ID   B0AZK2_ECOLX            Unreviewed;       939 AA.
AC   B0AZK2;
DT   26-FEB-2008, integrated into UniProtKB/TrEMBL.
DT   26-FEB-2008, sequence version 1.
DT   27-MAR-2024, entry version 52.
DE   RecName: Full=Intimin {ECO:0000256|ARBA:ARBA00017346};
DE   AltName: Full=Attaching and effacing protein {ECO:0000256|ARBA:ARBA00029955};
GN   Name=eae {ECO:0000313|EMBL:CAI46996.1};
OS   Escherichia coli.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=562 {ECO:0000313|EMBL:CAI46996.1};
RN   [1] {ECO:0000313|EMBL:CAI46996.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=CB 9786 {ECO:0000313|EMBL:CAI46996.1};
RA   Krause G., Beutin L.;
RT   "Intimin types of atypical enteropathogenic Escherichia coli.";
RL   Submitted (JAN-2005) to the EMBL/GenBank/DDBJ databases.
CC   -!- SUBCELLULAR LOCATION: Cell outer membrane
CC       {ECO:0000256|ARBA:ARBA00004203}; Single-pass membrane protein
CC       {ECO:0000256|ARBA:ARBA00004203}. Membrane
CC       {ECO:0000256|ARBA:ARBA00004167}; Single-pass membrane protein
CC       {ECO:0000256|ARBA:ARBA00004167}.
CC   -!- SIMILARITY: Belongs to the intimin/invasin family.
CC       {ECO:0000256|ARBA:ARBA00010116}.
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; AJ877229; CAI46996.1; -; Genomic_DNA.
DR   AlphaFoldDB; B0AZK2; -.
DR   GO; GO:0009279; C:cell outer membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0007155; P:cell adhesion; IEA:InterPro.
DR   Gene3D; 2.60.40.1080; -; 1.
DR   Gene3D; 2.60.40.10; Immunoglobulins; 2.
DR   Gene3D; 2.40.160.160; Inverse autotransporter, beta-domain; 1.
DR   Gene3D; 3.10.100.10; Mannose-Binding Protein A, subunit A; 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   PANTHER; PTHR39576; ATTACHING AND EFFACING PROTEIN HOMOLOG-RELATED-RELATED; 1.
DR   PANTHER; PTHR39576:SF1; INVASIN-RELATED; 1.
DR   Pfam; PF02369; Big_1; 2.
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; SSF56436; C-type lectin-like; 1.
DR   SUPFAM; SSF49373; Invasin/intimin cell-adhesion fragments; 3.
DR   PROSITE; PS51127; BIG1; 2.
DR   PROSITE; PS51782; LYSM; 1.
PE   3: Inferred from homology;
KW   Cell outer membrane {ECO:0000256|ARBA:ARBA00023237};
KW   Membrane {ECO:0000256|ARBA:ARBA00023136};
KW   Transmembrane {ECO:0000256|ARBA:ARBA00022692};
KW   Virulence {ECO:0000256|ARBA:ARBA00023026}.
FT   DOMAIN          63..112
FT                   /note="LysM"
FT                   /evidence="ECO:0000259|PROSITE:PS51782"
FT   DOMAIN          560..653
FT                   /note="Big-1"
FT                   /evidence="ECO:0000259|PROSITE:PS51127"
FT   DOMAIN          660..751
FT                   /note="Big-1"
FT                   /evidence="ECO:0000259|PROSITE:PS51127"
SQ   SEQUENCE   939 AA;  101775 MW;  18CFB708374B9F2D CRC64;
     MITHGFYART RHKHKLKKTF IMLSAGLGLF FYVNQNSFAN GENYFKLSSD SKLLTQNAAQ
     DRLFYTLKTG ETVANISKSQ GISLSVIWSL NKHLYSSESE MMKAGPGQQI ILPLKKLSVE
     YSALPVLGSA PVVAAGGVAG HTNKMTKMSP DATKSNTTDD KALNYAAQQA ASLGSQLQSR
     SLNGDYAKDT ALGMASSQAS SQLQAWLQHY GTAEVNLQSG NNFDGSSLDF LLPFYDSENM
     LAFGQVGARY IDSRFTANLG AGQRFFLPEN MLGYNVFIDQ DFSGDNTRLG IGGEYWRDYF
     KSSVNGYFRM SGWHESYNKK DYDERPANGF DIRFNGYLPS YPALGAKLMY EQYYGDNVAL
     FNSDKLQSNP GAATVGVNYT PIPLVTMGID YRHGTGNEND LLYSMQFRYQ FDKPWSQQIE
     PQYVNELRTL SGSRYDLVQR NNNIILEYKK QDILSLNIPH DINGTEHSTQ KIQLIVKSKY
     GLDRIVWDDS ALRSQGGQIQ HSGSQSAQDY QAILPAYVQG GSNIYKVTAR AYDRNGNSSN
     NVQLTITVLP NGQVVDQVGV TDFTADKTSA KADNVDTITY TATVKKNGVA QANAPVTFSI
     VSGTATLGAN SAKTDGNGKA TVTLKSGTPG QVVVSAKTAE MTSPLNASAV IFVDQTKASI
     TEIKADKTTA VANGKDAVTY TVKVMKNGQP LSGEEVSFTT TLGALSKPSE KTDANGYAKV
     TLTSTTQGKS LVSASVSNVA VDVKAPEVEF FTPLTIDDDS IEIVGTGVKG KLPTVWLQYG
     QVKLKASGGN GKYTWRSANT AIASVDASSG QITLKDKGAT TITVVSGDNQ TATYTIATPD
     SLIVSNLSKR VTYNDAVNTC KNLGGKLPSS QSELENVFKI WGAANKYEYY KSRQSISSWV
     QQTPGNMNSG VASTYDLVRK NPLSNVDVNG TNAYATCVK
//