ID   TIR_ECO1A               Reviewed;         551 AA.
AC   C8UFK8;
DT   14-DEC-2011, integrated into UniProtKB/Swiss-Prot.
DT   03-NOV-2009, sequence version 1.
DT   25-MAY-2022, entry version 51.
DE   RecName: Full=Translocated intimin receptor Tir;
DE   AltName: Full=Secreted effector protein Tir;
GN   Name=tir; Synonyms=espE; OrderedLocusNames=ECO111_3745;
OS   Escherichia coli O111:H- (strain 11128 / EHEC).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=585396;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=11128 / EHEC;
RX   PubMed=19815525; DOI=10.1073/pnas.0903585106;
RA   Ogura Y., Ooka T., Iguchi A., Toh H., Asadulghani M., Oshima K., Kodama T.,
RA   Abe H., Nakayama K., Kurokawa K., Tobe T., Hattori M., Hayashi T.;
RT   "Comparative genomics reveal the mechanism of the parallel evolution of
RT   O157 and non-O157 enterohemorrhagic Escherichia coli.";
RL   Proc. Natl. Acad. Sci. U.S.A. 106:17939-17944(2009).
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; AP010960; BAI37530.1; -; Genomic_DNA.
DR   RefSeq; WP_001369484.1; NC_013364.1.
DR   AlphaFoldDB; C8UFK8; -.
DR   SMR; C8UFK8; -.
DR   IntAct; C8UFK8; 1.
DR   EnsemblBacteria; BAI37530; BAI37530; ECO111_3745.
DR   KEGG; eoi:ECO111_3745; -.
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..551
FT                   /note="Translocated intimin receptor Tir"
FT                   /id="PRO_0000414055"
FT   TOPO_DOM        1..233
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        234..254
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        255..362
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        363..383
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        384..551
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   REGION          1..36
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          186..229
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          259..311
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          389..450
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOTIF           452..454
FT                   /note="Essential for actin pedestal formation"
FT                   /evidence="ECO:0000250"
FT   COMPBIAS        1..15
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        190..204
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        212..229
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        266..304
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        389..416
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        433..450
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   551 AA;  56975 MW;  6EC95F76EF0F44CC CRC64;
     MPIGNLGNNV NSNNLIPPAP PLPSQTDGAS RGGAGQLINS TGALGSRLLF SPLRNSIADS
     VDSRDIPGLP VHPSRLATAT SEICLLGGFE VLHDKGPLDT LNKQIGASAF RIEQQSDGSY
     AAIGEKNGVE VSVILNSQEL QSLQAIDIED KGRFVFTGGR GGGGHSMVTP ASDIAEARAK
     ILAKLDPNNH GGSQARNVDT RSVGVGSASG MDDSVVSETR TSSTASSVRS DPKFWVSIGA
     IAAGLAGLAA TGITQALALT PEPDDPTTTD PEQAASAAES ATRDQLTQEA FKNPENQKVS
     IDEIGNSIPS GELKDDVVAK IEEQAKEAGE AARQQAVESN AQAQQRYDTQ YARRQEELEL
     SSGIGYSLSS ALIVGGGIGA GVTTALHRRN QPAEQTTTTT THTVVQQQTG GNTPAQGGTD
     AIRAEDTSLN RRDSQRSTAS THWSDTSSAV VNPYAEVGEA RNSSPARQAE EHIYDEVAAD
     PNYSVIQNFS GNNQVTGRLM GTPGQGIQST YAILTNNSAG LRLGMGGLTG SGGSAVNTAN
     AAPTPGPGRF V