RPOB_DELAS
ID RPOB_DELAS Reviewed; 1370 AA.
AC A9BR98;
DT 14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT 15-JAN-2008, 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}; OrderedLocusNames=Daci_0510;
OS Delftia acidovorans (strain DSM 14801 / SPH-1).
OC Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC Comamonadaceae; Delftia.
OX NCBI_TaxID=398578;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 14801 / SPH-1;
RA Copeland A., Lucas S., Lapidus A., Barry K., Glavina del Rio T., Dalin E.,
RA Tice H., Pitluck S., Lowry S., Clum A., Schmutz J., Larimer F., Land M.,
RA Hauser L., Kyrpides N., Kim E., Schleheck D., Richardson P.;
RT "Complete sequence of Delftia acidovorans DSM 14801 / SPH-1.";
RL Submitted (NOV-2007) to the EMBL/GenBank/DDBJ databases.
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; CP000884; ABX33156.1; -; Genomic_DNA.
DR RefSeq; WP_012202442.1; NC_010002.1.
DR AlphaFoldDB; A9BR98; -.
DR SMR; A9BR98; -.
DR STRING; 398578.Daci_0510; -.
DR PRIDE; A9BR98; -.
DR EnsemblBacteria; ABX33156; ABX33156; Daci_0510.
DR KEGG; dac:Daci_0510; -.
DR eggNOG; COG0085; Bacteria.
DR HOGENOM; CLU_000524_4_0_4; -.
DR OMA; FMTWEGY; -.
DR Proteomes; UP000000784; 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; -; 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..1370
FT /note="DNA-directed RNA polymerase subunit beta"
FT /id="PRO_1000141683"
SQ SEQUENCE 1370 AA; 152887 MW; E64EF2DE118B3C6D CRC64;
MAYSYTERKR IRKSFGSRDS VLEVPYLLQM QKDAYTAFLQ SDVAPKKRTI EGLQAAFNSA
FPIVSHNGFV EMKFVEYNLA KPAFDVRECQ TRGLTFASAV RAKVQLIIYD RESSTSQSKV
VKEVKEQEVY MGEVPLMTEK GSFIINGTER VIVSQLHRSP GVFFEHDKGK THSSGKLLFS
ARIIPYRGSW LDFEFDPKDL LFFRVDRRRK MPVSILLKAI GLTPESILAN FFVNDNFRLM
DSGAQMEFVS ERLRGEVARF DITDKSGKVV VAKDKRVTAR HTRELEQSGT KFISVPEDFL
IGRVVAKNIV DPDTGEIIAK ANEELTESLL KKLRSAGIQD LQCIYTNELD QGAYISQTLR
TDETVDEFAA RVAIYRMMRP GEPPTEDAVQ ALFQRLFYNP DTYDLSRVGR MKFNAKVGRD
GATGPMVLSN EDILAVVKIL VDLRNGKGEV DDIDHLGNRR VRCVGELAEN QYRTGLARIE
KAVKERLGQA EQEPLMPHDL INSKPISAAL KEFFGASQLS QFMDQTNPLA EITHKRRVSA
LGPGGLTRER AGFEVRDVHV THYGRVCPIE TPEGPNIGLI NSLALYARLN EYGFIETPYR
RVADGKVTME IDYLSAIEEG KYIIAQANAE LDAEGRLIGD LVSAREKGDS TLVSAERVQY
MDVSPAQIVS VAASLIPFLE HDDANRALMG ANMSRQAVPV LRPEKPMVGT GIERVAAVDS
GTVVTATRGG IVDYVDATRI VVRVNDAEAV AGEVGVDIYN LIKYQRSNQN TNIHQRPIVK
RGDKLAKGDV VADGASTDLG EIAIGQNMLI AFMPWNGYNF EDSILINERV VAEDRYTSIH
IEELVVMARD TKLGAEEITR DIPNLSEQQL NRLDESGIIY VGAEVQPGDV LVGKVTPKGE
TTLTPEEKLL RAIFGEKASD VKDTSLRVDQ GSQGTVIDVQ VFTREGIQRD KRAQQIIDDE
LKRYRLDLND QLRIVEADAF DRIEKLLNGR VANGGPQKLA KGAKIDKAYL DGVEKFHWFD
IRPAEDEVAT QLESIKNSLE QTRHSFDLAF EEKRKKLTQG DELPAGVLKM VKVYLAVKRR
LQPGDKMAGR HGNKGVVSKI VPVEDMPYMA DGSTADIVLN PLGVPSRMNI GQVLEVHLGW
AGKGLGQRIG DMLQQEARAA EIRTFMEEIY NSRGRKEDLT QLDDKEIVSM AQALTTGVPF
ATPVFDGASE QEIQDMLHLA YPEELAQRKG LTESRTQAYL YDGRTGDRFE RPTTIGYMHY
LKLHHLVDDK MHARSTGPYS LVTQQPLGGK AQFGGQRFGE MEVWALEAYG AAYVLQEMLT
VKSDDVVGRT KVYESIVKGE HAIEAGMPES FNVLVKEIRS LGLDIELERS
