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TIR_ECO5E
ID   TIR_ECO5E               Reviewed;         558 AA.
AC   B5YWI0;
DT   14-DEC-2011, integrated into UniProtKB/Swiss-Prot.
DT   25-NOV-2008, sequence version 1.
DT   25-MAY-2022, entry version 53.
DE   RecName: Full=Translocated intimin receptor Tir;
DE   AltName: Full=Secreted effector protein Tir;
GN   Name=tir; Synonyms=espE; OrderedLocusNames=ECH74115_5056;
OS   Escherichia coli O157:H7 (strain EC4115 / EHEC).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=444450;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=EC4115 / EHEC;
RX   PubMed=22135463; DOI=10.1073/pnas.1107176108;
RA   Eppinger M., Mammel M.K., Leclerc J.E., Ravel J., Cebula T.A.;
RT   "Genomic anatomy of Escherichia coli O157:H7 outbreaks.";
RL   Proc. Natl. Acad. Sci. U.S.A. 108:20142-20147(2011).
CC   -!- FUNCTION: Multifunctional protein that is required for efficient
CC       pedestal formation in host epithelial cells during infection. The
CC       extracellular region acts as a receptor for bacterial intimin, allowing
CC       the bacterium to attach tightly to the host-cell surface.
CC       Simultaneously, the intracellular region initiates a signaling cascade
CC       in the host cell, which leads to actin polymerization and formation of
CC       actin pedestals at the sites of bacterial adhesion (By similarity).
CC       {ECO:0000250}.
CC   -!- SUBUNIT: Interacts with intimin and host proteins. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000250}. Host cell membrane
CC       {ECO:0000250}; Multi-pass membrane protein {ECO:0000250}. Note=Secreted
CC       via the type III secretion system (TTSS). Released into the host
CC       cytoplasm via TTSS and then independently inserts into the plasma
CC       membrane from a cytoplasmic location. In host cells, localizes to the
CC       tip of the actin pedestal (By similarity). {ECO:0000250}.
CC   -!- PTM: Phosphorylated by host kinases. {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the Tir receptor family. {ECO:0000305}.
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DR   EMBL; CP001164; ACI36828.1; -; Genomic_DNA.
DR   RefSeq; WP_001301454.1; NC_011353.1.
DR   AlphaFoldDB; B5YWI0; -.
DR   SMR; B5YWI0; -.
DR   KEGG; ecf:ECH74115_5056; -.
DR   HOGENOM; CLU_497576_0_0_6; -.
DR   OMA; QGIQSTY; -.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0020002; C:host cell plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   Gene3D; 4.10.820.10; -; 1.
DR   InterPro; IPR037003; Tir_central_sf.
DR   InterPro; IPR022638; Transloc_intimin_rcpt.
DR   InterPro; IPR022639; Transloc_intimin_rcpt_C.
DR   InterPro; IPR003536; Transloc_intimin_rcpt_cen_dom.
DR   InterPro; IPR022633; Transloc_intimin_rcpt_N.
DR   Pfam; PF07489; Tir_receptor_C; 1.
DR   Pfam; PF03549; Tir_receptor_M; 1.
DR   Pfam; PF07490; Tir_receptor_N; 1.
DR   PRINTS; PR01370; TRNSINTIMINR.
PE   3: Inferred from homology;
KW   Host cell membrane; Host membrane; Membrane; Phosphoprotein; Receptor;
KW   Secreted; Transmembrane; Transmembrane helix; Virulence.
FT   CHAIN           1..558
FT                   /note="Translocated intimin receptor Tir"
FT                   /id="PRO_0000414056"
FT   TOPO_DOM        1..230
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        231..251
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        252..362
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        363..383
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        384..558
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   REGION          1..44
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          182..226
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          257..280
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          388..451
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          533..558
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOTIF           456..458
FT                   /note="Essential for actin pedestal formation"
FT                   /evidence="ECO:0000250"
FT   COMPBIAS        30..44
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        206..226
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        258..280
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        537..552
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   558 AA;  58022 MW;  99C417222D4B4AA1 CRC64;
     MPIGNLGHNP NVNNSIPPAP PLPSQTDGAG GRGQLINSTG PLGSRALFTP VRNSMADSGD
     NRASDVPGLP VNPMRLAASE ITLNDGFEVL HDHGPLDTLN RQIGSSVFRV ETQEDGKHIA
     VGQRNGVETS VVLSDQEYAR LQSIDPEGKD KFVFTGGRGG AGHAMVTVAS DITEARQRIL
     ELLEPKGTGE SKGAGESKGV GELRESNSGA ENTTETQTST STSSLRSDPK LWLALGTVAT
     GLIGLAATGI VQALALTPEP DSPTTTDPDA AASATETATR DQLTKEAFQN PDNQKVNIDE
     LGNAIPSGVL KDDVVANIEE QAKAAGEEAK QQAIENNAQA QKKYDEQQAK RQEELKVSSG
     AGYGLSGALI LGGGIGVAVT AALHRKNQPV EQTTTTTTTT TTTSARTVEN KPANNTPAQG
     NVDTPGSEDT MESRRSSMAS TSSTFFDTSS IGTVQNPYAD VKTSLHDSQV PTSNSNTSVQ
     NMGNTDSVVY STIQHPPRDT TDNGARLLGN PSAGIQSTYA RLALSGGLRH DMGGLTGGSN
     SAVNTSNNPP APGSHRFV
 
 
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