ID   RPOB_BORHD              Reviewed;        1155 AA.
AC   B2S092;
DT   14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT   01-JUL-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=BH0389;
OS   Borrelia hermsii (strain HS1 / DAH).
OC   Bacteria; Spirochaetes; Spirochaetales; Borreliaceae; Borrelia.
OX   NCBI_TaxID=314723;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=HS1 / DAH;
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; CP000048; AAX16898.1; -; Genomic_DNA.
DR   RefSeq; WP_012422155.1; NC_010673.1.
DR   AlphaFoldDB; B2S092; -.
DR   SMR; B2S092; -.
DR   PRIDE; B2S092; -.
DR   KEGG; bhr:BH0389; -.
DR   HOGENOM; CLU_000524_4_1_12; -.
DR   OMA; FMTWEGY; -.
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_1000141664"
SQ   SEQUENCE   1155 AA;  129995 MW;  E48AC535A31E26BB CRC64;
     MIKRVHLGQG KAEEILDLPN LIEIQLNSYE KFLQLERLKT NRPLLNEGLE SVFRDVFPMK
     SSNGEVALEY EKYYIEYNSL SFTEKECKRK GQSYEAVLKI RLNLQFLTTG EIRQKDVYMG
     TIPLMTDRGT FIVNGAERVI VSQIHRSPGV VFYKEKDLYY ARIIPYRGSW LEFEIDSKKD
     YLYVKIDRKK RILVTLFLRA LGLNTRERII ETFYKIRKIE VNEDTKREIT GQYLATNIII
     KENMTYRAGD KITLQDIEDF LQNGVKEIDL IDFDGYDSVP GKHFISSDVI LNCFEKEDAY
     FSLKDGFKEL SRESVMLAVY SVLLPGEPIS IDNAESDLRN VFFSEKRYDL GHVGRYKLSK
     KFGLDDLTTS VLTMTDIVNT ISHLLRIYDG HDVLDDIDHL GNRRVRSVGE LLTNIYKGAM
     SRVEKIAKDR MSNKEVFNLK PQELISVKPI VSAVKEFFAT SQLSQFMDQV NPLAELTHKR
     RLNALGPGGL SRDRAGFEVR DVHYTHYGRM CPIETPEGPN IGLIVSLATY AKVNDYGFLE
     TPYRKVVDGK VTDEIEYLSA IDEEKKCIAQ ANAAVNAEGN YIDDLISVRV SGDYTTMIPK
     NIDYMDVSPR QLISVSSALI PFLEHNDANR ALMGSNMQRQ AVPLLFPQPP IVGTGMERIV
     AKDSGVVVKA KRSGIVVLAT SKKIVIRPED AADDHDLDEY ELAKYERTNQ DTSFNHSVLV
     KEGQVVNKGE IIADGPATRY GEVALGNNLL VGFIPWNGFN YEDAILISER IIKEDLYTSI
     HIKEFSIEVR ETKLGPEKVT ADIPNVSGKI LNKLDENGIV RIGTYVKPGD ILIGKVTPKS
     EGDITPEFKL LTSIFGEKAK DVKNNSLKVP HGTEGTVIDV QRITKDDVSN LPPGVDEILK
     VYIAKKRKLK EGDKMAGRHG NKGVVAKILP VEDMPYLADG TPLDICLNPL GVPSRMNIGQ
     LMESQLGLAG KYLGEYYDVP VFESATNECI QEKLKKAGFN ETSKAVLYDG YTGEPFENEV
     MVGIIYMLKL HHLVDDKMHA RSTGPYSLVS QQPLGGKAQF GGQRLGEMEV WALEAYGAAH
     TLQELLTVKS DDMSGRVKIY ENIVKGIPTN VSGIPESFNV LMQELRGLGF DLSIYDDKGN
     QIPLTEKEEE LINKT