RPOB_BACFR
ID RPOB_BACFR Reviewed; 1270 AA.
AC Q64NJ7;
DT 21-FEB-2006, integrated into UniProtKB/Swiss-Prot.
DT 25-OCT-2004, sequence version 1.
DT 03-AUG-2022, entry version 92.
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=BF4192;
OS Bacteroides fragilis (strain YCH46).
OC Bacteria; Bacteroidetes; Bacteroidia; Bacteroidales; Bacteroidaceae;
OC Bacteroides.
OX NCBI_TaxID=295405;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=YCH46;
RX PubMed=15466707; DOI=10.1073/pnas.0404172101;
RA Kuwahara T., Yamashita A., Hirakawa H., Nakayama H., Toh H., Okada N.,
RA Kuhara S., Hattori M., Hayashi T., Ohnishi Y.;
RT "Genomic analysis of Bacteroides fragilis reveals extensive DNA inversions
RT regulating cell surface adaptation.";
RL Proc. Natl. Acad. Sci. U.S.A. 101:14919-14924(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; AP006841; BAD50935.1; -; Genomic_DNA.
DR RefSeq; WP_005791521.1; NZ_UYXF01000007.1.
DR RefSeq; YP_101469.1; NC_006347.1.
DR AlphaFoldDB; Q64NJ7; -.
DR SMR; Q64NJ7; -.
DR STRING; 295405.BF4192; -.
DR EnsemblBacteria; BAD50935; BAD50935; BF4192.
DR GeneID; 66331185; -.
DR KEGG; bfr:BF4192; -.
DR PATRIC; fig|295405.11.peg.4047; -.
DR HOGENOM; CLU_000524_4_1_10; -.
DR OMA; FMTWEGY; -.
DR Proteomes; UP000002197; 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; -; 3.
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..1270
FT /note="DNA-directed RNA polymerase subunit beta"
FT /id="PRO_0000224030"
SQ SEQUENCE 1270 AA; 142454 MW; 3B625FF19595460D CRC64;
MSSNTVNQRV NFASTKNPLE YPDFLEVQLK SFQDFLQLDT PPEKRKKEGL YKVFAENFPI
ADTRNNFVLE FLDYYIDPPR YTIDDCIERG LTYSVPLKAK LKLYCTDPDH EDFDTVIQDV
FLGPIPYMTD KATFVINGAE RVVVSQLHRS PGVFFGQSVH ANGTKLYSAR IIPFKGSWIE
FATDINNVMY AYIDRKKKLP VTTLLRAIGF ENDKDILEIF NLAEDVKVNK TNLKKVVGRK
LAARVLKTWI EDFVDEDTGE VVSIERNEVI IDRETVIEPE HIDEIIDSGV QNILIHKEEP
NQSDYSIIYN TLQKDPSNSE KEAVLYIYRQ LRNADPADDA SAREVINNLF FSEKRYDLGD
VGRYRINKKL NLTTDMDVRV LTKEDIIEII KYLIELINSK ADVDDIDHLS NRRVRTVGEQ
LSNQFAVGLA RMSRTIRERM NVRDNEVFTP IDLINAKTIS SVINSFFGTN ALSQFMDQTN
PLAEITHKRR MSALGPGGLS RERAGFEVRD VHYTHYGRLC PIETPEGPNI GLISSLCVFA
KINDLGFIET PYRKVDNGKV DLSENGLVYL TAEEEEAKII AQGNAPLNDD GTFIRNKVKS
RQDADYPVVE PSEVELMDVA PQQIASIAAS LIPFLEHDDA NRALMGSNMM RQAVPLLRSE
APIVGTGIER QLVRDSRTQI AAEGDGVIDF VDATTIRILY DRTEDEEFVS FEPALKEYRI
PKFRKTNQNM TIDLRPTCNK GDRVTKGQIL TEGYSTENGE LALGKNLLVA YMPWKGYNYE
DAIVLNERVV REDLLTSVHV EEYSLEVRET KRGMEELTSD IPNVSEEATK DLDENGIVRV
GARIQPGDIL IGKITPKGES DPSPEEKLLR AIFGDKAGDV KDASLKASPS LKGVIIDKKL
FSRVIKNRSS KLADKALLPK IDDEFESKVA DLKRILVKKL MVLTEGKVSQ GVKDYLGAEV
IAKGSKFSAS DFDSLDFTAI QLSDWTNDDH ANGMIRDLIL NFIKKYKELD AELKRKKFAI
TIGDELPAGI IQMAKVYIAK KRKIGVGDKM AGRHGNKGIV SRVVRQEDMP FLEDGTPVDI
VLNPLGVPSR MNIGQIFEAV LGRAGKNLGV KFATPIFDGA TLDDLNEWTD KAGLPRYCKT
YLCDGGTGER FDQPATVGVT YMLKLGHMVE DKMHARSIGP YSLITQQPLG GKAQFGGQRF
GEMEVWALEG FGASHILQEI LTIKSDDVVG RSKAYEAIVK GEPMPQPGIP ESLNVLLHEL
RGLGLSINLE
