ID   EAE_ECO11               Reviewed;         935 AA.
AC   O31000;
DT   29-AUG-2001, integrated into UniProtKB/Swiss-Prot.
DT   01-JAN-1998, sequence version 1.
DT   25-MAY-2022, entry version 99.
DE   RecName: Full=Intimin;
DE   AltName: Full=Attaching and effacing protein;
DE            Short=Eae protein;
GN   Name=eae; Synonyms=eaeA;
OS   Escherichia coli O111:H-.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=168927;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=9529069; DOI=10.1128/iai.66.4.1467-1472.1998;
RA   Voss E., Paton A.W., Manning P.A., Paton J.C.;
RT   "Molecular analysis of Shiga toxigenic Escherichia coli O111:H-proteins
RT   which react with sera from patients with hemolytic-uremic syndrome.";
RL   Infect. Immun. 66:1467-1472(1998).
CC   -!- FUNCTION: Necessary for the production of attaching and effacing
CC       lesions on tissue culture cells. Believed to mediate adherence.
CC   -!- SUBCELLULAR LOCATION: Cell outer membrane {ECO:0000250}; Single-pass
CC       membrane protein {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the intimin/invasin family. {ECO:0000305}.
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DR   EMBL; AF025311; AAC69247.1; -; Genomic_DNA.
DR   AlphaFoldDB; O31000; -.
DR   SMR; O31000; -.
DR   GO; GO:0009279; C:cell outer membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0007155; P:cell adhesion; IEA:InterPro.
DR   CDD; cd00118; LysM; 1.
DR   Gene3D; 2.40.160.160; -; 1.
DR   Gene3D; 2.60.40.10; -; 2.
DR   Gene3D; 3.10.100.10; -; 1.
DR   Gene3D; 3.10.350.10; -; 1.
DR   InterPro; IPR003344; Big_1_dom.
DR   InterPro; IPR003343; Big_2.
DR   InterPro; IPR016186; C-type_lectin-like/link_sf.
DR   InterPro; IPR016187; CTDL_fold.
DR   InterPro; IPR024519; IAT_beta.
DR   InterPro; IPR038177; IAT_beta_sf.
DR   InterPro; IPR013783; Ig-like_fold.
DR   InterPro; IPR003535; Intimin/invasin_bac.
DR   InterPro; IPR013117; Intimin_C.
DR   InterPro; IPR008964; Invasin/intimin_cell_adhesion.
DR   InterPro; IPR018392; LysM_dom.
DR   InterPro; IPR036779; LysM_dom_sf.
DR   Pfam; PF02369; Big_1; 2.
DR   Pfam; PF02368; Big_2; 1.
DR   Pfam; PF11924; IAT_beta; 1.
DR   Pfam; PF07979; Intimin_C; 1.
DR   Pfam; PF01476; LysM; 1.
DR   PRINTS; PR01369; INTIMIN.
DR   SMART; SM00634; BID_1; 2.
DR   SMART; SM00635; BID_2; 1.
DR   SMART; SM00257; LysM; 1.
DR   SUPFAM; SSF49373; SSF49373; 3.
DR   SUPFAM; SSF56436; SSF56436; 1.
DR   PROSITE; PS51127; BIG1; 2.
DR   PROSITE; PS51782; LYSM; 1.
PE   3: Inferred from homology;
KW   Cell outer membrane; Membrane; Repeat; Transmembrane; Transmembrane helix;
KW   Virulence.
FT   CHAIN           1..935
FT                   /note="Intimin"
FT                   /id="PRO_0000211826"
FT   TRANSMEM        20..39
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   DOMAIN          63..112
FT                   /note="LysM"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01118"
FT   DOMAIN          560..653
FT                   /note="Big-1 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00445"
FT   DOMAIN          660..754
FT                   /note="Big-1 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00445"
FT   DOMAIN          924..935
FT                   /note="BIG2"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   935 AA;  101570 MW;  406E79CDC07DEB11 CRC64;
     MITHGFYART RHKHKLKKTF IMLSAGLGLF FYVNQNSFAN GENYFKLSSD SKLLTQNVAQ
     DRLFYTLKTG ETVSSISKSQ GISLSVIWSL NKHLYSSESE MLKAAPGQQI ILPLKKLSVE
     YGALPVLGSA PVVAAGGVAG HTNKMTKMSP DATQSNMTDD RALNYTAQQA ASLGSQLQSR
     SLHGDYAKDT ALGIAGNQAS SQLQAWLQHY GTAEVNLQSG NNFDGSSLDF LLPFYDSEKM
     LAFGQVGARY IDSRFTANLG AGQRFFLPEN MLGYNVFIDQ DFSGDNTRLG IGGEYWRDYF
     KSSVNGYFRM SGWHESYNKK DYDERPANGF DIRFNGYLPS YPALGAKLMY EQYYGDNVAL
     FNSDKLQSNP GAATVGVNYT PIPLVTMGID YRHGTGYEND LLYSMQFRYQ FDKPWSPQIE
     PQYVNELRTL SGSRYDLVQR NNNIILEYKK QDILSLNIPH DINGTEHSTQ KIQLIVKSKY
     GLDRIVWDDS ALRSQGGQIQ HSGSQSAQDY QAILPAYVQG GSNIYKVTAR AYDRNGNSSN
     NVQLTITVLS NGQVVDQVGV TDFTADKTSA KADGTEAITY TATVKKNGVT QANVPVSFNI
     VSGTATLGAN SATTDANGKA TVTLKSSTPG QVVVSAKTAE MTSALNASAV IFVEQTKASI
     TEIKADKTTA VANGNDAVTY TVKVMKEGQP VHGHSVAFTT NFGMFNGKSQ TQNATTGSDG
     RATITLTSSS AGKATVSATV SGGNDVKAPE VTFFDGLKID NKVDILGKNV TGDLPNIWLQ
     YGQFKLKVSG GNGTYSWHSE NTNIATVDES GKVTLKGKGT AVINVTSGDK QTVSYTIKAP
     NYMIRVGNKA SYANAMSFCG NLLPSSQTVL SNVYNSWGPA NGYDHYRSMQ SITAWITQTE
     ADKISGVSTT YDLITQNPHK DVSLNAPNVY AVCVE