EVGA_ECOL6
ID EVGA_ECOL6 Reviewed; 204 AA.
AC P0ACZ5; P30854;
DT 22-NOV-2005, integrated into UniProtKB/Swiss-Prot.
DT 22-NOV-2005, sequence version 1.
DT 03-AUG-2022, entry version 101.
DE RecName: Full=DNA-binding transcriptional activator EvgA {ECO:0000305};
GN Name=evgA; OrderedLocusNames=c2905;
OS Escherichia coli O6:H1 (strain CFT073 / ATCC 700928 / UPEC).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=199310;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CFT073 / ATCC 700928 / UPEC;
RX PubMed=12471157; DOI=10.1073/pnas.252529799;
RA Welch R.A., Burland V., Plunkett G. III, Redford P., Roesch P., Rasko D.,
RA Buckles E.L., Liou S.-R., Boutin A., Hackett J., Stroud D., Mayhew G.F.,
RA Rose D.J., Zhou S., Schwartz D.C., Perna N.T., Mobley H.L.T.,
RA Donnenberg M.S., Blattner F.R.;
RT "Extensive mosaic structure revealed by the complete genome sequence of
RT uropathogenic Escherichia coli.";
RL Proc. Natl. Acad. Sci. U.S.A. 99:17020-17024(2002).
CC -!- FUNCTION: Member of the two-component regulatory system EvgS/EvgA.
CC Regulates the expression of emrKY operon and yfdX. Seems also to
CC control expression of at least one other multidrug efflux operon (By
CC similarity). {ECO:0000250}.
CC -!- SUBUNIT: Homodimer. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
CC -!- PTM: Phosphorylated by EvgS. {ECO:0000250}.
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DR EMBL; AE014075; AAN81355.1; -; Genomic_DNA.
DR RefSeq; WP_000991370.1; NC_004431.1.
DR AlphaFoldDB; P0ACZ5; -.
DR SMR; P0ACZ5; -.
DR STRING; 199310.c2905; -.
DR EnsemblBacteria; AAN81355; AAN81355; c2905.
DR GeneID; 66673761; -.
DR KEGG; ecc:c2905; -.
DR eggNOG; COG2197; Bacteria.
DR HOGENOM; CLU_000445_90_1_6; -.
DR OMA; YKKRLMQ; -.
DR BioCyc; ECOL199310:C2905-MON; -.
DR Proteomes; UP000001410; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR GO; GO:0000160; P:phosphorelay signal transduction system; IEA:UniProtKB-KW.
DR GO; GO:0006355; P:regulation of transcription, DNA-templated; IEA:InterPro.
DR CDD; cd06170; LuxR_C_like; 1.
DR Gene3D; 1.10.10.10; -; 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 InterPro; IPR036388; WH-like_DNA-bd_sf.
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; PS00622; HTH_LUXR_1; 1.
DR PROSITE; PS50043; HTH_LUXR_2; 1.
DR PROSITE; PS50110; RESPONSE_REGULATORY; 1.
PE 3: Inferred from homology;
KW Activator; Cytoplasm; DNA-binding; Phosphoprotein; Transcription;
KW Transcription regulation; Two-component regulatory system.
FT CHAIN 1..204
FT /note="DNA-binding transcriptional activator EvgA"
FT /id="PRO_0000081037"
FT DOMAIN 2..117
FT /note="Response regulatory"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00169"
FT DOMAIN 137..202
FT /note="HTH luxR-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00411"
FT DNA_BIND 161..180
FT /note="H-T-H motif"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00411"
FT MOD_RES 52
FT /note="4-aspartylphosphate"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00169"
SQ SEQUENCE 204 AA; 22690 MW; E68F932F3729FBBB CRC64;
MNAIIIDDHP LAIAAIRNLL IKNDIEILAE LTEGGSAVQR VETLKPDIVI IDVDIPGVNG
IQVLETLRKR QYSGIIIIVS AKNDHFYGKH CADAGANGFV SKKEGMNNII AAIEAAKNGY
CYFPFSLNRF VGSLTSDQQK LDSLSKQEIS VMRYILDGKD NNDIAEKMFI SNKTVSTYKS
RLMEKLECKS LMDLYTFAQR NKIG