#=GF ID   Tir_receptor_C
#=GF AC   PF07489.15
#=GF DE   Translocated intimin receptor (Tir) C-terminus
#=GF AU   Moxon SJ;0000-0003-4644-1816
#=GF SE   PRINTS
#=GF GA   25.00 25.00;
#=GF TC   34.90 359.60;
#=GF NC   23.90 23.20;
#=GF BM   hmmbuild HMM.ann SEED.ann
#=GF SM   hmmsearch -Z 75585367 --cpu 4 -E 1000 HMM pfamseq
#=GF TP   Domain
#=GF RN   [1]
#=GF RM   10890451
#=GF RT   Crystal structure of enteropathogenic Escherichia coli
#=GF RT   intimin-receptor complex. 
#=GF RA   Luo Y, Frey EA, Pfuetzner RA, Creagh AL, Knoechel DG, Haynes CA,
#=GF RA   Finlay BB, Strynadka NC; 
#=GF RL   Nature 2000;405:1073-1077.
#=GF RN   [2]
#=GF RM   11207537
#=GF RT   Identification of the intimin-binding domain of Tir of
#=GF RT   enteropathogenic Escherichia coli. 
#=GF RA   de Grado M, Abe A, Gauthier A, Steele-Mortimer O, DeVinney R,
#=GF RA   Finlay BB; 
#=GF RL   Cell Microbiol 1999;1:7-17.
#=GF DR   INTERPRO; IPR022639;
#=GF DR   SCOP; 1f02; fa;
#=GF DR   SO; 0000417; polypeptide_domain;
#=GF CC   Intimin and its translocated intimin receptor (Tir) are
#=GF CC   bacterial proteins that mediate adhesion between mammalian cells
#=GF CC   and attaching and effacing (A/E) pathogens. A unique and
#=GF CC   essential feature of A/E bacterial pathogens is the formation of
#=GF CC   actin-rich pedestals beneath the intimately adherent bacteria
#=GF CC   and localised destruction of the intestinal brush border. The
#=GF CC   bacterial outer membrane adhesin, intimin, is necessary for the
#=GF CC   production of the A/E lesion and diarrhoea. The A/E bacteria
#=GF CC   translocate their own receptor for intimin, Tir, into the
#=GF CC   membrane of mammalian cells using the type III secretion system.
#=GF CC   The translocated Tir triggers additional host signalling events
#=GF CC   and actin nucleation, which are essential for lesion formation
#=GF CC   [1]. This family represents the Tir C-terminal domain  which has
#=GF CC   been reported to bind uninfected host cells and beta-1 integrins
#=GF CC   although the role of intimin binding to integrins is unclear.
#=GF CC   This intimin C-terminal domain has also been shown to be
#=GF CC   sufficient for Tir recognition [2].
#=GF SQ   2
#=GS D2TKE8_CITRI/335-547  AC D2TKE8.1
#=GS TIR_ECO57/334-558     AC Q7DB77.1
D2TKE8_CITRI/335-547             VESNAQAQQRHDDQQAKRQQELDLSSGIGYGLSSALIVGGGIGAGVTAMLHRRNPPTEQ-TIATTHSV-----.IQQQTGGNTRAQGGADTTGVENASLTRRDSQASVAStQWSDTS-GDVV-NPYAEGWMSRNNPSL..LAPEEPIYDEVAPD-PNYSVIQHFSGNNPVT.GRLVGSPGQGIQSTYALLASSGGLRLGMGGLTGGGESAGSAANAATTPGVERFV
TIR_ECO57/334-558                IENNAQAQKKYDEQQAKRQEELKVSSGAGYGLSGALILGGGIGVAVTAALHRKNQPVEQTTTTTTTTTTTSARtVENKPANNTPAQGNVDTPGSEDTMESRRSSMASTSS.TFFDTSSIGTVQNPYADVKTSLHDSQVptSNSNTSVQNMGNTDSVVYSTIQHPPRDTTDNgARLLGNPSAGIQSTYARLALSGGLRHDMGGLTGGSNSAVNTSNNPPAPGSHRFV
#=GC seq_cons                    lEsNAQAQp+aD-QQAKRQpELclSSGhGYGLSuALIlGGGIGsuVTAhLHR+N.PsEQ.ThsTTpos......lpppsusNT.AQGssDTsGsEss..oRRsS.ASsuS.pa.DTS.hssV.NPYA-shhShpsspl...ssppsl.s.sssD.ssYSsIQH.stsssss.uRLlGsPutGIQSTYAhLA.SGGLRhsMGGLTGGupSAsssuNssssPGscRFV
//