ID   RPOB_TROWH              Reviewed;        1157 AA.
AC   P59643;
DT   23-APR-2003, integrated into UniProtKB/Swiss-Prot.
DT   23-APR-2003, sequence version 1.
DT   03-AUG-2022, entry version 80.
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};
OS   Tropheryma whipplei (Whipple's bacillus) (Tropheryma whippelii).
OC   Bacteria; Actinobacteria; Micrococcales; Tropherymataceae; Tropheryma.
OX   NCBI_TaxID=2039;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA   Maiwald M., Lepp P.W., Relman D.A.;
RT   "Analysis of conserved non-rRNA genes of Tropheryma whipplei: implications
RT   for genome structure, strain typing, and phylogenetic relationships.";
RL   Submitted (FEB-2002) 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; AF483653; AAO84493.1; -; Genomic_DNA.
DR   AlphaFoldDB; P59643; -.
DR   SMR; P59643; -.
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; 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..1157
FT                   /note="DNA-directed RNA polymerase subunit beta"
FT                   /id="PRO_0000047989"
SQ   SEQUENCE   1157 AA;  127924 MW;  895CE73845FD1B50 CRC64;
     MSLFGVGFLA FAKGKRVCAI GRSSLGKISD PLEVPNLLDL QLDSFDWLIG GPRWRAALDA
     YRKNPSGAPI AEKSGLDEVF DEISPIEDSA GNMQLNFSKP VLEAEELSVR ECRVRGRTYS
     APLYVEAEFM NHDTGEIKTQ TVFMGDFPLM TDKGTFVING TERVVVSQLV RSPGVYFERT
     PEKNSEKDLF SGRIIPARGA WLEFEVDRHD QLGVRVDRKR RQPVIFFLRA IGMTDDEIRD
     AFGEFESISV QHEKNIGLSR DDALREIYRR VRPGEQASAE AGRALLENFY FTSRRFDLAR
     VGRYKVNRKL GVDVDPTRMV LTRSDIIATI RYLAALHLGF SEVAVLNSNK SVPISTDDID
     HLGNRRIRPV GELVQNQLRA GLARMERVVR ERMTTQDIEA IIPQTLINVM PIVAALKEFY
     GTSQLSQFMD QNNPLAGLTH KRRLSALGPG GLSRERAGVE VRDVNPSHYG RMCPIETPEG
     PNIGLIGSLA CYSRVNSFGF IETPYRRVVN GKVTDDIEYM TATQEDEHAI AQASTPLRPD
     NSFVDERVLV RRKGGEVEVV PADQVDYMDV SGRQMVSVAT SLIPFLEHND ANRALMGSNM
     QRQAVPLLVT ESPLVGTGME RYVAIDAGDV LIAEDPGIVG DVSADVVTVK QDDGKHRDYH
     VGKFVRSNQG NCYNQRVVVR SGDRVEKGTV LADGPCTDKG ELSLGRNLLV AFMPWEGYNF
     EDAIIISQNL VKDDTLSSIH IEEHEVSTRD TKLGSEEITR DLPNVSMDYI KDLDERGIIR
     IGAEVGPGDI LVGKVTPKGE TELSAEERLL RAIFNEKSME VRDTSLKVPH GQQGTVIDVK
     LFDAVDGEDK LGAGINQRVV VYIAHKRKIT EGDKLAGRHG NKGVISKILP VEDMPFMADG
     TPVDIILNPL GVPARMNFGQ VLETHLGWIS KQGWKIEGDP DWAKDIRVRE AQPDSRVSSP
     VFDGISEGEI TGLFSSVFPN RDGERAVGSD GKAILYDGRT GEPFPEPISV GYMYVLKLHH
     LVDDKIHARS TGPYSMIIQQ PLGGKAQFGG QRFGEMEVWA LEAYGAAHAL QELLTIKSDD
     VVGRVKVYDA IVKGYPIPTP GVPESFKVIV KEMQSLCINI EVVSDGEDDV SADAETLQIE
     EGLDTSPKVE VGSLEEV