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RPOB_BORGP
ID   RPOB_BORGP              Reviewed;        1155 AA.
AC   Q661M9;
DT   21-FEB-2006, integrated into UniProtKB/Swiss-Prot.
DT   11-OCT-2004, sequence version 1.
DT   03-AUG-2022, entry version 103.
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=BG0390;
OS   Borrelia garinii subsp. bavariensis (strain ATCC BAA-2496 / DSM 23469 /
OS   PBi) (Borrelia bavariensis).
OC   Bacteria; Spirochaetes; Spirochaetales; Borreliaceae; Borreliella.
OX   NCBI_TaxID=290434;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-2496 / DSM 23469 / PBi;
RX   PubMed=15547252; DOI=10.1093/nar/gkh953;
RA   Gloeckner G., Lehmann R., Romualdi A., Pradella S., Schulte-Spechtel U.,
RA   Schilhabel M., Wilske B., Suehnel J., Platzer M.;
RT   "Comparative analysis of the Borrelia garinii genome.";
RL   Nucleic Acids Res. 32:6038-6046(2004).
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; CP000013; AAU07242.1; -; Genomic_DNA.
DR   RefSeq; WP_011193715.1; NZ_CP028872.1.
DR   AlphaFoldDB; Q661M9; -.
DR   SMR; Q661M9; -.
DR   STRING; 290434.BG0390; -.
DR   EnsemblBacteria; AAU07242; AAU07242; BG0390.
DR   KEGG; bga:BG0390; -.
DR   eggNOG; COG0085; Bacteria.
DR   HOGENOM; CLU_000524_4_0_12; -.
DR   OMA; FMTWEGY; -.
DR   OrthoDB; 9601at2; -.
DR   Proteomes; UP000002276; 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_0000224034"
SQ   SEQUENCE   1155 AA;  129675 MW;  4D1BB9DD02849590 CRC64;
     MIKRVHLGQG RADEILDLPN LIEIQLNSYE KFLQLDKLKN KKPLLNEGLE SVFRNIFPIK
     SGNGDVALEY ERYYIENDAL NFTEKECKRK GQSYEAVLKV RLNLQFLTTG EIRQKDVYMG
     TIPLMTERGT FIINGAERVV VSQIHRSPGV VFYKEKDLYS ARIIPYRGSW LEFEIDSKKD
     YLYVKIDRKK RILITLFLRA LGFDTREKII ETFYNIKKIK VEDSTKRDLP GQYLAKSINI
     RENMYYRAGD KITLQDVEDF LQNGVNEIEL VDFDGYDAIS GKCFVSSNVI LNCLEKEDAF
     FALKDGSKEL PKESVMLAVY GALFPGEPIS IDNAENDLKT IFFSERRYDL GRVGRYKLSK
     KFGFDDLSTS VLTMYDIVNT ISHLLRIYEG HDILDDIDHL GNRRVRSVGE LLTNIYKGAM
     SRVEKIAKDR MSNKEVFNLK PQELISVKPI VSAVKEFFAT SQLSQFMDQV NPLAELTHKR
     RLNALGPGGL SRDRAGFEVR DVHYTHYGRM CPIETPEGPN IGLIVSLATY SRVNDYGFLE
     TPYRKVVNGE VTDELEYLSA IDEEKKCIAQ ANAAFNSNGK YLEDLVSVRI SGDYTTTNPK
     NIDYMDVSPR QLISVSSALI PFLEHNDANR ALMGSNMQRQ AVPLLFPKPP IVGTGMESVV
     AKDSGVVVKA KRSGEVILAT SSKIVVKPFE SENAKDLDEY HIVKYERTNQ DTCFNQSVLV
     KEGQKVESGE 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 QEKLKKAGFN PTSKEILYDG YTGEPFENEV
     MVGVIYMLKL HHLVDDKMHA RSTGPYSLVS QQPLGGKAQF GGQRLGEMEV WALEAYGAAH
     TLQELLTVKS DDMSGRVKIY ENIVKGVPTN VSGIPESFNV LMQELRGLGL DLSIYDDNGN
     QVPLTEKEEE LINKG
 
 
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