ID   RPOB_BORRA              Reviewed;        1155 AA.
AC   B5RRJ7;
DT   14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT   04-NOV-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=BRE_387;
OS   Borrelia recurrentis (strain A1).
OC   Bacteria; Spirochaetes; Spirochaetales; Borreliaceae; Borrelia.
OX   NCBI_TaxID=412418;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=A1;
RX   PubMed=18787695; DOI=10.1371/journal.pgen.1000185;
RA   Lescot M., Audic S., Robert C., Nguyen T.T., Blanc G., Cutler S.J.,
RA   Wincker P., Couloux A., Claverie J.-M., Raoult D., Drancourt M.;
RT   "The genome of Borrelia recurrentis, the agent of deadly louse-borne
RT   relapsing fever, is a degraded subset of tick-borne Borrelia duttonii.";
RL   PLoS Genet. 4:E1000185-E1000185(2008).
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; CP000993; ACH94631.1; -; Genomic_DNA.
DR   RefSeq; WP_012538867.1; NC_011244.1.
DR   AlphaFoldDB; B5RRJ7; -.
DR   SMR; B5RRJ7; -.
DR   EnsemblBacteria; ACH94631; ACH94631; BRE_387.
DR   KEGG; bre:BRE_387; -.
DR   HOGENOM; CLU_000524_4_3_12; -.
DR   OMA; FMTWEGY; -.
DR   OrthoDB; 9601at2; -.
DR   Proteomes; UP000000612; 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; 1.
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_1000141666"
SQ   SEQUENCE   1155 AA;  130087 MW;  591E70C71E18D27C CRC64;
     MIKRVHLGQG KAEEILNLPN LIEIQLNSYE KFLQLERLKN NKPLLNEGLE SVFRDVFPMK
     SSNGEVALEY EKYYIEYDSI SFTEKECKRK GQSYEAVLKI RLNLQFLTTG EIRQKDVYMG
     TIPLMTDRGT FIVNGAERVI VSQIHRSPGV VFYKEKDLYY ARIIPYRGSW LEFEIDSKKD
     YLYVKIDRKK RILVTLFLRA LGLDTREKII ETFYKIRKIE VNDDTKREIT GQYLATNITI
     KENMTYRAGD KITLQDIEDF LQNGVKEINL IDFDGYDSVP GKHFISSDVI LNCFEKEDAY
     FALKDGFKEL SRESVMLAVY SVLLPGEPIS IDNAENDLRT IFFSEKRYDL GHVGRYKLSK
     KFGLDDLTTS VLTMTDIVNT ISHLLRIYDG HDVLDDIDHL GNRRVRSVGE LLTNIYKGAM
     SRVEKIAKDR MSNKEVFNLK PQELISVKPV VSAVKEFFAT SQLSQFMDQV NPLAELTHKR
     RLNALGPGGL SRDRAGFEVR DVHYTHYGRM CPIETPEGPN IGLIVSLATY SKVNDYGFLE
     TPYRKVIDGK VTDDIEYLSA IDEEKKCIAQ ANASVSSDGN YTDDLVSVRI SGDYTTMMPK
     NIDYMDVSPR QLISVSSALI PFLEHNDANR ALMGSNMQRQ AVPLLFPQPP IVGTGMERIV
     AKDSGVVIKA KRPGRVVLAT NKKIVIKPDN ATSERDLDEY ELYKYERTNQ DTSFNHSVLV
     KNGQIVNKDE IIADGPATRY GELALGNNLL VGFIPWNGFN YEDAILISER IVKEDLYTSI
     HIKEFSIEVR ETKLGPEKVT ADIPNVSGKI LSKLDENGIV RIGTYVKPGD ILIGKVTPKS
     EGDITPEFKL LTSIFGEKAK DVKNNSLKVP HGTEGTVIDV QRITKDDVGN LPPGVDEILK
     VYIAKKRKLK EGDKMAGRHG NKGVVAKILP VEDMPYLADG TPLDICLNPL GVPSRMNIGQ
     LMESQLGLAG KYLGEYYDVP VFESATNECI QEKLKKAGFN ETSKAVLYDG YTGEPFENEV
     MVGVIYMLKL HHLVDDKMHA RSTGPYSLVS QQPLGGKAQF GGQRLGEMEV WALEAYGAAH
     TLQELLTVKS DDMSGRVKIY ENIVKGIPTN VSGIPESFNV LMQELRGLGF DLSIYDDNGN
     QIPLTEKEEE LINKT