TIR1_ECOLX
ID TIR1_ECOLX Reviewed; 538 AA.
AC P0DJ90; Q47014;
DT 14-DEC-2011, integrated into UniProtKB/Swiss-Prot.
DT 14-DEC-2011, sequence version 1.
DT 25-MAY-2022, entry version 40.
DE RecName: Full=Translocated intimin receptor Tir;
DE AltName: Full=Secreted effector protein Tir;
GN Name=tir; Synonyms=espE;
OS Escherichia coli.
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=562;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=O26:H- / 95ZG1 / EHEC;
RX PubMed=9784578; DOI=10.1128/iai.66.11.5580-5586.1998;
RA Paton A.W., Manning P.A., Woodrow M.C., Paton J.C.;
RT "Translocated intimin receptors (Tir) of Shiga-toxigenic Escherichia coli
RT isolates belonging to serogroups O26, O111, and O157 react with sera from
RT patients with hemolytic-uremic syndrome and exhibit marked sequence
RT heterogeneity.";
RL Infect. Immun. 66:5580-5586(1998).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 2-19, SUBCELLULAR
RP LOCATION, AND PHOSPHORYLATION.
RC STRAIN=O26:H- / 413/89-1 / EHEC;
RX PubMed=9632251; DOI=10.1046/j.1365-2958.1998.00798.x;
RA Deibel C., Kramer S., Chakraborty T., Ebel F.;
RT "EspE, a novel secreted protein of attaching and effacing bacteria, is
RT directly translocated into infected host cells, where it appears as a
RT tyrosine-phosphorylated 90 kDa protein.";
RL Mol. Microbiol. 28:463-474(1998).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=O26:H- / 413/89-1 / EHEC;
RA Benkel P., Chakraborty T.;
RT "Genetic organisation and sequence of the LEE II locus in Shiga toxin-
RT producing Escherichia coli.";
RL Submitted (APR-2000) to the EMBL/GenBank/DDBJ databases.
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:0000269|PubMed:9632251}. Host cell
CC membrane {ECO:0000269|PubMed:9632251}; Multi-pass membrane protein
CC {ECO:0000269|PubMed:9632251}. Note=Secreted via the type III secretion
CC system (TTSS). Released into the host cytoplasm via TTSS and then
CC independently inserts into the plasma membrane from a cytoplasmic
CC location. In host cells, localizes to the tip of the actin pedestal.
CC -!- PTM: Phosphorylated by host kinases. {ECO:0000269|PubMed:9632251}.
CC -!- SIMILARITY: Belongs to the Tir receptor family. {ECO:0000305}.
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DR EMBL; AF070068; AAC69316.1; -; Genomic_DNA.
DR EMBL; AJ223063; CAA11065.1; -; Genomic_DNA.
DR EMBL; AJ277443; CAC81869.1; -; Genomic_DNA.
DR RefSeq; WP_001121330.1; NZ_WJGB01000091.1.
DR AlphaFoldDB; P0DJ90; -.
DR SMR; P0DJ90; -.
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 1: Evidence at protein level;
KW Direct protein sequencing; Host cell membrane; Host membrane; Membrane;
KW Phosphoprotein; Receptor; Secreted; Transmembrane; Transmembrane helix;
KW Virulence.
FT CHAIN 1..538
FT /note="Translocated intimin receptor Tir"
FT /id="PRO_0000414052"
FT TOPO_DOM 1..222
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 223..243
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 244..354
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 355..375
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 376..538
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT REGION 1..37
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 184..204
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 279..299
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 313..347
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 380..449
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 440..442
FT /note="Essential for actin pedestal formation"
FT /evidence="ECO:0000250"
FT COMPBIAS 184..200
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 279..293
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 380..440
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 538 AA; 55421 MW; 31D7A8E227B3D06C CRC64;
MPIGNLGHNP NVRALIPPAP PLPSQTDGAG GARNQLINSN GPMGSRLLFT PIRNSVADAA
DSRASDIPGL PTNPLRFAAS EVSLHGALEV LHDKGGLDTL NSAIGSSLFR VETRDDGSHV
AIGQKNGLET TVVLSEQEFS SLQSLDPEGK NKFVFTGGRG GAGHAMVTVA SDIAEARQRI
IDKLEPKDTK ETKEPGDPNS GEGKIIEIHT STSTSSLRAD PKLWLSLGTI AAGLIGMAAT
GIAQAVALTP EPDDPITTDP DAAANTAEAA AKDQLTKEAF QNPDNQKVNI DENGNAIPSG
ELKDDVVAQI AEQAKAAGEQ ARQEAIESNS QAQQKYDEQH AKREQEMSLS SGVGYGISGA
LILGGGIGAG VTAALHRKNQ PAEQTITTRT VVDNQPTNNA SAQGNTDTSG PEESPASRRN
SNASLASNGS DTSSTGTVEN PYADVGMPRN DSLARISEEP IYDEVAADPN YSVIQHFSGN
SPVTGRLVGT PGQGIQSTYA LLASSGGLRL GMGGLTGGGE SAVSTANAAP TPGPARFV
