EXAE_PSEPU
ID EXAE_PSEPU Reviewed; 214 AA.
AC A8R3S7;
DT 03-OCT-2012, integrated into UniProtKB/Swiss-Prot.
DT 15-JAN-2008, sequence version 1.
DT 25-MAY-2022, entry version 51.
DE RecName: Full=Transcriptional activator protein ExaE;
GN Name=exaE {ECO:0000312|EMBL:BAF91143.1};
OS Pseudomonas putida (Arthrobacter siderocapsulatus).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC Pseudomonadaceae; Pseudomonas.
OX NCBI_TaxID=303;
RN [1] {ECO:0000305, ECO:0000312|EMBL:BAF91143.1}
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, AND INDUCTION.
RC STRAIN=HK5 {ECO:0000312|EMBL:BAF91143.1};
RX PubMed=18218017; DOI=10.1111/j.1574-6968.2008.01060.x;
RA Promden W., Vangnai A.S., Pongsawasdi P., Adachi O., Matsushita K.,
RA Toyama H.;
RT "Disruption of quinoprotein ethanol dehydrogenase gene and adjacent genes
RT in Pseudomonas putida HK5.";
RL FEMS Microbiol. Lett. 280:203-209(2008).
RN [2] {ECO:0000305}
RP FUNCTION, AND INDUCTION.
RC STRAIN=HK5 {ECO:0000269|PubMed:19202108};
RX PubMed=19202108; DOI=10.1099/mic.0.021956-0;
RA Promden W., Vangnai A.S., Toyama H., Matsushita K., Pongsawasdi P.;
RT "Analysis of the promoter activities of the genes encoding three
RT quinoprotein alcohol dehydrogenases in Pseudomonas putida HK5.";
RL Microbiology 155:594-603(2009).
CC -!- FUNCTION: Positive regulator of the expression of the gene qedA and the
CC activity of ADH I but does not affect the activities of ADH IIB or ADH
CC IIG. {ECO:0000269|PubMed:18218017, ECO:0000269|PubMed:19202108}.
CC -!- INDUCTION: Up-regulated by AgmR but the exaE promoter is down-regulated
CC in the presence of a combination of glucose and ethanol.
CC {ECO:0000269|PubMed:18218017, ECO:0000269|PubMed:19202108}.
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DR EMBL; AB333783; BAF91143.1; -; Genomic_DNA.
DR AlphaFoldDB; A8R3S7; -.
DR SMR; A8R3S7; -.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR GO; GO:0000160; P:phosphorelay signal transduction system; IEA:InterPro.
DR GO; GO:0006355; P:regulation of transcription, DNA-templated; IEA:InterPro.
DR CDD; cd06170; LuxR_C_like; 1.
DR InterPro; IPR011006; CheY-like_superfamily.
DR InterPro; IPR016032; Sig_transdc_resp-reg_C-effctor.
DR InterPro; IPR001789; Sig_transdc_resp-reg_receiver.
DR InterPro; IPR000792; Tscrpt_reg_LuxR_C.
DR Pfam; PF00196; GerE; 1.
DR Pfam; PF00072; Response_reg; 1.
DR PRINTS; PR00038; HTHLUXR.
DR SMART; SM00421; HTH_LUXR; 1.
DR SMART; SM00448; REC; 1.
DR SUPFAM; SSF46894; SSF46894; 1.
DR SUPFAM; SSF52172; SSF52172; 1.
DR PROSITE; PS50043; HTH_LUXR_2; 1.
DR PROSITE; PS50110; RESPONSE_REGULATORY; 1.
PE 2: Evidence at transcript level;
KW DNA-binding; Phosphoprotein; Transcription; Transcription regulation.
FT CHAIN 1..214
FT /note="Transcriptional activator protein ExaE"
FT /id="PRO_0000419531"
FT DOMAIN 2..118
FT /note="Response regulatory"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00169"
FT DOMAIN 143..208
FT /note="HTH luxR-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00411"
FT DNA_BIND 167..186
FT /note="H-T-H motif"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00411"
FT MOD_RES 53
FT /note="4-aspartylphosphate"
FT /evidence="ECO:0000250|UniProtKB:P36556,
FT ECO:0000255|PROSITE-ProRule:PRU00169"
SQ SEQUENCE 214 AA; 23014 MW; 6699A2434DD26854 CRC64;
MGILLVDDHP MIRLGLAHFL GEGLNGLPVR EAGSGEEALQ QVQEELPGLV IMDFDLPGIS
GLETTRRLRQ RLPQLRVLFF SEHTELGLVR QALDAGACGF LSKAAAPAVV LEAVRRVLAG
HAYIEQPLAT QLACQPHPGQ GGGNARLQGL TQREIEVFLM LAKGTPTRLI AQQLCISAKT
VSNYLTLLKS KLQVSSHAEL VHLAIEAGLL RIAA
