RPOB_BORA1
ID RPOB_BORA1 Reviewed; 1370 AA.
AC Q2L2M3;
DT 30-MAY-2006, integrated into UniProtKB/Swiss-Prot.
DT 11-SEP-2007, sequence version 2.
DT 03-AUG-2022, entry version 88.
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=BAV0013;
OS Bordetella avium (strain 197N).
OC Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC Alcaligenaceae; Bordetella.
OX NCBI_TaxID=360910;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=197N;
RX PubMed=16885469; DOI=10.1128/jb.01927-05;
RA Sebaihia M., Preston A., Maskell D.J., Kuzmiak H., Connell T.D., King N.D.,
RA Orndorff P.E., Miyamoto D.M., Thomson N.R., Harris D., Goble A., Lord A.,
RA Murphy L., Quail M.A., Rutter S., Squares R., Squares S., Woodward J.,
RA Parkhill J., Temple L.M.;
RT "Comparison of the genome sequence of the poultry pathogen Bordetella avium
RT with those of B. bronchiseptica, B. pertussis, and B. parapertussis reveals
RT extensive diversity in surface structures associated with host
RT interaction.";
RL J. Bacteriol. 188:6002-6015(2006).
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=CAJ47597.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AM167904; CAJ47597.1; ALT_INIT; Genomic_DNA.
DR RefSeq; WP_039052216.1; NC_010645.1.
DR AlphaFoldDB; Q2L2M3; -.
DR SMR; Q2L2M3; -.
DR STRING; 360910.BAV0013; -.
DR PRIDE; Q2L2M3; -.
DR EnsemblBacteria; CAJ47597; CAJ47597; BAV0013.
DR GeneID; 41391942; -.
DR KEGG; bav:BAV0013; -.
DR eggNOG; COG0085; Bacteria.
DR HOGENOM; CLU_000524_4_3_4; -.
DR OrthoDB; 9601at2; -.
DR Proteomes; UP000001977; 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_0000237298"
SQ SEQUENCE 1370 AA; 153500 MW; 61FF2659AAB6B874 CRC64;
MPYSYTEKKR IRKSFAKRED VQNVPFLLAT QLQSYLTFLQ AETATADRVN EGLQAAFTSI
FPIVSHNGMA RLEFVSYALG EPVFDVKECQ QRGLTYASPL RAKVRLVLLD REVSKPTIKE
VKEQEVYMGE IPLMTTTGSF VINGTERVIV SQLHRSPGVF FEHDRGKTHS SGKLLFSARV
IPYRGSWLDF EFDPKDVLFF RVDRRRKMPV TILLKAIGMT PESILAHFFD FDNFELKSEG
AMMEFVPERW KGEMARFDIT DRAGKVIVEK DKRINAKHLR DLANGGIQRI SVPEDFLYGR
VLAKNVVDPD TGEVIALAND EITESVLDAM RAAKVLDLQT LYTNDLDRGP YISQTLRTDE
TVDQTAARVA IYRMMRPGEP PTEEAVEALF QRLFYSEETY DLSRVGRMKV NSRLGRGDDA
NGPMTLTDED ILETIKVLVE LRNGRGQIDD IDHLGNRRVR CVGELAENQF RAGLVRVERA
VKERLGQAET ENLMPHDLIN SKPISAAIKE FFGSSQLSQF MDQTNPLSEI THKRRVSALG
PGGLTRERAG FEVRDVHPTH YGRVCPIETP EGPNIGLINS MALYARLNEY GFLETPYRKI
IDGRVSDQID YLSAIEESHY VIAQANAALD AEGRFVDDLV ACREAGETML TSPVNVHYMD
VAPSQIVSVA ASLIPFLEHD DANRALMGAN MQRQAVPCLR PEKPLVGTGI ERTVAVDSGT
TVQALRGGLV DHVDAERVVI RVNDEENVAG EVGVDIYNLI KYTRSNQNTN INQRPIVKRG
DRVAKGDVLA DGASTDLGEL ALGQNMLIAF MPWNGYNFED SILISERVVA DDRYTSVHIE
ELTVVARDTK LGPEEITRDI SNLAETQLNR LDESGIVYIG AEVSADDVLV GKVTPKGETQ
LTPEEKLLRA IFGEKASDVK DTSLRVPSGM TGTVIDVQVF TREGIVRDKR AQSIIDDELR
RYRQDLNDQL RIVENDQFDR IEKLLVGKTV NGGPRKLAKG ATVTKAYLAD LDRWQWFDIR
LSDEPHAVVL EQAKESLEQK RHQFDLAFEE KRKKLTQGDE LPPGVLKMIK VYLAVKRRLQ
PGDKMAGRHG NKGVVSRITP VEDMPHMADG TTADIVLNPL GVPSRMNVGQ VLEVHLGWAA
KGVGQRIADM LQDERTAQVK NIRAYLEKVY NTTGTGARIS ELSDEEVIEL ANNLKRGVPF
ATPVFDGATE DEITMMLELA YPDDVAKRMQ LTPSRAQAWL FDGRTGEKFE RPVTIGYMHY
LKLHHLVDDK MHARSTGPYS LVTQQPLGGK AQFGGQRFGE MEVWALEAYG ASYTLQEMLT
VKSDDITGRT KVYENIVKGD HVIDAGMPES FNVLVKEIRS LALDMDLERN