ID   RPOB_MYCBO              Reviewed;        1178 AA.
AC   P0A681; A0A1R3XW58; O08406; P47766; Q53424; Q59564; Q9X6Q3; Q9X6U9; Q9XC82;
AC   Q9XC83; Q9XC84; Q9XC85; X2BFU0;
DT   15-MAR-2005, integrated into UniProtKB/Swiss-Prot.
DT   15-MAR-2005, sequence version 1.
DT   03-AUG-2022, entry version 96.
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};
GN   OrderedLocusNames=BQ2027_MB0686;
OS   Mycobacterium bovis (strain ATCC BAA-935 / AF2122/97).
OC   Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC   Mycobacterium; Mycobacterium tuberculosis complex.
OX   NCBI_TaxID=233413;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-935 / AF2122/97;
RX   PubMed=12788972; DOI=10.1073/pnas.1130426100;
RA   Garnier T., Eiglmeier K., Camus J.-C., Medina N., Mansoor H., Pryor M.,
RA   Duthoy S., Grondin S., Lacroix C., Monsempe C., Simon S., Harris B.,
RA   Atkin R., Doggett J., Mayes R., Keating L., Wheeler P.R., Parkhill J.,
RA   Barrell B.G., Cole S.T., Gordon S.V., Hewinson R.G.;
RT   "The complete genome sequence of Mycobacterium bovis.";
RL   Proc. Natl. Acad. Sci. U.S.A. 100:7877-7882(2003).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND GENOME REANNOTATION.
RC   STRAIN=ATCC BAA-935 / AF2122/97;
RX   PubMed=28385856; DOI=10.1128/genomea.00157-17;
RA   Malone K.M., Farrell D., Stuber T.P., Schubert O.T., Aebersold R.,
RA   Robbe-Austerman S., Gordon S.V.;
RT   "Updated reference genome sequence and annotation of Mycobacterium bovis
RT   AF2122/97.";
RL   Genome Announc. 5:E00157-E00157(2017).
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}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=SIT99284.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR   EMBL; LT708304; SIT99284.1; ALT_INIT; Genomic_DNA.
DR   RefSeq; NP_854344.1; NC_002945.3.
DR   AlphaFoldDB; P0A681; -.
DR   SMR; P0A681; -.
DR   EnsemblBacteria; SIT99284; SIT99284; BQ2027_MB0686.
DR   PATRIC; fig|233413.5.peg.746; -.
DR   Proteomes; UP000001419; 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; 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..1178
FT                   /note="DNA-directed RNA polymerase subunit beta"
FT                   /id="PRO_0000047928"
FT   REGION          1..37
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        11..36
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1178 AA;  129865 MW;  3DA88DEC6A7DF661 CRC64;
     MLEGCILADS RQSKTAASPS PSRPQSSSNN SVPGAPNRVS FAKLREPLEV PGLLDVQTDS
     FEWLIGSPRW RESAAERGDV NPVGGLEEVL YELSPIEDFS GSMSLSFSDP RFDDVKAPVD
     ECKDKDMTYA APLFVTAEFI NNNTGEIKSQ TVFMGDFPMM TEKGTFIING TERVVVSQLV
     RSPGVYFDET IDKSTDKTLH SVKVIPSRGA WLEFDVDKRD TVGVRIDRKR RQPVTVLLKA
     LGWTSEQIVE RFGFSEIMRS TLEKDNTVGT DEALLDIYRK LRPGEPPTKE SAQTLLENLF
     FKEKRYDLAR VGRYKVNKKL GLHVGEPITS STLTEEDVVA TIEYLVRLHE GQTTMTVPGG
     VEVPVETDDI DHFGNRRLRT VGELIQNQIR VGMSRMERVV RERMTTQDVE AITPQTLINI
     RPVVAAIKEF FGTSQLSQFM DQNNPLSGLT HKRRLSALGP GGLSRERAGL EVRDVHPSHY
     GRMCPIETPE GPNIGLIGSL SVYARVNPFG FIETPYRKVV DGVVSDEIVY LTADEEDRHV
     VAQANSPIDA DGRFVEPRVL VRRKAGEVEY VPSSEVDYMD VSPRQMVSVA TAMIPFLEHD
     DANRALMGAN MQRQAVPLVR SEAPLVGTGM ELRAAIDAGD VVVAEESGVI EEVSADYITV
     MHDNGTRRTY RMRKFARSNH GTCANQCPIV DAGDRVEAGQ VIADGPCTDD GEMALGKNLL
     VAIMPWEGHN YEDAIILSNR LVEEDVLTSI HIEEHEIDAR DTKLGAEEIT RDIPNISDEV
     LADLDERGIV RIGAEVRDGD ILVGKVTPKG ETELTPEERL LRAIFGEKAR EVRDTSLKVP
     HGESGKVIGI RVFSREDEDE LPAGVNELVR VYVAQKRKIS DGDKLAGRHG NKGVIGKILP
     VEDMPFLADG TPVDIILNTH GVPRRMNIGQ ILETHLGWCA HSGWKVDAAK GVPDWAARLP
     DELLEAQPNA IVSTPVFDGA QEAELQGLLS CTLPNRDGDV LVDADGKAML FDGRSGEPFP
     YPVTVGYMYI MKLHHLVDDK IHARSTGPYS MITQQPLGGK AQFGGQRFGE MECWAMQAYG
     AAYTLQELLT IKSDDTVGRV KVYEAIVKGE NIPEPGIPES FKVLLKELQS LCLNVEVLSS
     DGAAIELREG EDEDLERAAA NLGINLSRNE SASVEDLA