TIR2_ECOLX
ID TIR2_ECOLX Reviewed; 538 AA.
AC P0DJ91; 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=84/110/1 / EPEC, and O26:K60:H- / E65/56 / EPEC;
RA Krejany E.O.;
RL Submitted (MAR-1999) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION IN VIRULENCE, AND DISRUPTION
RP PHENOTYPE.
RC STRAIN=O103:K-:H2 / E22 / EPEC;
RX PubMed=10722617; DOI=10.1128/iai.68.4.2171-2182.2000;
RA Marches O., Nougayrede J.-P., Boullier S., Mainil J., Charlier G.,
RA Raymond I., Pohl P., Boury M., De Rycke J., Milon A., Oswald E.;
RT "Role of tir and intimin in the virulence of rabbit enteropathogenic
RT Escherichia coli serotype O103:H2.";
RL Infect. Immun. 68:2171-2182(2000).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=O128:H2 / 9812 / APEC, and O26:K60 / B6 / APEC;
RX PubMed=19506015; DOI=10.1128/iai.00090-09;
RA Muller D., Benz I., Liebchen A., Gallitz I., Karch H., Schmidt M.A.;
RT "Comparative analysis of the locus of enterocyte effacement and its
RT flanking regions.";
RL Infect. Immun. 77:3501-3513(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, ECO:0000269|PubMed:10722617}.
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 -!- DISRUPTION PHENOTYPE: In a rabbit ligated ileal loop model, mutants do
CC not induce formation of A/E lesions. {ECO:0000269|PubMed:10722617}.
CC -!- SIMILARITY: Belongs to the Tir receptor family. {ECO:0000305}.
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DR EMBL; U59502; AAC32028.2; -; Genomic_DNA.
DR EMBL; AF132728; AAD27868.1; -; Genomic_DNA.
DR EMBL; AF113597; AAF03080.1; -; Genomic_DNA.
DR EMBL; FM201463; CAR47988.1; -; Genomic_DNA.
DR EMBL; FM201464; CAR48058.1; -; Genomic_DNA.
DR RefSeq; WP_001121330.1; NZ_WJGB01000091.1.
DR AlphaFoldDB; P0DJ91; -.
DR SMR; P0DJ91; -.
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 Host cell membrane; Host membrane; Membrane; Phosphoprotein; Receptor;
KW Secreted; Transmembrane; Transmembrane helix; Virulence.
FT CHAIN 1..538
FT /note="Translocated intimin receptor Tir"
FT /id="PRO_0000414053"
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
