GenomeNet

Database: Pfam
Entry: Tir_receptor_N
LinkDB: Tir_receptor_N
Original site: Tir_receptor_N 
#=GF ID   Tir_receptor_N
#=GF AC   PF07490.15
#=GF DE   Translocated intimin receptor (Tir) N-terminus
#=GF AU   Griffiths-Jones SR;0000-0001-6043-807X
#=GF AU   Moxon SJ;0000-0003-4644-1816
#=GF SE   PRINTS
#=GF GA   25.00 25.00;
#=GF TC   42.00 442.30;
#=GF NC   21.30 20.60;
#=GF BM   hmmbuild HMM.ann SEED.ann
#=GF SM   hmmsearch -Z 75585367 -E 1000 --cpu 4 HMM pfamseq
#=GF TP   Family
#=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; IPR022633;
#=GF DR   SCOP; 1f02; fa;
#=GF DR   SO; 0100021; polypeptide_conserved_region;
#=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 N-terminal domain  which is
#=GF CC   involved in Tir stability and Tir secretion [2].
#=GF SQ   2
#=GS TIR_ECO57/1-267     AC Q7DB77.1
#=GS D2TKE8_CITRI/1-268  AC D2TKE8.1
TIR_ECO57/1-267                MPIGNLGHNPNVNNSIPPAPPLPSQTDG.A-GGRGQLINSTGPLGSRALFTPVRNSMADSGDNRASDVPGLPVNPMRLAASEITLNDGFEVLHDHGPLDTLNRQIGSSVFRVETQEDGKHIAVGQRNGVETSVVLSDQEYARLQSIDPEGKDKFVFTGGRGGAGHAMVTVASDITEARQRILELLEPKGTGESKGAGESKGVGELRESNSG-AENTTETQTSTSTSSLRSDPKLWLALGTVATGLIGLAATGIVQALALTPEPDSPTTTD
D2TKE8_CITRI/1-268             MPIGNLGNNNISNNLIPPAPPLPSQTDGaTRGNGSSLISSTGSLGSRLLFSPLRSSIVDTVDSR--DVPGLPEHPLRFATSETCLHGGFEVLHDKGPLDTLNQKIGSSVFRVEQQPDGTHAAIGVKDGVEVSVTLNSSELQSLQSLDTEGNGRFVFTGGRGGSGHAMVTVASDISQAREKIIAKLDPDNHGGRQPKDIDTRSVGVGSASGMGDGVVSETHTSTTTSSVRSDPKFWVSVGAIAAGLAGLAATGIVQAVALTPAPDDPTTTD
#=GC seq_cons                  MPIGNLGpNs.sNN.IPPAPPLPSQTDG.s.GstupLIsSTGsLGSRhLFoPlRsShsDosDsR..DVPGLP.pPhRhAsSEhsLpsGFEVLHD+GPLDTLNppIGSSVFRVEpQ.DGpHhAlG.+sGVEsSVsLsspEhtpLQSlDsEGps+FVFTGGRGGuGHAMVTVASDIopARp+IlthL-PcspGtppsts.sptsstltpusuh.stssoETpTSToTSSlRSDPKhWlulGslAsGLhGLAATGIVQAlALTPtPDsPTTTD
//
DBGET integrated database retrieval system