ID   RPOB_BURCJ              Reviewed;        1368 AA.
AC   B4E5B2;
DT   14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT   23-SEP-2008, sequence version 1.
DT   03-AUG-2022, entry version 80.
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=BceJ2315_02290; ORFNames=BCAL0226;
OS   Burkholderia cenocepacia (strain ATCC BAA-245 / DSM 16553 / LMG 16656 /
OS   NCTC 13227 / J2315 / CF5610) (Burkholderia cepacia (strain J2315)).
OC   Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC   Burkholderiaceae; Burkholderia; Burkholderia cepacia complex.
OX   NCBI_TaxID=216591;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-245 / DSM 16553 / LMG 16656 / NCTC 13227 / J2315 / CF5610;
RX   PubMed=18931103; DOI=10.1128/jb.01230-08;
RA   Holden M.T., Seth-Smith H.M., Crossman L.C., Sebaihia M., Bentley S.D.,
RA   Cerdeno-Tarraga A.M., Thomson N.R., Bason N., Quail M.A., Sharp S.,
RA   Cherevach I., Churcher C., Goodhead I., Hauser H., Holroyd N., Mungall K.,
RA   Scott P., Walker D., White B., Rose H., Iversen P., Mil-Homens D.,
RA   Rocha E.P., Fialho A.M., Baldwin A., Dowson C., Barrell B.G., Govan J.R.,
RA   Vandamme P., Hart C.A., Mahenthiralingam E., Parkhill J.;
RT   "The genome of Burkholderia cenocepacia J2315, an epidemic pathogen of
RT   cystic fibrosis patients.";
RL   J. Bacteriol. 191:261-277(2009).
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; AM747720; CAR50537.1; -; Genomic_DNA.
DR   RefSeq; WP_012492293.1; NC_011000.1.
DR   AlphaFoldDB; B4E5B2; -.
DR   SMR; B4E5B2; -.
DR   STRING; 216591.BCAL0226; -.
DR   EnsemblBacteria; CAR50537; CAR50537; BCAL0226.
DR   KEGG; bcj:BCAL0226; -.
DR   eggNOG; COG0085; Bacteria.
DR   HOGENOM; CLU_000524_4_0_4; -.
DR   OMA; FMTWEGY; -.
DR   OrthoDB; 9601at2; -.
DR   BioCyc; BCEN216591:G1G1V-268-MON; -.
DR   Proteomes; UP000001035; 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; -; 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..1368
FT                   /note="DNA-directed RNA polymerase subunit beta"
FT                   /id="PRO_1000141670"
SQ   SEQUENCE   1368 AA;  153242 MW;  957B0A026880A180 CRC64;
     MQYSFTEKKR IRKSFAKRPI VHQVPFLLAT QLESFSTFLQ ADVPATQRKP EGLQAAFTSV
     FPIVSHNGFA RLEFVSYALS SPAFNIKECQ QRGLTYCSAL RAKVRLVILD KESPNKPVVK
     EVKEQEVYMG EIPLMTPTGS FVINGTERVI VSQLHRSPGV FFEHDKGKTH SSGKLLFSAR
     IIPYRGSWLD FEFDPKDILY FRVDRRRKMP VTILLKAIGL TPEQILANFF VFDNFTLMDE
     GAQLEFVPER LRGEVARFDI TDRDGKVIVQ KDKRINAKHI RDLEAAKTKF ISVPEDYLLG
     RVLAKNVVDG DTGEVIASAN DEVTESVLEK LREAGIKDIQ TLYTNDLDQG PYISSTLRVD
     ETTDKTAARI AIHRMMRPGE PPTEEAVEAL FNRLFYSEEA YDLSKVGRMK FNRRVGRDEI
     VGPMTLQDDD ILATIKILVE LRNGKGEVDD IDHLGNRRVR CVGELAENQF RAGLVRVERA
     VKERLGQAES ENLMPHDLIN SKPISSAIRE FFGSSQLSQF MDQTNPLSEI THKRRVSALG
     PGGLTRERAG FEVRDVHPTH YGRVCPIETP EGPNIGLINS LALYAHLNEY GFLETPYRKV
     VDSKVTDQID YLSAIEEGRY MIAQANAAID EDGRLIDELV SSREAGETMM VTPDRIQYMD
     VAPSQIVSVA ASLIPFLEHD DANRALMGSN MQRQAVPCLR PEKPVVGTGI ERTCAVDSGT
     TVQAFRGGVV DYVDAGRIVI RVNDDEAVAG EVGVDIYNLI KYTRSNQNTN INQRPIVKMG
     DKVSRGDVLA DGASTDLGEL ALGQNMLIAF MPWNGYNFED SILISEKVVA DDRYTSIHIE
     ELNVVARDTK LGPEEITRDI SNLAEVQLGR LDESGIVYIG AEVEAGDVLV GKVTPKGETQ
     LTPEEKLLRA IFGEKASDVK DTSLRVPSGM SGTVIDVQVF TREGIQRDKR AQQIIDDELK
     RYRLDLNDQL RIVEGDAFQR LARMLVGKVA NGGPKKLAKG TKIDQAYLED LDHYHWFDIR
     LADDEAAASL EAIKNSIEEK RHQFDLAFEE KRKKLTQGDE LPPGVLKMVK VYLAVKRRLQ
     PGDKMAGRHG NKGVVSKIVP IEDMPYMADG RPADVVLNPL GVPSRMNVGQ VLEVHLGWAA
     KGLGWRIGEM LQRQAKIEEL RTFLTKIYNE SGRQEDLESF TDDEILELAK NLREGVPFAT
     PVFDGATEEE MGKMLDLAFP DDIAEQLGMN PSKNQVRLYD GRTGEMFERR VTLGYMHYLK
     LHHLVDDKMH ARSTGPYSLV TQQPLGGKAQ FGGQRFGEME VWALEAYGAS YVLQEMLTVK
     SDDVTGRTKV YENLVKGDHV IDAGMPESFN VLVKEIRSLG IDIDLDRN