RPOB_BORBU
ID RPOB_BORBU Reviewed; 1155 AA.
AC Q59191; O51350;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 15-DEC-1998, sequence version 2.
DT 03-AUG-2022, entry version 128.
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=BB_0389;
OS Borreliella burgdorferi (strain ATCC 35210 / DSM 4680 / CIP 102532 / B31)
OS (Borrelia burgdorferi).
OC Bacteria; Spirochaetes; Spirochaetales; Borreliaceae; Borreliella.
OX NCBI_TaxID=224326;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 35210 / DSM 4680 / CIP 102532 / B31;
RX PubMed=9074501; DOI=10.1016/s0378-1119(96)00714-7;
RA Alekshun M., Kashlev M., Schwartz I.;
RT "Molecular cloning and characterization of Borrelia burgdorferi rpoB.";
RL Gene 186:227-235(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 35210 / DSM 4680 / CIP 102532 / B31;
RX PubMed=9403685; DOI=10.1038/37551;
RA Fraser C.M., Casjens S., Huang W.M., Sutton G.G., Clayton R.A.,
RA Lathigra R., White O., Ketchum K.A., Dodson R.J., Hickey E.K., Gwinn M.L.,
RA Dougherty B.A., Tomb J.-F., Fleischmann R.D., Richardson D.L.,
RA Peterson J.D., Kerlavage A.R., Quackenbush J., Salzberg S.L., Hanson M.,
RA van Vugt R., Palmer N., Adams M.D., Gocayne J.D., Weidman J.F.,
RA Utterback T.R., Watthey L., McDonald L.A., Artiach P., Bowman C.,
RA Garland S.A., Fujii C., Cotton M.D., Horst K., Roberts K.M., Hatch B.,
RA Smith H.O., Venter J.C.;
RT "Genomic sequence of a Lyme disease spirochaete, Borrelia burgdorferi.";
RL Nature 390:580-586(1997).
CC -!- FUNCTION: DNA-dependent RNA polymerase catalyzes the transcription of
CC DNA into RNA using the four ribonucleoside triphosphates as substrates.
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; L48488; AAC37118.1; -; Genomic_DNA.
DR EMBL; AE000783; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR PIR; D70148; D70148.
DR RefSeq; WP_002660664.1; NC_001318.1.
DR RefSeq; YP_008686574.1; NC_001318.1.
DR AlphaFoldDB; Q59191; -.
DR SMR; Q59191; -.
DR PRIDE; Q59191; -.
DR PATRIC; fig|224326.49.peg.784; -.
DR OMA; FMTWEGY; -.
DR Proteomes; UP000001807; 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..1155
FT /note="DNA-directed RNA polymerase subunit beta"
FT /id="PRO_0000047866"
FT CONFLICT 39..40
FT /note="KS -> EKV (in Ref. 1; AAC37118)"
FT /evidence="ECO:0000305"
FT CONFLICT 78
FT /note="D -> V (in Ref. 1; AAC37118)"
FT /evidence="ECO:0000305"
FT CONFLICT 129
FT /note="G -> A (in Ref. 1; AAC37118)"
FT /evidence="ECO:0000305"
FT CONFLICT 180..184
FT /note="DYLYV -> IIFIE (in Ref. 1; AAC37118)"
FT /evidence="ECO:0000305"
FT CONFLICT 191..193
FT /note="RIL -> EYV (in Ref. 1; AAC37118)"
FT /evidence="ECO:0000305"
FT CONFLICT 306
FT /note="G -> A (in Ref. 1; AAC37118)"
FT /evidence="ECO:0000305"
FT CONFLICT 316
FT /note="M -> S (in Ref. 1; AAC37118)"
FT /evidence="ECO:0000305"
FT CONFLICT 566..567
FT /note="KC -> NV (in Ref. 1; AAC37118)"
FT /evidence="ECO:0000305"
FT CONFLICT 573..574
FT /note="AA -> RR (in Ref. 1; AAC37118)"
FT /evidence="ECO:0000305"
FT CONFLICT 580..581
FT /note="KY -> ND (in Ref. 1; AAC37118)"
FT /evidence="ECO:0000305"
FT CONFLICT 869..891
FT /note="VPHGTEGTVIDVQRITKEDVGNL -> FLMVLKVLLLMFKGLPKRILVS
FT (in Ref. 1; AAC37118)"
FT /evidence="ECO:0000305"
FT CONFLICT 898..903
FT /note="ILKVYV -> NLSSLA (in Ref. 1; AAC37118)"
FT /evidence="ECO:0000305"
FT CONFLICT 1078..1085
FT /note="AAHTLQEL -> RRTPSRT (in Ref. 1; AAC37118)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1155 AA; 129624 MW; 1295040746D73173 CRC64;
MIKRVHLGQG RADEILDLPN LIEIQLNSYE KFLQLDKLKS KKPLLNEGLE SVFRNIFPIK
SGNGDVALEY ERYYIENDAL NFTEKECKRK GQSYEAVLKV RLNLQFLTTG EIRQKDVYMG
TIPLMTERGT FIINGAERVV VSQIHRSPGV VFYKEKDLYS ARIIPYRGSW LEFEIDSKKD
YLYVKIDRKK RILITLFLRA LGFDTREKII ETFYNIKKIK VEDGTKRDLP GQYLAKSINI
RENMYYRAGD KITLQDVEDF LQNGVNEIEL VDFDGYNDIS GKRFVSSNVI LNCLEKEDAF
FALKDGSKEL PKESVMLAVY GSLFPGEPIS IDNAENDLKT IFFSERRYDL GRVGRYKLSK
KFGFDDLTTS VLTMDDIVNT ISHLLRIYEG HDILDDIDHL GNRRVRSVGE LLTNIYKGAM
SRVEKIAKDR MSNKEVFNLK PQELISVKPI VSAVKEFFAT SQLSQFMDQV NPLAELTHKR
RLNALGPGGL SRDRAGFEVR DVHYTHYGRM CPIETPEGPN IGLIVSLATY SRVNDYGFLE
TPYRKVVNGV VTDQLEYLSA IDEEKKCIAQ ANAAFNSNGK YLEDLVSVRI SGDYTTTSPT
NIDYMDVSPR QLISVSSALI PFLEHNDANR ALMGSNMQRQ AVPLLFPKPP IVGTGMESVV
AKDSGVVVKA KRSGEVILAT SSKIVVKPFE AENAKDLDEY 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 KYLGESYNVP VFESATNEQI QEKLKTAGFN PTSKEILYDG YTGEPFENEV
MVGVIYMLKL HHLVDDKMHA RSTGPYSLVS QQPLGGKAQF GGQRLGEMEV WALEAYGAAH
TLQELLTVKS DDMSGRVKIY ENIVKGVPTN VSGIPESFNV LMQELRGLGL DLSIYDDAGN
QVPLTEKEEE LINKS
