RPOB_BORBZ
ID RPOB_BORBZ Reviewed; 1155 AA.
AC B7J1W1;
DT 14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT 10-FEB-2009, sequence version 1.
DT 03-AUG-2022, entry version 73.
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=BbuZS7_0391;
OS Borreliella burgdorferi (strain ZS7) (Borrelia burgdorferi).
OC Bacteria; Spirochaetes; Spirochaetales; Borreliaceae; Borreliella.
OX NCBI_TaxID=445985;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ZS7;
RX PubMed=20935092; DOI=10.1128/jb.01158-10;
RA Schutzer S.E., Fraser-Liggett C.M., Casjens S.R., Qiu W.G., Dunn J.J.,
RA Mongodin E.F., Luft B.J.;
RT "Whole-genome sequences of thirteen isolates of Borrelia burgdorferi.";
RL J. Bacteriol. 193:1018-1020(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; CP001205; ACK74701.1; -; Genomic_DNA.
DR RefSeq; WP_002657846.1; NC_011728.1.
DR AlphaFoldDB; B7J1W1; -.
DR SMR; B7J1W1; -.
DR EnsemblBacteria; ACK74701; ACK74701; BbuZS7_0391.
DR GeneID; 56567817; -.
DR KEGG; bbz:BbuZS7_0391; -.
DR HOGENOM; CLU_000524_4_1_12; -.
DR OMA; FMTWEGY; -.
DR OrthoDB; 9601at2; -.
DR Proteomes; UP000006901; 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; Transcription;
KW Transferase.
FT CHAIN 1..1155
FT /note="DNA-directed RNA polymerase subunit beta"
FT /id="PRO_1000141662"
SQ SEQUENCE 1155 AA; 129685 MW; 6D7DBC0E01A1FBF8 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 VDFDGYDDIS GKRFVSSNVI LNCLEKEDAF
FALKDGSKEL PKESVMLAVY SSLFPGEPIS IDNAENDLKT IFFSERRYDL GRVGRYKLSK
KFGFDDLTTS VLTMDDIVNT ISHLLRIYEG HDILDDIDHL GNRRVRSVGE LLTNIYKGAM
SRVEKIAKDR MSNKEVFNLK PQELISVKPI VSAVKEFFAT SQLSQFMDQV NPLAELTHKR
RLNALGPGGL SRDRAGFEVR DVHYTHYGRM CPIETPEGPN IGLIVSLATY SRVNDYGFLE
TPYRKVVNGE 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