RPOB_POLSJ
ID RPOB_POLSJ Reviewed; 1370 AA.
AC Q123G3;
DT 11-SEP-2007, integrated into UniProtKB/Swiss-Prot.
DT 22-AUG-2006, 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=Bpro_4442;
OS Polaromonas sp. (strain JS666 / ATCC BAA-500).
OC Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC Comamonadaceae; Polaromonas; unclassified Polaromonas.
OX NCBI_TaxID=296591;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JS666 / ATCC BAA-500;
RX PubMed=18723656; DOI=10.1128/aem.00197-08;
RA Mattes T.E., Alexander A.K., Richardson P.M., Munk A.C., Han C.S.,
RA Stothard P., Coleman N.V.;
RT "The genome of Polaromonas sp. strain JS666: insights into the evolution of
RT a hydrocarbon- and xenobiotic-degrading bacterium, and features of
RT relevance to biotechnology.";
RL Appl. Environ. Microbiol. 74:6405-6416(2008).
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; CP000316; ABE46329.1; -; Genomic_DNA.
DR RefSeq; WP_011485318.1; NC_007948.1.
DR AlphaFoldDB; Q123G3; -.
DR SMR; Q123G3; -.
DR STRING; 296591.Bpro_4442; -.
DR PRIDE; Q123G3; -.
DR EnsemblBacteria; ABE46329; ABE46329; Bpro_4442.
DR KEGG; pol:Bpro_4442; -.
DR eggNOG; COG0085; Bacteria.
DR HOGENOM; CLU_000524_4_3_4; -.
DR OMA; FMTWEGY; -.
DR OrthoDB; 9601at2; -.
DR Proteomes; UP000001983; 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_0000300368"
SQ SEQUENCE 1370 AA; 152529 MW; 803E03E3A8D2F172 CRC64;
MAYSYTERKR IRKSFGNRES VLTVPYLLQM QKDAYTAFLQ ADRAPQKRTV EGLQAAFENA
FPIVSHNGFV EMKFIEYNLA KPAFDVRECQ TRGLTFASAV RAKVQLIIYD RESSTSQSKV
VKEVKEQEVY MGEVPLMTDK GSFVINGTER VIVSQLHRSP GVFFEHDKGK THSSGKLLFS
ARIIPYRGSW LDFEFDPKDV LYFRVDRRRK MPVTILLKAI GLNPESILAN FFVFDHFRLM
DSGAQMEFVA ERMRGEVARF DITDKSGKVV VAKDKRITVR HTRELEQSGT TTISVPEDFL
VGRVVAKNIV DAETGEIIAK ANDELTELLL KKLRLAGVQD LQVLYTNELD QGAYISQTLR
ADETADEFAA RVAIYRMMRP GEPPTEDAVQ ALFQRLFYNP DTYDLSKVGR MKFNARVGRD
DSTGPMVMTN EDILAVVKIL VDLRNGNGEV DDIDHLGNRR VRCVGELAEN QYRTGLARIE
KAVKERLGQA EQEPLMPHDL INSKPISAAL KEFFGASQLS QFMDQTNPLS EITHKRRVSA
LGPGGLTRER AGFEVRDVHV THYGRVCPIE TPEGPNIGLI NSLALYARLN EYGFIETPYR
RVVDSKITDQ IDYLSAIEEG KYVIAQANAL LDDSGTLTGD LVSARENGES VLVGAERIQY
MDVSPAQIVS VAASLVPFLE HDDANRALMG ANMQRQAVPV LRPEKAFVGT GIERVSAVDS
GTVVTANRGG VVDYVDATRI VVRVNDAEAL AGEVGVDIYN LIKYQRSNQN TNIHQRPIVK
IGDKLAKGDV IADGASTDIG ELALGQNMLV AFMPWNGYNF EDSILISERV VAEDRYTSIH
IEELVVMARD TKLGSEEITR DIPNLSEQQL NRLDESGIIY VGAEVQPGDT LVGKVTPKGE
TTLTPEEKLL RAIFGEKASD VKDTSLRVSQ GSQGTVIDVQ VFTREGIVRD KRAQQIIDDE
LKRFRLDLND QLRIVEADAF DRIEKLLNGK VANGGPKKLA KGTKIDKAYL ADVEKYHWFD
IRPADDEVAS QLESIKNAME QTRHSFDLAF EEKRKKLTQG DELPAGVLKM VKVYLAVKRR
LQPGDKMAGR HGNKGVVSKI VPVEDMPYMA DGTPCDIVLN PLGVPSRMNV GQVLEVHLGW
AAKGLGQRIG DMLQAEAKVA ELRKFMDTLY NKSGRVEDLA NLSDTDVLEM ARNLTTGVPF
ATPVFDGASE EDIMTMLKLA YPDDIAKAKG LTATRTQAQL YDGRTGDQFE RTTTVGYMHV
LKLHHLVDDK MHARSTGPYS LVTQQPLGGK AQFGGQRFGE MEVWALEAYG ASYTLQEMLT
VKSDDVQGRT KVYESIVKGE HAITAGMPES FNVLVKEIRS LGIDIELERS
