RPOB_BURM9
ID RPOB_BURM9 Reviewed; 1368 AA.
AC A2S7G6;
DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT 06-MAR-2007, sequence version 1.
DT 03-AUG-2022, entry version 84.
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=BMA10229_A1914;
OS Burkholderia mallei (strain NCTC 10229).
OC Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC Burkholderiaceae; Burkholderia; pseudomallei group.
OX NCBI_TaxID=412022;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NCTC 10229;
RX PubMed=20333227; DOI=10.1093/gbe/evq003;
RA Losada L., Ronning C.M., DeShazer D., Woods D., Fedorova N., Kim H.S.,
RA Shabalina S.A., Pearson T.R., Brinkac L., Tan P., Nandi T., Crabtree J.,
RA Badger J., Beckstrom-Sternberg S., Saqib M., Schutzer S.E., Keim P.,
RA Nierman W.C.;
RT "Continuing evolution of Burkholderia mallei through genome reduction and
RT large-scale rearrangements.";
RL Genome Biol. Evol. 2:102-116(2010).
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; CP000546; ABN03098.1; -; Genomic_DNA.
DR RefSeq; WP_004198365.1; NC_008836.1.
DR AlphaFoldDB; A2S7G6; -.
DR SMR; A2S7G6; -.
DR PRIDE; A2S7G6; -.
DR EnsemblBacteria; ABN03098; ABN03098; BMA10229_A1914.
DR GeneID; 56594534; -.
DR KEGG; bml:BMA10229_A1914; -.
DR HOGENOM; CLU_000524_4_3_4; -.
DR OMA; FMTWEGY; -.
DR Proteomes; UP000002283; Chromosome I.
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; Transcription;
KW Transferase.
FT CHAIN 1..1368
FT /note="DNA-directed RNA polymerase subunit beta"
FT /id="PRO_1000051963"
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
