EAE_ECO57
ID EAE_ECO57 Reviewed; 934 AA.
AC P43261; O85627; Q47168;
DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT 29-AUG-2001, sequence version 2.
DT 03-AUG-2022, entry version 156.
DE RecName: Full=Intimin;
DE AltName: Full=Attaching and effacing protein;
DE Short=Eae protein;
DE AltName: Full=Gamma-intimin;
GN Name=eae; Synonyms=eaeA; OrderedLocusNames=Z5110, ECs4559; ORFNames=L0025;
OS Escherichia coli O157:H7.
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=83334;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=O157:H7 / EDL933 / ATCC 700927 / EHEC;
RX PubMed=1552854; DOI=10.1111/j.1365-2958.1992.tb01484.x;
RA Yu J., Kaper J.B.;
RT "Cloning and characterization of the eae gene of enterohaemorrhagic
RT Escherichia coli O157:H7.";
RL Mol. Microbiol. 6:411-417(1992).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=O157:H7 / CL-8;
RX PubMed=1577255; DOI=10.1016/0378-1097(92)90563-4;
RA Beebakhee G., Louie M., de Azavedo J., Brunton J.;
RT "Cloning and nucleotide sequence of the eae gene homologue from
RT enterohemorrhagic Escherichia coli serotype O157:H7.";
RL FEMS Microbiol. Lett. 70:63-68(1992).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=O157:H7 / EDL933 / ATCC 700927 / EHEC;
RX PubMed=9673266; DOI=10.1128/iai.66.8.3810-3817.1998;
RA Perna N.T., Mayhew G.F., Posfai G., Elliott S., Donnenberg M.S.,
RA Kaper J.B., Blattner F.R.;
RT "Molecular evolution of a pathogenicity island from enterohemorrhagic
RT Escherichia coli O157:H7.";
RL Infect. Immun. 66:3810-3817(1998).
RN [4]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=O157:H- / DEC 3f / EHEC, and O157:H7 / DEC 3a / EHEC;
RX PubMed=10331248; DOI=10.1093/oxfordjournals.molbev.a026032;
RA McGraw E.A., Li J., Selander R.K., Whittam T.S.;
RT "Molecular evolution and mosaic structure of alpha, beta, and gamma
RT intimins of pathogenic Escherichia coli.";
RL Mol. Biol. Evol. 16:12-22(1999).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=O157:H7 / EDL933 / ATCC 700927 / EHEC;
RX PubMed=11206551; DOI=10.1038/35054089;
RA Perna N.T., Plunkett G. III, Burland V., Mau B., Glasner J.D., Rose D.J.,
RA Mayhew G.F., Evans P.S., Gregor J., Kirkpatrick H.A., Posfai G.,
RA Hackett J., Klink S., Boutin A., Shao Y., Miller L., Grotbeck E.J.,
RA Davis N.W., Lim A., Dimalanta E.T., Potamousis K., Apodaca J.,
RA Anantharaman T.S., Lin J., Yen G., Schwartz D.C., Welch R.A.,
RA Blattner F.R.;
RT "Genome sequence of enterohaemorrhagic Escherichia coli O157:H7.";
RL Nature 409:529-533(2001).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=O157:H7 / Sakai / RIMD 0509952 / EHEC;
RX PubMed=11258796; DOI=10.1093/dnares/8.1.11;
RA Hayashi T., Makino K., Ohnishi M., Kurokawa K., Ishii K., Yokoyama K.,
RA Han C.-G., Ohtsubo E., Nakayama K., Murata T., Tanaka M., Tobe T., Iida T.,
RA Takami H., Honda T., Sasakawa C., Ogasawara N., Yasunaga T., Kuhara S.,
RA Shiba T., Hattori M., Shinagawa H.;
RT "Complete genome sequence of enterohemorrhagic Escherichia coli O157:H7 and
RT genomic comparison with a laboratory strain K-12.";
RL DNA Res. 8:11-22(2001).
RN [7]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-37.
RC STRAIN=O157:H7 / HA1 / EHEC;
RX PubMed=8566710; DOI=10.1111/j.1574-6968.1995.tb07856.x;
RA Zhao S., Mitchell S.E., Meng J., Doyle M.P., Kresovich S.;
RT "Cloning and nucleotide sequence of a gene upstream of the eaeA gene of
RT enterohemorrhagic Escherichia coli O157:H7.";
RL FEMS Microbiol. Lett. 133:35-39(1995).
RN [8]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 684-928.
RX PubMed=8005211; DOI=10.1017/s0950268800051153;
RA Louie M., de Azavedo J., Clarke R., Borczyk A., Lior H., Richter M.,
RA Brunton J.;
RT "Sequence heterogeneity of the eae gene and detection of verotoxin-
RT producing Escherichia coli using serotype-specific primers.";
RL Epidemiol. Infect. 112:449-461(1994).
CC -!- FUNCTION: Necessary for the production of attaching and effacing
CC lesions on tissue culture cells.
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; Z11541; CAA77642.1; -; Genomic_DNA.
DR EMBL; X60439; CAA42967.1; -; Genomic_DNA.
DR EMBL; AF071034; AAC31504.1; -; Genomic_DNA.
DR EMBL; AF081182; AAD05498.1; -; Genomic_DNA.
DR EMBL; AF081183; AAD05499.1; -; Genomic_DNA.
DR EMBL; AE005174; AAG58823.1; -; Genomic_DNA.
DR EMBL; BA000007; BAB37982.1; -; Genomic_DNA.
DR EMBL; U32312; AAB00111.1; -; Genomic_DNA.
DR EMBL; L08095; AAA21468.1; -; Genomic_DNA.
DR PIR; C86045; C86045.
DR PIR; G91198; G91198.
DR PIR; I41193; I41193.
DR RefSeq; NP_312586.1; NC_002695.1.
DR RefSeq; WP_000627885.1; NZ_SWKA01000005.1.
DR PDB; 2ZQK; X-ray; 2.80 A; A/B=747-934.
DR PDB; 2ZWK; X-ray; 3.10 A; A/C/E=752-934.
DR PDB; 3NCW; X-ray; 2.80 A; A/B/C/D=747-934.
DR PDB; 3NCX; X-ray; 2.60 A; A/B=747-934.
DR PDB; 4E1S; X-ray; 1.86 A; A=208-449.
DR PDB; 5G26; X-ray; 2.42 A; A=208-449.
DR PDBsum; 2ZQK; -.
DR PDBsum; 2ZWK; -.
DR PDBsum; 3NCW; -.
DR PDBsum; 3NCX; -.
DR PDBsum; 4E1S; -.
DR PDBsum; 5G26; -.
DR AlphaFoldDB; P43261; -.
DR BMRB; P43261; -.
DR SMR; P43261; -.
DR STRING; 155864.EDL933_4947; -.
DR TCDB; 1.B.54.1.1; the intimin/invasin (int/inv) or autotransporter-3 (at-3) family.
DR EnsemblBacteria; AAG58823; AAG58823; Z5110.
DR EnsemblBacteria; BAB37982; BAB37982; ECs_4559.
DR GeneID; 915471; -.
DR KEGG; ece:Z5110; -.
DR KEGG; ecs:ECs_4559; -.
DR PATRIC; fig|386585.9.peg.4776; -.
DR eggNOG; COG5492; Bacteria.
DR HOGENOM; CLU_000210_1_1_6; -.
DR OMA; PENMLGY; -.
DR EvolutionaryTrace; P43261; -.
DR PHI-base; PHI:7913; -.
DR Proteomes; UP000000558; Chromosome.
DR Proteomes; UP000002519; Chromosome.
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 1: Evidence at protein level;
KW 3D-structure; Cell outer membrane; Membrane; Reference proteome; Repeat;
KW Transmembrane; Transmembrane helix; Virulence.
FT CHAIN 1..934
FT /note="Intimin"
FT /id="PRO_0000211828"
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..753
FT /note="Big-1 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00445"
FT DOMAIN 787..834
FT /note="BIG2"
FT /evidence="ECO:0000255"
FT CONFLICT 221
FT /note="N -> D (in Ref. 1; CAA77642)"
FT /evidence="ECO:0000305"
FT CONFLICT 311..312
FT /note="SG -> RR (in Ref. 1; CAA77642)"
FT /evidence="ECO:0000305"
FT CONFLICT 318
FT /note="N -> H (in Ref. 1; CAA77642)"
FT /evidence="ECO:0000305"
FT CONFLICT 642
FT /note="T -> S (in Ref. 1; CAA77642)"
FT /evidence="ECO:0000305"
FT CONFLICT 769
FT /note="V -> VK (in Ref. 2)"
FT /evidence="ECO:0000305"
FT CONFLICT 771..772
FT /note="GE -> SM (in Ref. 2)"
FT /evidence="ECO:0000305"
FT CONFLICT 903
FT /note="R -> S (in Ref. 8; AAA21468)"
FT /evidence="ECO:0000305"
FT STRAND 212..221
FT /evidence="ECO:0007829|PDB:4E1S"
FT STRAND 225..236
FT /evidence="ECO:0007829|PDB:4E1S"
FT STRAND 238..251
FT /evidence="ECO:0007829|PDB:4E1S"
FT STRAND 254..266
FT /evidence="ECO:0007829|PDB:4E1S"
FT STRAND 271..281
FT /evidence="ECO:0007829|PDB:4E1S"
FT TURN 282..285
FT /evidence="ECO:0007829|PDB:4E1S"
FT STRAND 286..297
FT /evidence="ECO:0007829|PDB:4E1S"
FT STRAND 300..309
FT /evidence="ECO:0007829|PDB:4E1S"
FT STRAND 317..319
FT /evidence="ECO:0007829|PDB:4E1S"
FT STRAND 323..326
FT /evidence="ECO:0007829|PDB:4E1S"
FT STRAND 329..338
FT /evidence="ECO:0007829|PDB:4E1S"
FT STRAND 341..353
FT /evidence="ECO:0007829|PDB:4E1S"
FT STRAND 355..358
FT /evidence="ECO:0007829|PDB:4E1S"
FT STRAND 363..365
FT /evidence="ECO:0007829|PDB:4E1S"
FT STRAND 367..369
FT /evidence="ECO:0007829|PDB:4E1S"
FT STRAND 371..382
FT /evidence="ECO:0007829|PDB:4E1S"
FT STRAND 385..394
FT /evidence="ECO:0007829|PDB:4E1S"
FT HELIX 395..397
FT /evidence="ECO:0007829|PDB:4E1S"
FT STRAND 398..410
FT /evidence="ECO:0007829|PDB:4E1S"
FT HELIX 415..418
FT /evidence="ECO:0007829|PDB:4E1S"
FT HELIX 423..428
FT /evidence="ECO:0007829|PDB:4E1S"
FT TURN 430..432
FT /evidence="ECO:0007829|PDB:4E1S"
FT STRAND 446..448
FT /evidence="ECO:0007829|PDB:4E1S"
FT STRAND 760..764
FT /evidence="ECO:0007829|PDB:3NCX"
FT TURN 765..768
FT /evidence="ECO:0007829|PDB:3NCX"
FT STRAND 769..772
FT /evidence="ECO:0007829|PDB:3NCX"
FT STRAND 775..778
FT /evidence="ECO:0007829|PDB:3NCX"
FT STRAND 782..784
FT /evidence="ECO:0007829|PDB:3NCX"
FT STRAND 787..789
FT /evidence="ECO:0007829|PDB:3NCX"
FT STRAND 794..799
FT /evidence="ECO:0007829|PDB:3NCX"
FT TURN 801..803
FT /evidence="ECO:0007829|PDB:3NCX"
FT STRAND 804..806
FT /evidence="ECO:0007829|PDB:3NCX"
FT STRAND 810..814
FT /evidence="ECO:0007829|PDB:3NCX"
FT STRAND 816..818
FT /evidence="ECO:0007829|PDB:3NCX"
FT STRAND 820..826
FT /evidence="ECO:0007829|PDB:3NCX"
FT TURN 827..829
FT /evidence="ECO:0007829|PDB:2ZWK"
FT STRAND 831..836
FT /evidence="ECO:0007829|PDB:3NCX"
FT STRAND 842..848
FT /evidence="ECO:0007829|PDB:3NCX"
FT HELIX 851..857
FT /evidence="ECO:0007829|PDB:3NCX"
FT TURN 858..860
FT /evidence="ECO:0007829|PDB:3NCX"
FT HELIX 866..876
FT /evidence="ECO:0007829|PDB:3NCX"
FT HELIX 879..881
FT /evidence="ECO:0007829|PDB:3NCX"
FT HELIX 883..885
FT /evidence="ECO:0007829|PDB:3NCX"
FT STRAND 892..894
FT /evidence="ECO:0007829|PDB:3NCX"
FT HELIX 899..904
FT /evidence="ECO:0007829|PDB:3NCX"
FT STRAND 906..911
FT /evidence="ECO:0007829|PDB:3NCX"
FT TURN 912..914
FT /evidence="ECO:0007829|PDB:3NCX"
FT STRAND 917..922
FT /evidence="ECO:0007829|PDB:3NCX"
FT STRAND 929..933
FT /evidence="ECO:0007829|PDB:3NCX"
SQ SEQUENCE 934 AA; 101836 MW; BE73686D7F79D3C9 CRC64;
MITHGCYTRT RHKHKLKKTL IMLSAGLGLF FYVNQNSFAN GENYFKLGSD SKLLTHDSYQ
NRLFYTLKTG ETVADLSKSQ DINLSTIWSL NKHLYSSESE MMKAAPGQQI ILPLKKLPFE
YSALPLLGSA PLVAAGGVAG HTNKLTKMSP DVTKSNMTDD KALNYAAQQA ASLGSQLQSR
SLNGDYAKDT ALGIAGNQAS SQLQAWLQHY GTAEVNLQSG NNFDGSSLDF LLPFYDSEKM
LAFGQVGARY IDSRFTANLG AGQRFFLPAN MLGYNVFIDQ DFSGDNTRLG IGGEYWRDYF
KSSVNGYFRM SGWHESYNKK DYDERPANGF DIRFNGYLPS YPALGAKLIY EQYYGDNVAL
FNSDKLQSNP GAATVGVNYT PIPLVTMGID YRHGTGNEND LLYSMQFRYQ FDKSWSQQIE
PQYVNELRTL SGSRYDLVQR NNNIILEYKK QDILSLNIPH DINGTEHSTQ KIQLIVKSKY
GLDRIVWDDS ALRSQGGQIQ HSGSQSAQDY QAILPAYVQG GSNIYKVTAR AYDRNGNSSN
NVQLTITVLS NGQVVDQVGV TDFTADKTSA KADNADTITY TATVKKNGVA QANVPVSFNI
VSGTATLGAN SAKTDANGKA TVTLKSSTPG QVVVSAKTAE MTSALNASAV IFFDQTKASI
TEIKADKTTA VANGKDAIKY TVKVMKNGQP VNNQSVTFST NFGMFNGKSQ TQATTGNDGR
ATITLTSSSA GKATVSATVS DGAEVKATEV TFFDELKIDN KVDIIGNNVR GELPNIWLQY
GQFKLKASGG DGTYSWYSEN TSIATVDASG KVTLNGKGSV VIKATSGDKQ TVSYTIKAPS
YMIKVDKQAY YADAMSICKN LLPSTQTVLS DIYDSWGAAN KYSHYSSMNS ITAWIKQTSS
EQRSGVSSTY NLITQNPLPG VNVNTPNVYA VCVE
