##gff-version 3
B7UM99	UniProtKB	Chain	1	550	.	.	.	ID=PRO_0000414050;Note=Translocated intimin receptor Tir	
B7UM99	UniProtKB	Topological domain	1	233	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
B7UM99	UniProtKB	Transmembrane	234	254	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
B7UM99	UniProtKB	Topological domain	255	362	.	.	.	Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255	
B7UM99	UniProtKB	Transmembrane	363	383	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
B7UM99	UniProtKB	Topological domain	384	550	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
B7UM99	UniProtKB	Region	1	38	.	.	.	Note=Disordered;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite	
B7UM99	UniProtKB	Region	185	228	.	.	.	Note=Disordered;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite	
B7UM99	UniProtKB	Region	260	285	.	.	.	Note=Disordered;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite	
B7UM99	UniProtKB	Region	332	354	.	.	.	Note=Disordered;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite	
B7UM99	UniProtKB	Region	389	449	.	.	.	Note=Disordered;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite	
B7UM99	UniProtKB	Motif	452	454	.	.	.	Note=Essential for NCK-independent actin pedestal formation	
B7UM99	UniProtKB	Compositional bias	214	228	.	.	.	Note=Polar residues;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite	
B7UM99	UniProtKB	Compositional bias	266	285	.	.	.	Note=Polar residues;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite	
B7UM99	UniProtKB	Compositional bias	389	419	.	.	.	Note=Polar residues;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite	
B7UM99	UniProtKB	Compositional bias	431	449	.	.	.	Note=Polar residues;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite	
B7UM99	UniProtKB	Modified residue	454	454	.	.	.	Note=Phosphotyrosine;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:15813734;Dbxref=PMID:15813734	
B7UM99	UniProtKB	Modified residue	474	474	.	.	.	Note=Phosphotyrosine;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:15813734,ECO:0000269|PubMed:16636066;Dbxref=PMID:15813734,PMID:16636066	
B7UM99	UniProtKB	Mutagenesis	452	452	.	.	.	Note=Lack of pedestal formation%3B when associated with F-474. N->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:17521329;Dbxref=PMID:17521329	
B7UM99	UniProtKB	Mutagenesis	453	453	.	.	.	Note=Lack of pedestal formation%3B when associated with F-474. P->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:17521329;Dbxref=PMID:17521329	
B7UM99	UniProtKB	Mutagenesis	454	454	.	.	.	Note=Lack of pedestal formation%3B when associated with F-474. Y->A;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:15813734,ECO:0000269|PubMed:17521329;Dbxref=PMID:15813734,PMID:17521329	
B7UM99	UniProtKB	Mutagenesis	454	454	.	.	.	Note=Does not inhibit translocation into the host cell. Almost no change in actin polymerization. Lack of pedestal formation%3B when associated with F-474. Y->F;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:15813734,ECO:0000269|PubMed:17521329;Dbxref=PMID:15813734,PMID:17521329	
B7UM99	UniProtKB	Mutagenesis	474	474	.	.	.	Note=Loss of phosphorylation and strong decrease in actin polymerization. Y->D%2CE;Ontology_term=ECO:0000269,ECO:0000269,ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:10096089,ECO:0000269|PubMed:11918809,ECO:0000269|PubMed:15813734,ECO:0000269|PubMed:17521329;Dbxref=PMID:10096089,PMID:11918809,PMID:15813734,PMID:17521329	
B7UM99	UniProtKB	Mutagenesis	474	474	.	.	.	Note=Loss of phosphorylation and strong decrease in actin polymerization. Lack of pedestal formation%3B when associated with F-454. Y->F;Ontology_term=ECO:0000269,ECO:0000269,ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:10096089,ECO:0000269|PubMed:11918809,ECO:0000269|PubMed:15813734,ECO:0000269|PubMed:17521329;Dbxref=PMID:10096089,PMID:11918809,PMID:15813734,PMID:17521329	
B7UM99	UniProtKB	Mutagenesis	474	474	.	.	.	Note=Does not inhibit translocation into the host cell. Loss of phosphorylation and strong decrease in actin polymerization. Y->S;Ontology_term=ECO:0000269,ECO:0000269,ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:10096089,ECO:0000269|PubMed:11918809,ECO:0000269|PubMed:15813734,ECO:0000269|PubMed:17521329;Dbxref=PMID:10096089,PMID:11918809,PMID:15813734,PMID:17521329	
B7UM99	UniProtKB	Mutagenesis	483	483	.	.	.	Note=Does not inhibit translocation into the host cell. Y->S;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:10096089;Dbxref=PMID:10096089	
B7UM99	UniProtKB	Sequence conflict	412	430	.	.	.	Note=NTPAQGGTDATRAEDASLN->IPQHKVALMPQERRRFSD;Ontology_term=ECO:0000305;evidence=ECO:0000305	
B7UM99	UniProtKB	Sequence conflict	533	533	.	.	.	Note=S->T;Ontology_term=ECO:0000305;evidence=ECO:0000305	
B7UM99	UniProtKB	Beta strand	41	43	.	.	.	Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:5WEZ	
B7UM99	UniProtKB	Beta strand	46	50	.	.	.	Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:5WEZ