RPOB_PARPJ
ID RPOB_PARPJ Reviewed; 1368 AA.
AC B2T759;
DT 14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT 01-JUL-2008, sequence version 1.
DT 03-AUG-2022, entry version 79.
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=Bphyt_3652;
OS Paraburkholderia phytofirmans (strain DSM 17436 / LMG 22146 / PsJN)
OS (Burkholderia phytofirmans).
OC Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC Burkholderiaceae; Paraburkholderia.
OX NCBI_TaxID=398527;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 17436 / LMG 22146 / PsJN;
RX PubMed=21551308; DOI=10.1128/jb.05055-11;
RA Weilharter A., Mitter B., Shin M.V., Chain P.S., Nowak J., Sessitsch A.;
RT "Complete genome sequence of the plant growth-promoting endophyte
RT Burkholderia phytofirmans strain PsJN.";
RL J. Bacteriol. 193:3383-3384(2011).
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; CP001052; ACD18042.1; -; Genomic_DNA.
DR RefSeq; WP_012434577.1; NC_010681.1.
DR AlphaFoldDB; B2T759; -.
DR SMR; B2T759; -.
DR STRING; 398527.Bphyt_3652; -.
DR EnsemblBacteria; ACD18042; ACD18042; Bphyt_3652.
DR KEGG; bpy:Bphyt_3652; -.
DR eggNOG; COG0085; Bacteria.
DR HOGENOM; CLU_000524_4_0_4; -.
DR OMA; FMTWEGY; -.
DR OrthoDB; 9601at2; -.
DR Proteomes; UP000001739; 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_1000141673"
SQ SEQUENCE 1368 AA; 153057 MW; 9C95DC35C6BCCBB2 CRC64;
MQYSFTEKKR IRKSFAKRPI VHQVPFLLAT QLESFSTFLQ ADTSSTQRKP EGLQAAFTSV
FPIVSHNGFA RLEFVSYMLS PPAFNIKECQ QRGLTYCSAL RAKVRLVLLD KESPSKPVVK
EVKEQEVYMG EIPLMTPTGS FVINGTERVI VSQLHRSPGV FFEHDKGKTH SSGKLLFSAR
IIPYRGSWLD FEFDPKDVLY FRVDRRRKMP VTILLKAIGL TPEQILANFF VFDNFTLMPE
GAQMEFVPER LRGEVARFDI TDRDGNVIVQ KDKRINAKHI RDLDNAKTKF ISVPEDYLLG
RVLAKNVVDG DTGEVIANAN DEITETVLEK LRESKIKDIQ TLYTNDLDQG PYISSTLRID
ETADKMAARI AIYRMMRPGE PPTEEAVEAL FNRLFYSEDA YDLSKVGRMK FNRRVGRDEI
VGPMTLQDDD ILATIKILVE LRNGKGEVDD IDHLGNRRVR CVGELAENQF RAGLVRVERA
VKERLGQAES ENLMPHDLIN SKPISSAIRE FFGSSQLSQF MDQTNPLSEI THKRRVSALG
PGGLTRERAG FEVRDVHPTH YGRVCPIETP EGPNIGLINS LALYAHLNEY GFLETPYRKV
VDSKVTDQID YLSAIEEGRY VIAQANAAVA EDGSLTDELV SSREAGETLM VTPDRIQYMD
VAPSQIVSVA ASLIPFLEHD DANRALMGSN MQRQAVPCLR PEKAVVGTGI ERTVAVDSGT
TVQAFRGGVV DYVDAGRMVI RVNDDEAAAG ETGVDIYNLI KYTRSNQNTN INQRPIVKVG
DIVSRGDVLA DGASTDLGEL ALGQNMLVAF MPWNGYNFED SILISEKVVA DDRYTSIHIE
ELNVVARDTK LGPEEITRDI SNLAEVQLGR LDESGIVYIG AEVEAGDVLV GKVTPKGETQ
LTPEEKLLRA IFGEKASDVK DTSLRVPSGM SGTVIDVQVF TREGIQRDKR AQQIIDDELK
RYRLDLNDQL RIVEGDAFQR LARMLDGKVA NGGPKKLAKG TKIEQAYLQD LDHYHWFDIR
LADEEAAAQL EAIKDSIEQK RHQFDLAFEE KRKKLTQGDE LPPGVLKMVK VYLAVKRRLQ
PGDKMAGRHG NKGVVSKIVP IEDMPYMADG RPADVVLNPL GVPSRMNVGQ VLEVHLGWAA
KGLGWRIGEM LQRQAKIAEL REFLTKIYNE SGRAEELDSF TDDEIVELAK NLREGVPFAT
PVFDGATEEE MSRALDLAFP DDIAKNLGMT PSKNQVRLYD GRTGEMFERT VTVGYMHYLK
LHHLVDDKMH ARSTGPYSLV TQQPLGGKAQ FGGQRFGEME VWALEAYGAS YVLQEMLTVK
SDDVTGRTKV YENLVKGDHV IDAGMPESFN VLVKEIRSLG IDIDLDRN
