ID   RPOB_BORBR              Reviewed;        1370 AA.
AC   Q7WRD9;
DT   16-JAN-2004, integrated into UniProtKB/Swiss-Prot.
DT   11-SEP-2007, sequence version 2.
DT   03-AUG-2022, entry version 98.
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=BB0014;
OS   Bordetella bronchiseptica (strain ATCC BAA-588 / NCTC 13252 / RB50)
OS   (Alcaligenes bronchisepticus).
OC   Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC   Alcaligenaceae; Bordetella.
OX   NCBI_TaxID=257310;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-588 / NCTC 13252 / RB50;
RX   PubMed=12910271; DOI=10.1038/ng1227;
RA   Parkhill J., Sebaihia M., Preston A., Murphy L.D., Thomson N.R.,
RA   Harris D.E., Holden M.T.G., Churcher C.M., Bentley S.D., Mungall K.L.,
RA   Cerdeno-Tarraga A.-M., Temple L., James K.D., Harris B., Quail M.A.,
RA   Achtman M., Atkin R., Baker S., Basham D., Bason N., Cherevach I.,
RA   Chillingworth T., Collins M., Cronin A., Davis P., Doggett J., Feltwell T.,
RA   Goble A., Hamlin N., Hauser H., Holroyd S., Jagels K., Leather S.,
RA   Moule S., Norberczak H., O'Neil S., Ormond D., Price C., Rabbinowitsch E.,
RA   Rutter S., Sanders M., Saunders D., Seeger K., Sharp S., Simmonds M.,
RA   Skelton J., Squares R., Squares S., Stevens K., Unwin L., Whitehead S.,
RA   Barrell B.G., Maskell D.J.;
RT   "Comparative analysis of the genome sequences of Bordetella pertussis,
RT   Bordetella parapertussis and Bordetella bronchiseptica.";
RL   Nat. Genet. 35:32-40(2003).
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=CAE30516.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR   EMBL; BX640437; CAE30516.1; ALT_INIT; Genomic_DNA.
DR   RefSeq; WP_033447220.1; NC_002927.3.
DR   AlphaFoldDB; Q7WRD9; -.
DR   SMR; Q7WRD9; -.
DR   STRING; 257310.BB0014; -.
DR   EnsemblBacteria; CAE30516; CAE30516; BB0014.
DR   GeneID; 56481303; -.
DR   KEGG; bbr:BB0014; -.
DR   eggNOG; COG0085; Bacteria.
DR   HOGENOM; CLU_000524_4_3_4; -.
DR   OrthoDB; 9601at2; -.
DR   Proteomes; UP000001027; 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..1370
FT                   /note="DNA-directed RNA polymerase subunit beta"
FT                   /id="PRO_0000047865"
SQ   SEQUENCE   1370 AA;  153123 MW;  7FB880D738ECFDCC CRC64;
     MPYSYTEKKR IRKSFAKRED VQNVPFLLAT QLQSYLTFLQ ADTATSDRVN EGLQAAFSSI
     FPIVSHNGMA RLEFVSYALG EPVFDVKECQ QRGLTYASPL RAKVRLVLLD REVSKPTIKE
     VKEQEVYMGE IPLMTGTGSF VINGTERVIV SQLHRSPGVF FEHDRGKTHS SGKLLFSARV
     IPYRGSWLDF EFDPKDVLFF RVDRRRKMPV TILLKAIGMT PESILAHFFD FDNFELKSEG
     GMMEFVAERW KGEMARFDIA DRDGKVIVEK DKRINAKHLR DLAAGGIQRV SVPEDFLYGR
     VLAKNIVDPD TGEVVAHAND EITESVLNAM RAANVRDIQT LYTNDLDRGP YISQTLRADE
     TADQMAARVA IYRMMRPGEP PTEEAVEALF QRLFYSEETY DLSRVGRMKV NSRLGRGDDS
     TGPMTLTNED ILETIKVLVE LRNGRGQIDD IDHLGNRRVR CVGELAENQF RAGLVRVERA
     VKERLGQAET ENLMPHDLIN SKPISAAIKE FFGSSQLSQF MDQTNPLSEI THKRRVSALG
     PGGLTRERAG FEVRDVHPTH YGRVCPIETP EGPNIGLINS MALYARLNEY GFLETPYRKI
     IDGKVSDQID YLSAIEESHY VIAQANAALD DEGRFVDDLV ACREAGETML TAPGNVHYMD
     VAPSQIVSVA ASLIPFLEHD DANRALMGAN MQRQAVPCLR PEKPLVGTGV ERTVAVDSGT
     TVQALRGGVV DHVDADRVVI RVNDEENVAG EVGVDIYNLI KYTRSNQNTN INQRPIVARG
     DKVAKGDVLA DGASTDLGEL ALGQNMLIAF MPWNGYNFED SILISERVVA DDRYTSIHIE
     ELTVVARDTK LGPEEITRDI SNLAETQLNR LDDSGIVYIG AEVSADDVLV GKVTPKGETQ
     LTPEEKLLRA IFGEKASDVK DTSLRVPSGM TGTVIDVQVF TREGIVRDKR AQSIIDDELR
     RYRQDLNDQL RIVENDQFDR IEKMLVGKAV NGGPRKLAKG ATLTKAYLAD LDRWQWFDIR
     LADEQHAVVL EQAKESLEQK RHQFDLAFEE KRKKLTQGDE LPPGVLKMIK VYLAVKRRLQ
     PGDKMAGRHG NKGVVSRITP VEDMPHMADG TPADIVLNPL GVPSRMNVGQ VLEVHLGWAA
     KGVGYRIADM LRDERTAQAK SVRGYLEKVY NTTGSSAHID SLTDEEVLEL ANNLKKGVPF
     ATPVFDGATE EEIGKMLELA YPDDVAARMR LTASRSQAWL YDGRTGEQFE RPVTIGYMHY
     LKLHHLVDDK MHARSTGPYS LVTQQPLGGK AQFGGQRFGE MEVWALEAYG ASYTLQEMLT
     VKSDDITGRT KVYENIVKGD HVIDAGMPES FNVLVKEIRS LALDMDLERN