EAE_ECO27
ID EAE_ECO27 Reviewed; 939 AA.
AC P19809; B7UM97;
DT 01-FEB-1991, integrated into UniProtKB/Swiss-Prot.
DT 05-MAY-2009, sequence version 2.
DT 25-MAY-2022, entry version 139.
DE RecName: Full=Intimin;
DE AltName: Full=Attaching and effacing protein;
DE Short=Eae protein;
GN Name=eae; Synonyms=eaeA; OrderedLocusNames=E2348C_3939;
OS Escherichia coli O127:H6 (strain E2348/69 / EPEC).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=574521;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=E2348/69 / EPEC;
RX PubMed=2172966; DOI=10.1073/pnas.87.20.7839;
RA Jerse A.E., Yu J., Tall B.D., Kaper J.B.;
RT "A genetic locus of enteropathogenic Escherichia coli necessary for the
RT production of attaching and effacing lesions on tissue culture cells.";
RL Proc. Natl. Acad. Sci. U.S.A. 87:7839-7843(1990).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=E2348/69 / EPEC;
RX PubMed=9593291; DOI=10.1046/j.1365-2958.1998.00783.x;
RA Elliott S.J., Wainwright L.A., McDaniel T.K., Jarvis K.G., Deng Y.K.,
RA Lai L.C., McNamara B.P., Donnenberg M.S., Kaper J.B.;
RT "The complete sequence of the locus of enterocyte effacement (LEE) from
RT enteropathogenic Escherichia coli E2348/69.";
RL Mol. Microbiol. 28:1-4(1998).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=E2348/69 / EPEC;
RX PubMed=18952797; DOI=10.1128/jb.01238-08;
RA Iguchi A., Thomson N.R., Ogura Y., Saunders D., Ooka T., Henderson I.R.,
RA Harris D., Asadulghani M., Kurokawa K., Dean P., Kenny B., Quail M.A.,
RA Thurston S., Dougan G., Hayashi T., Parkhill J., Frankel G.;
RT "Complete genome sequence and comparative genome analysis of
RT enteropathogenic Escherichia coli O127:H6 strain E2348/69.";
RL J. Bacteriol. 191:347-354(2009).
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; Single-pass membrane
CC protein.
CC -!- SIMILARITY: Belongs to the intimin/invasin family. {ECO:0000305}.
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; M58154; AAA62775.1; -; Genomic_DNA.
DR EMBL; AF022236; AAC38392.1; -; Genomic_DNA.
DR EMBL; FM180568; CAS11487.1; -; Genomic_DNA.
DR PIR; I41197; I41197.
DR RefSeq; WP_000627890.1; NC_011601.1.
DR PDB; 1E5U; NMR; -; I=753-939.
DR PDB; 1F00; X-ray; 1.90 A; I=658-939.
DR PDB; 1F02; X-ray; 2.90 A; I=658-939.
DR PDB; 2MPW; NMR; -; A=39-143.
DR PDBsum; 1E5U; -.
DR PDBsum; 1F00; -.
DR PDBsum; 1F02; -.
DR PDBsum; 2MPW; -.
DR AlphaFoldDB; P19809; -.
DR BMRB; P19809; -.
DR SASBDB; P19809; -.
DR SMR; P19809; -.
DR IntAct; P19809; 1.
DR ABCD; P19809; 1 sequenced antibody.
DR EnsemblBacteria; CAS11487; CAS11487; E2348C_3939.
DR KEGG; ecg:E2348C_3939; -.
DR HOGENOM; CLU_000210_1_1_6; -.
DR OMA; PENMLGY; -.
DR EvolutionaryTrace; P19809; -.
DR Proteomes; UP000008205; 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; 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; Repeat; Transmembrane;
KW Transmembrane helix; Virulence.
FT CHAIN 1..939
FT /note="Intimin"
FT /id="PRO_0000211827"
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..751
FT /note="Big-1 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00445"
FT CONFLICT 105
FT /note="A -> E (in Ref. 1; AAA62775 and 2; AAC38392)"
FT /evidence="ECO:0000305"
FT HELIX 41..43
FT /evidence="ECO:0007829|PDB:2MPW"
FT STRAND 50..52
FT /evidence="ECO:0007829|PDB:2MPW"
FT HELIX 54..61
FT /evidence="ECO:0007829|PDB:2MPW"
FT STRAND 62..66
FT /evidence="ECO:0007829|PDB:2MPW"
FT HELIX 73..80
FT /evidence="ECO:0007829|PDB:2MPW"
FT HELIX 84..91
FT /evidence="ECO:0007829|PDB:2MPW"
FT TURN 92..94
FT /evidence="ECO:0007829|PDB:2MPW"
FT STRAND 95..97
FT /evidence="ECO:0007829|PDB:2MPW"
FT HELIX 98..102
FT /evidence="ECO:0007829|PDB:2MPW"
FT STRAND 109..113
FT /evidence="ECO:0007829|PDB:2MPW"
FT STRAND 118..121
FT /evidence="ECO:0007829|PDB:2MPW"
FT STRAND 141..143
FT /evidence="ECO:0007829|PDB:2MPW"
FT STRAND 659..666
FT /evidence="ECO:0007829|PDB:1F00"
FT STRAND 668..674
FT /evidence="ECO:0007829|PDB:1F00"
FT STRAND 678..686
FT /evidence="ECO:0007829|PDB:1F00"
FT STRAND 695..706
FT /evidence="ECO:0007829|PDB:1F00"
FT STRAND 708..711
FT /evidence="ECO:0007829|PDB:1F00"
FT STRAND 716..723
FT /evidence="ECO:0007829|PDB:1F00"
FT STRAND 728..730
FT /evidence="ECO:0007829|PDB:1F00"
FT STRAND 732..736
FT /evidence="ECO:0007829|PDB:1F00"
FT STRAND 748..751
FT /evidence="ECO:0007829|PDB:1F00"
FT STRAND 761..763
FT /evidence="ECO:0007829|PDB:1F00"
FT TURN 764..766
FT /evidence="ECO:0007829|PDB:1F00"
FT STRAND 769..771
FT /evidence="ECO:0007829|PDB:1F00"
FT STRAND 774..777
FT /evidence="ECO:0007829|PDB:1F00"
FT STRAND 781..783
FT /evidence="ECO:0007829|PDB:1F00"
FT STRAND 786..788
FT /evidence="ECO:0007829|PDB:1F00"
FT STRAND 790..792
FT /evidence="ECO:0007829|PDB:1E5U"
FT STRAND 793..798
FT /evidence="ECO:0007829|PDB:1F00"
FT TURN 800..802
FT /evidence="ECO:0007829|PDB:1F00"
FT STRAND 803..805
FT /evidence="ECO:0007829|PDB:1F00"
FT TURN 807..809
FT /evidence="ECO:0007829|PDB:1F00"
FT STRAND 811..814
FT /evidence="ECO:0007829|PDB:1F00"
FT STRAND 816..818
FT /evidence="ECO:0007829|PDB:1F00"
FT STRAND 820..826
FT /evidence="ECO:0007829|PDB:1F00"
FT TURN 827..829
FT /evidence="ECO:0007829|PDB:1F00"
FT STRAND 830..836
FT /evidence="ECO:0007829|PDB:1F00"
FT STRAND 840..851
FT /evidence="ECO:0007829|PDB:1F00"
FT HELIX 853..862
FT /evidence="ECO:0007829|PDB:1F00"
FT STRAND 864..866
FT /evidence="ECO:0007829|PDB:1F02"
FT HELIX 871..881
FT /evidence="ECO:0007829|PDB:1F00"
FT HELIX 884..886
FT /evidence="ECO:0007829|PDB:1F00"
FT HELIX 888..890
FT /evidence="ECO:0007829|PDB:1F00"
FT STRAND 897..899
FT /evidence="ECO:0007829|PDB:1F00"
FT HELIX 904..909
FT /evidence="ECO:0007829|PDB:1F00"
FT STRAND 911..916
FT /evidence="ECO:0007829|PDB:1F00"
FT TURN 917..919
FT /evidence="ECO:0007829|PDB:1F00"
FT STRAND 920..927
FT /evidence="ECO:0007829|PDB:1F00"
FT STRAND 928..930
FT /evidence="ECO:0007829|PDB:1E5U"
FT STRAND 933..938
FT /evidence="ECO:0007829|PDB:1F00"
SQ SEQUENCE 939 AA; 102353 MW; C42BC5C0A965B0BD CRC64;
MITHGFYART RHKHKLKKTF IMLSAGLGLF FYVNQNSFAN GENYFKLGSD SKLLTHNSYQ
NRLFYTLKTG ETVADLSKSQ DINLSTIWSL NKHLYSSESE MMKAAPGQQI ILPLKKLPFE
YSALPLLGSA PLVAAGGVAG HTNKLTKMSP DVTKSNMTDD KALNYAAQQA ASLGSQLQSR
SLNGDYAKDT ALGIAGNQAS SQLQAWLQHY GTAEVNLQSG NNFDGSSLDF LLPFYDSEKM
LAFGQVGARY IDSRFTANLG AGQRFFLPEN MLGYNVFIDQ DFSGDNTRLG IGGEYWRDYF
KSSVNGYFRM SGWHESYNKK DYDERPANGF DIRFNGYLPS YPALGAKLMY EQYYGDNVAL
FNSDKLQSNP GAATVGVNYT PIPLVTMGID YRHGTGNEND LLYSMQFRYQ FDKPWSQQIE
PQYVNELRTL SGSRYDLVQR NNNIILEYKK QDILSLNIPH DINGTERSTQ KIQLIVKSKY
GLDRIVWDDS ALRSQGGQIQ HSGSQSAQDY QAILPAYVQG GSNVYKVTAR AYDRNGNSSN
NVLLTITVLS NGQVVDQVGV TDFTADKTSA KADGTEAITY TATVKKNGVA QANVPVSFNI
VSGTAVLSAN SANTNGSGKA TVTLKSDKPG QVVVSAKTAE MTSALNANAV IFVDQTKASI
TEIKADKTTA VANGQDAITY TVKVMKGDKP VSNQEVTFTT TLGKLSNSTE KTDTNGYAKV
TLTSTTPGKS LVSARVSDVA VDVKAPEVEF FTTLTIDDGN IEIVGTGVKG KLPTVWLQYG
QVNLKASGGN GKYTWRSANP AIASVDASSG QVTLKEKGTT TISVISSDNQ TATYTIATPN
SLIVPNMSKR VTYNDAVNTC KNFGGKLPSS QNELENVFKA WGAANKYEYY KSSQTIISWV
QQTAQDAKSG VASTYDLVKQ NPLNNIKASE SNAYATCVK
