EVGA_SHIFL
ID EVGA_SHIFL Reviewed; 204 AA.
AC P0ACZ7; P30854;
DT 22-NOV-2005, integrated into UniProtKB/Swiss-Prot.
DT 22-NOV-2005, sequence version 1.
DT 25-MAY-2022, entry version 117.
DE RecName: Full=DNA-binding transcriptional activator EvgA {ECO:0000305};
GN Name=evgA; OrderedLocusNames=SF2436, S2573;
OS Shigella flexneri.
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Shigella.
OX NCBI_TaxID=623;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=301 / Serotype 2a;
RX PubMed=12384590; DOI=10.1093/nar/gkf566;
RA Jin Q., Yuan Z., Xu J., Wang Y., Shen Y., Lu W., Wang J., Liu H., Yang J.,
RA Yang F., Zhang X., Zhang J., Yang G., Wu H., Qu D., Dong J., Sun L.,
RA Xue Y., Zhao A., Gao Y., Zhu J., Kan B., Ding K., Chen S., Cheng H.,
RA Yao Z., He B., Chen R., Ma D., Qiang B., Wen Y., Hou Y., Yu J.;
RT "Genome sequence of Shigella flexneri 2a: insights into pathogenicity
RT through comparison with genomes of Escherichia coli K12 and O157.";
RL Nucleic Acids Res. 30:4432-4441(2002).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700930 / 2457T / Serotype 2a;
RX PubMed=12704152; DOI=10.1128/iai.71.5.2775-2786.2003;
RA Wei J., Goldberg M.B., Burland V., Venkatesan M.M., Deng W., Fournier G.,
RA Mayhew G.F., Plunkett G. III, Rose D.J., Darling A., Mau B., Perna N.T.,
RA Payne S.M., Runyen-Janecky L.J., Zhou S., Schwartz D.C., Blattner F.R.;
RT "Complete genome sequence and comparative genomics of Shigella flexneri
RT serotype 2a strain 2457T.";
RL Infect. Immun. 71:2775-2786(2003).
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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AE005674; AAN43947.1; -; Genomic_DNA.
DR EMBL; AE014073; AAP17757.1; -; Genomic_DNA.
DR RefSeq; NP_708240.1; NC_004337.2.
DR RefSeq; WP_000991370.1; NZ_WPGW01000144.1.
DR PDB; 5F64; X-ray; 2.71 A; A/B/C/D=1-204.
DR PDBsum; 5F64; -.
DR AlphaFoldDB; P0ACZ7; -.
DR SMR; P0ACZ7; -.
DR STRING; 198214.SF2436; -.
DR EnsemblBacteria; AAN43947; AAN43947; SF2436.
DR EnsemblBacteria; AAP17757; AAP17757; S2573.
DR GeneID; 1025897; -.
DR GeneID; 66673761; -.
DR KEGG; sfl:SF2436; -.
DR KEGG; sfx:S2573; -.
DR PATRIC; fig|198214.7.peg.2910; -.
DR HOGENOM; CLU_000445_90_1_6; -.
DR OMA; YKKRLMQ; -.
DR OrthoDB; 1687028at2; -.
DR Proteomes; UP000001006; Chromosome.
DR Proteomes; UP000002673; 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 1: Evidence at protein level;
KW 3D-structure; Activator; Cytoplasm; DNA-binding; Phosphoprotein;
KW Reference proteome; Transcription; Transcription regulation;
KW Two-component regulatory system.
FT CHAIN 1..204
FT /note="DNA-binding transcriptional activator EvgA"
FT /id="PRO_0000081038"
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"
FT STRAND 1..6
FT /evidence="ECO:0007829|PDB:5F64"
FT HELIX 10..22
FT /evidence="ECO:0007829|PDB:5F64"
FT STRAND 25..32
FT /evidence="ECO:0007829|PDB:5F64"
FT HELIX 37..44
FT /evidence="ECO:0007829|PDB:5F64"
FT STRAND 47..52
FT /evidence="ECO:0007829|PDB:5F64"
FT STRAND 56..58
FT /evidence="ECO:0007829|PDB:5F64"
FT HELIX 60..69
FT /evidence="ECO:0007829|PDB:5F64"
FT STRAND 74..82
FT /evidence="ECO:0007829|PDB:5F64"
FT HELIX 87..93
FT /evidence="ECO:0007829|PDB:5F64"
FT STRAND 97..101
FT /evidence="ECO:0007829|PDB:5F64"
FT HELIX 102..104
FT /evidence="ECO:0007829|PDB:5F64"
FT HELIX 107..117
FT /evidence="ECO:0007829|PDB:5F64"
FT STRAND 120..124
FT /evidence="ECO:0007829|PDB:5F64"
FT HELIX 127..129
FT /evidence="ECO:0007829|PDB:5F64"
FT STRAND 131..133
FT /evidence="ECO:0007829|PDB:5F64"
FT HELIX 135..142
FT /evidence="ECO:0007829|PDB:5F64"
FT HELIX 146..155
FT /evidence="ECO:0007829|PDB:5F64"
FT TURN 156..158
FT /evidence="ECO:0007829|PDB:5F64"
FT HELIX 161..167
FT /evidence="ECO:0007829|PDB:5F64"
FT HELIX 172..185
FT /evidence="ECO:0007829|PDB:5F64"
FT HELIX 191..200
FT /evidence="ECO:0007829|PDB:5F64"
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
