EAE_CITFR
ID EAE_CITFR Reviewed; 936 AA.
AC Q07591;
DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1995, sequence version 1.
DT 25-MAY-2022, entry version 97.
DE RecName: Full=Intimin;
DE AltName: Full=Attaching and effacing protein;
DE Short=Eae protein;
GN Name=eae;
OS Citrobacter freundii.
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Citrobacter; Citrobacter freundii complex.
OX NCBI_TaxID=546;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=8500884; DOI=10.1128/iai.61.6.2486-2492.1993;
RA Schauer D.B., Falkow S.;
RT "Attaching and effacing locus of a Citrobacter freundii biotype that causes
RT transmissible murine colonic hyperplasia.";
RL Infect. Immun. 61:2486-2492(1993).
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; L11691; AAA23097.1; -; Genomic_DNA.
DR PIR; I40705; I40705.
DR AlphaFoldDB; Q07591; -.
DR SMR; Q07591; -.
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 Gene3D; 2.40.160.160; -; 1.
DR Gene3D; 2.60.40.10; -; 2.
DR Gene3D; 3.10.100.10; -; 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 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..936
FT /note="Intimin"
FT /id="PRO_0000211825"
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 557..650
FT /note="Big-1 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00445"
FT DOMAIN 657..748
FT /note="Big-1 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00445"
FT DOMAIN 781..831
FT /note="BIG2"
FT /evidence="ECO:0000255"
SQ SEQUENCE 936 AA; 102104 MW; DC8929527D765EFA CRC64;
MIIHGFCTGT RHKHKLRKTF IMLGAGLGLF FSVNQNSFAN GENYFKLRAD SKLINNNIAQ
DRLFYTLKTG ESVAQLSKSQ GISVPVIWSL NKHLYSSESE MMKASPGQQI ILPLKKLSAE
YSTLPILGTA PVVAAADVAG HTKKMSQDTT KSNTSDDKAL NYAAQQAASL GSQLQSRSLN
GDYAKDTALS MAGNQASSQM QAWLQHYGTA EVNLQSGNNF DGSSLDFLLP FYDTENMLAF
GQVGARYIDS RFTANLGAGQ RFFLPENMLG YNVFIDQDFS GNNTRLGIGG EYWRDYFKSS
VNGYFRMSGW HESYNKKDYD ERPANGFDIR FNGYLPSYPA LGGKLMYEQY YGDNVALFNA
DKLYSNPGAV TVGVNYTPIP LVTMGIDYRH GTGNENDLLY SMQFHYQFDK PWSQQIEPQY
VNELRTLSGS RYDLVQRNNN IILDYKKQDI LSMNIPHNIN GTEHSTHKIQ LIVKSKYGLE
RIVWDDSTLR TQGGQIQHSE RKAHNDYQAI LPAYVQGGSN VYKVTRRAYD RNGNSSNNVQ
LTITVLSNGQ VVDKVGITNF TADKTSAKAD NSDTITYTAT VKKNGVAQAN VPVSFNIVSG
TATLSAKSAN TNSSGKATVT LKSDKPGQVV VSAKTAEMTS ALNANAVIFV DQTKASITEI
KVDKTIATAD NKDTIEYTVK VMKGGNPISG QKVTFSKDFG TLNKTEATTD QNGYATVKLS
SGTPGKAIVS AKVSEVNTEV KAATVEFFAP LSIDGNKVTV IGTGVTGSLP KNWLQYGQVK
LQATGGNGKY TWKSSNTKIA SVDNSGVITL NEKGSATITV VSGDNQSATY TINTPDNIII
AVDKINRMAY SEAESRCQAI SSNLAQSKSV LENIYSKWGA ANKYPYYSSS NSLTAWIKQS
TSDSASGVSN TYDLVTTNSL TNVKATDKNA FAVCVK