ID   CFAD_ECOLX              Reviewed;         265 AA.
AC   P25393;
DT   01-MAY-1992, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1995, sequence version 2.
DT   25-MAY-2022, entry version 91.
DE   RecName: Full=CFA/I fimbrial subunit D;
DE   AltName: Full=Colonization factor antigen I subunit D;
GN   Name=cfaD;
OS   Escherichia coli.
OG   Plasmid NTP503.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=562;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=1971911; DOI=10.1016/0882-4010(90)90073-y;
RA   Savelkoul P.H.M., Willshaw G.A., McConnell M.M., Smith H.R., Hamers A.M.,
RA   van der Zeijst B.A.M., Gaastra W.;
RT   "Expression of CFA/I fimbriae is positively regulated.";
RL   Microb. Pathog. 8:91-99(1990).
RN   [2]
RP   CHARACTERIZATION.
RX   PubMed=1378396; DOI=10.1002/j.1460-2075.1992.tb05328.x;
RA   Jordi B.J.A.M., Dagberg B., de Haan L.A.M., Hamers A.M.;
RT   "The positive regulator CfaD overcomes the repression mediated by histone-
RT   like protein H-NS (H1) in the CFA/I fimbrial operon of Escherichia coli.";
RL   EMBO J. 11:2627-2632(1992).
CC   -!- FUNCTION: Transcriptional activator of the CFA/I adhesin (cfAA) gene of
CC       enterotoxygenic escherichia coli at the temperature of 37 degrees
CC       Celsius.
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DR   EMBL; M55609; AAA62773.1; -; Genomic_DNA.
DR   PIR; I41162; I41162.
DR   RefSeq; WP_000346362.1; NZ_POSQ01000105.1.
DR   AlphaFoldDB; P25393; -.
DR   SMR; P25393; -.
DR   GO; GO:0003700; F:DNA-binding transcription factor activity; IEA:InterPro.
DR   GO; GO:0043565; F:sequence-specific DNA binding; IEA:InterPro.
DR   InterPro; IPR009057; Homeobox-like_sf.
DR   InterPro; IPR018060; HTH_AraC.
DR   InterPro; IPR018062; HTH_AraC-typ_CS.
DR   InterPro; IPR020449; Tscrpt_reg_HTH_AraC-type.
DR   Pfam; PF12833; HTH_18; 1.
DR   PRINTS; PR00032; HTHARAC.
DR   SMART; SM00342; HTH_ARAC; 1.
DR   SUPFAM; SSF46689; SSF46689; 1.
DR   PROSITE; PS00041; HTH_ARAC_FAMILY_1; 1.
DR   PROSITE; PS01124; HTH_ARAC_FAMILY_2; 1.
PE   1: Evidence at protein level;
KW   Activator; DNA-binding; Plasmid; Transcription; Transcription regulation.
FT   CHAIN           1..265
FT                   /note="CFA/I fimbrial subunit D"
FT                   /id="PRO_0000194577"
FT   DOMAIN          164..261
FT                   /note="HTH araC/xylS-type"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00593"
FT   DNA_BIND        181..202
FT                   /note="H-T-H motif"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00593"
FT   DNA_BIND        228..251
FT                   /note="H-T-H motif"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00593"
SQ   SEQUENCE   265 AA;  30853 MW;  2A7C32DCCBFBEFF9 CRC64;
     MDFKYTEEKE MIKINNIMIH KYTVLYTSNC IMDIYSEEEK ITCFSNRLVF LERGVNISVR
     IQKKILSERP YVAFRLNGDI LRHLKNALMI IYGMSKVDTN DCRGMSRKIM TTEVNKTLLD
     ELKNINSHDD SAFISSLIYL ISKIENNEKI IESIYISSVS FFSDKVRNVI EKDLSRKWTL
     GIIADAFNVS EITIRKRLES ENTNFNQILM QLRMSKAALL LLENSYQISQ ISNMIGISSA
     SYFIRVFNKH YGVTPKQFFT YFKGG