ID   RPOB_BORPD              Reviewed;        1370 AA.
AC   A9IJ25;
DT   14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT   05-FEB-2008, sequence version 1.
DT   03-AUG-2022, entry version 77.
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=Bpet4965;
OS   Bordetella petrii (strain ATCC BAA-461 / DSM 12804 / CCUG 43448).
OC   Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC   Alcaligenaceae; Bordetella.
OX   NCBI_TaxID=340100;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-461 / DSM 12804 / CCUG 43448;
RX   PubMed=18826580; DOI=10.1186/1471-2164-9-449;
RA   Gross R., Guzman C.A., Sebaihia M., Martin dos Santos V.A.P., Pieper D.H.,
RA   Koebnik R., Lechner M., Bartels D., Buhrmester J., Choudhuri J.V.,
RA   Ebensen T., Gaigalat L., Herrmann S., Khachane A.N., Larisch C., Link S.,
RA   Linke B., Meyer F., Mormann S., Nakunst D., Rueckert C.,
RA   Schneiker-Bekel S., Schulze K., Voerholter F.-J., Yevsa T., Engle J.T.,
RA   Goldman W.E., Puehler A., Goebel U.B., Goesmann A., Bloecker H., Kaiser O.,
RA   Martinez-Arias R.;
RT   "The missing link: Bordetella petrii is endowed with both the metabolic
RT   versatility of environmental bacteria and virulence traits of pathogenic
RT   Bordetellae.";
RL   BMC Genomics 9:449-449(2008).
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; AM902716; CAP45317.1; -; Genomic_DNA.
DR   AlphaFoldDB; A9IJ25; -.
DR   SMR; A9IJ25; -.
DR   STRING; 94624.Bpet4965; -.
DR   EnsemblBacteria; CAP45317; CAP45317; Bpet4965.
DR   KEGG; bpt:Bpet4965; -.
DR   eggNOG; COG0085; Bacteria.
DR   OMA; FMTWEGY; -.
DR   Proteomes; UP000001225; 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; Reference proteome;
KW   Transcription; Transferase.
FT   CHAIN           1..1370
FT                   /note="DNA-directed RNA polymerase subunit beta"
FT                   /id="PRO_1000141665"
SQ   SEQUENCE   1370 AA;  153390 MW;  5CC500890AD7201A CRC64;
     MPYSYTEKKR IRKSFAKRED VQDVPFLLAT QLQSYLTFLQ ADTPPSDRAS EGLQAAFSSI
     FPIVSHNGMA RLEFVSYVLG EPVFDVKECQ QRGLTYASPL RAKVRLVLLD REVSKPTIKE
     VKEQEVYMGE IPLMTGTGSF VINGTERVIV SQLHRSPGVF FEHDRGKTHS SGKLLFSARV
     IPYRGSWLDF EFDPKDVLFF RVDRRRKMPV TILLKAIGMT PESILAHFFD FDNFELKSEG
     GMIEFVPERW KGEMARFDIT GRDGNVIVEK DKRINAKHLR DMANANIQRV SVPEEFLYGR
     VLAKNIVDPD TGEVVAHAND EITESVLSAL RAANVRDIQT LYTNDLDRGP YISQTLRTDE
     TADQMAARVA IYRMMRPGEP PTEDAVEALF QRLFYSEETY DLSRVGRMKV NSRLGRGEDI
     TGPMTLTNED ILETIKVLVE LRNGRGQIDD IDHLGNRRVR CVGELAENQF RAGLVRVERA
     VKERLGQAET ENLMPHDLIN SKPISAAIKE FFGSSQLSQF MDQTNPLSEI THKRRVSALG
     PGGLTRERAG FEVRDVHPTH YGRVCPIETP EGPNIGLINS MALYARLNEY GFLETPYRKI
     IDGKVSDQID YLSAIEESNY VIAQANAALD DEGRFVDDLV ACREAGETML TAPANVHYMD
     VAPSQIVSVA ASLIPFLEHD DANRALMGAN MQRQAVPCLR PEKPVVGTGV ERTVAVDSGT
     TVQALRGGVV DHVDAERVVI RVNDDENVAG EVGVDIYNLI KYTRSNQNTN INQRPIVKRG
     DKVAKGDVLA DGASTDLGEL ALGQNMLIAF MPWNGYNFED SILISEKVVA DDRYTSIHIE
     ELTVVARDTK LGPEEITRDI SNLAETQLNR LDDSGIVYIG AEVTADDVLV GKVTPKGETQ
     LTPEEKLLRA IFGEKASDVK DTSLRVPSGM VGTVIDVQVF TREGIVRDKR AQSIIDDELR
     RYRQDLNDQL RIVENDQFDR IEKLLIGKTV NGGPRKLAKG ATITKAYLAD LDRWQWFDIR
     LADEPHAVVL EQAKESLEQK RHQFDLAFEE KRKKLTQGDE LPPGVLKMIK VYLAVKRRLQ
     PGDKMAGRHG NKGVVSRITP VEDMPHMADG TPADIVLNPL GVPSRMNVGQ VLEVHLGWAA
     KGVGHRIADM LRDERTAQVK NVRAYLDKVY NTTGTGEQID TLTDDEVMEL AQNLKNGVPF
     ATPVFDGATE EEIGKMLELA YPDEVAKRMQ LTDSRTQAWL FDGRTGEKFE RPVTVGYMHY
     LKLHHLVDDK MHARSTGPYS LVTQQPLGGK AQFGGQRFGE MEVWALEAYG AAYTLQEMLT
     VKSDDITGRT KVYENIVKGD HVIDAGMPES FNVLVKEIRS LALDMDLERN