD ILVGKVTPKS
EGDITPEFRL LTSIFGEKAK DVKNNSLKVP HGTEGTVIDV QRITKEDVGN LSPGVEEILK
VYVAKKRKLK EGDKMAGRHG NKGVVAKILP VEDMPYLADG TPLDICLNPL GVPSRMNIGQ
LMESQLGLAG KYLSESYNVP VFESATNEQI QEKLKKAGFN PTSKEILYDG YTGEPFENEV
MVGVIYMLKL HHLVDDKMHA RSTGPYSLVS QQPLGGKAQF GGQRLGEMEV WALEAYGAAH
TLQELLTVKS DDMSGRVKIY ENIVKGVPTN VSGIPESFNV LMQELRGLGL DLSIYDDNGN
QVPLTEKEEE LINKS