ID   RPOB_BURPS              Reviewed;        1368 AA.
AC   Q63Q03;
DT   21-FEB-2006, integrated into UniProtKB/Swiss-Prot.
DT   25-OCT-2004, sequence version 1.
DT   03-AUG-2022, entry version 89.
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=BPSL3221;
OS   Burkholderia pseudomallei (strain K96243).
OC   Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC   Burkholderiaceae; Burkholderia; pseudomallei group.
OX   NCBI_TaxID=272560;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=K96243;
RX   PubMed=15377794; DOI=10.1073/pnas.0403302101;
RA   Holden M.T.G., Titball R.W., Peacock S.J., Cerdeno-Tarraga A.-M.,
RA   Atkins T., Crossman L.C., Pitt T., Churcher C., Mungall K.L., Bentley S.D.,
RA   Sebaihia M., Thomson N.R., Bason N., Beacham I.R., Brooks K., Brown K.A.,
RA   Brown N.F., Challis G.L., Cherevach I., Chillingworth T., Cronin A.,
RA   Crossett B., Davis P., DeShazer D., Feltwell T., Fraser A., Hance Z.,
RA   Hauser H., Holroyd S., Jagels K., Keith K.E., Maddison M., Moule S.,
RA   Price C., Quail M.A., Rabbinowitsch E., Rutherford K., Sanders M.,
RA   Simmonds M., Songsivilai S., Stevens K., Tumapa S., Vesaratchavest M.,
RA   Whitehead S., Yeats C., Barrell B.G., Oyston P.C.F., Parkhill J.;
RT   "Genomic plasticity of the causative agent of melioidosis, Burkholderia
RT   pseudomallei.";
RL   Proc. Natl. Acad. Sci. U.S.A. 101:14240-14245(2004).
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; BX571965; CAH37232.1; -; Genomic_DNA.
DR   RefSeq; WP_004198365.1; NZ_CP009538.1.
DR   RefSeq; YP_109815.1; NC_006350.1.
DR   AlphaFoldDB; Q63Q03; -.
DR   SMR; Q63Q03; -.
DR   STRING; 272560.BPSL3221; -.
DR   EnsemblBacteria; CAH37232; CAH37232; BPSL3221.
DR   GeneID; 56594534; -.
DR   KEGG; bps:BPSL3221; -.
DR   PATRIC; fig|272560.51.peg.2017; -.
DR   eggNOG; COG0085; Bacteria.
DR   OMA; FMTWEGY; -.
DR   Proteomes; UP000000605; Chromosome 1.
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; -; 2.
DR   Gene3D; 2.40.50.150; -; 1.
DR   Gene3D; 3.90.1110.10; -; 2.
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..1368
FT                   /note="DNA-directed RNA polymerase subunit beta"
FT                   /id="PRO_0000224038"
SQ   SEQUENCE   1368 AA;  153151 MW;  7EDFD6048DF7CD1A CRC64;
     MQYSFTEKKR IRKSFAKRSI VHQVPFLLAT QLESFSTFLQ ADVPTAQRKS EGLQAAFTSV
     FPIVSHNGFA RLEFVSYALS SPAFNIKECQ QRGLTYCSAL RAKVRLVLLD KESPSKPVVK
     EVKEQEVYMG EIPLMTPTGS FVINGTERVI VSQLHRSPGV FFEHDKGKTH SSGKLLFSAR
     IIPYRGSWLD FEFDPKDVLY FRVDRRRKMP VTILLKAIGL TPEQILANFF VFDNFTLMDE
     GAQMEFVPER LRGEVARFDI TDREGKVIVQ KDKRINAKHI RDLEAAKTKY ISVPEDYLLG
     RVLAKNVVDG DTGEVIANAN DEITEGVLEK LREAKIKEIQ TLYTNDLDQG PYISSTLRVD
     ETVDKTAARI AIYRMMRPGE PPTEEAVEAL FNRLFYSEDA YDLSKVGRMK FNRRVGRDEI
     TGPMTLQDDD ILATIKILVE LRNGKGEVDD IDHLGNRRVR CVGELAENQF RAGLVRVERA
     VKERLGQAES ENLMPHDLIN SKPISSAIRE FFGSSQLSQF MDQTNPLSEI THKRRVSALG
     PGGLTRERAG FEVRDVHPTH YGRVCPIETP EGPNIGLINS LALYAHLNEY GFLETPYRKV
     VDSKVTDQID YLSAIEEGRY MIAQANAAIG DDGALVDELV SSREAGETMM VTPDRIQYMD
     VAPSQIVSVA ASLIPFLEHD DANRALMGSN MQRQAVPCLR PEKPVVGTGI ERTVAVDSGT
     TVQALRGGVV DYVDAGRIVI RVNDDEAVAG EVGVDIYNLI KYTRSNQNTN INQRPIVKMG
     DKVSRGDVLA DGASTDLGEL ALGQNMLIAF MPWNGYNFED SILISERVVA DDRYTSIHIE
     ELNVVARDTK LGPEEITRDI SNLAEVQLGR LDESGIVYIG AEVEAGDVLV GKVTPKGETQ
     LTPEEKLLRA IFGEKASDVK DTSLRVPSGM SGTVIDVQVF TREGIQRDKR AQQIIDDELK
     RYRLDLNDQL RIVEGDAFQR LARMLVGKVA NGGPKKLAKG TKIDQAYLED LDHYHWFDIR
     LADDEAAVQL EAIKNSIEEK RHQFDLAFEE KRKKLTQGDE LPPGVLKMVK VYLAVKRRLQ
     PGDKMAGRHG NKGVVSKIVP VEDMPYMADG RPADVVLNPL GVPSRMNVGQ VLEVHLGWAA
     KGLGWRIGEM LARQTKIEEL RVFLTKIYNE SGRAEDLESF SDDEILELAK NLREGVPFAT
     PVFDGATEEE MSKMLDLAFP DDIAEQLDMN PSKNQVRLYD GRTGEPFERR VTVGYMHYLK
     LHHLVDDKMH ARSTGPYSLV TQQPLGGKAQ FGGQRFGEME VWALEAYGAS YVLQEMLTVK
     SDDVTGRTKV YENLVKGDHV IDAGMPESFN VLVKEIRSLG IDIDLDRN