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Translocated intimin receptor Tir (Secreted effector protein Tir)

 TIR_ECO27               Reviewed;         550 AA.
B7UM99; O50190; O52147;
14-DEC-2011, integrated into UniProtKB/Swiss-Prot.
10-FEB-2009, sequence version 1.
25-OCT-2017, entry version 58.
RecName: Full=Translocated intimin receptor Tir;
AltName: Full=Secreted effector protein Tir;
Name=tir; Synonyms=espE; OrderedLocusNames=E2348C_3941;
Escherichia coli O127:H6 (strain E2348/69 / EPEC).
Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
Enterobacteriaceae; Escherichia.
NCBI_TaxID=574521;
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 2-31, FUNCTION,
INTERACTION WITH INTIMIN, SUBCELLULAR LOCATION, SECRETION VIA TYPE III
SECRETION SYSTEM, PHOSPHORYLATION, AND GENE NAME.
STRAIN=E2348/69 / EPEC;
PubMed=9390560; DOI=10.1016/S0092-8674(00)80437-7;
Kenny B., DeVinney R., Stein M., Reinscheid D.J., Frey E.A.,
Finlay B.B.;
"Enteropathogenic E. coli (EPEC) transfers its receptor for intimate
adherence into mammalian cells.";
Cell 91:511-520(1997).
[2]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
STRAIN=E2348/69 / EPEC;
PubMed=9593291; DOI=10.1046/j.1365-2958.1998.00783.x;
Elliott S.J., Wainwright L.A., McDaniel T.K., Jarvis K.G., Deng Y.K.,
Lai L.C., McNamara B.P., Donnenberg M.S., Kaper J.B.;
"The complete sequence of the locus of enterocyte effacement (LEE)
from enteropathogenic Escherichia coli E2348/69.";
Mol. Microbiol. 28:1-4(1998).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=E2348/69 / EPEC;
PubMed=18952797; DOI=10.1128/JB.01238-08;
Iguchi A., Thomson N.R., Ogura Y., Saunders D., Ooka T.,
Henderson I.R., Harris D., Asadulghani M., Kurokawa K., Dean P.,
Kenny B., Quail M.A., Thurston S., Dougan G., Hayashi T., Parkhill J.,
Frankel G.;
"Complete genome sequence and comparative genome analysis of
enteropathogenic Escherichia coli O127:H6 strain E2348/69.";
J. Bacteriol. 191:347-354(2009).
[4]
SUBCELLULAR LOCATION.
STRAIN=E2348/69 / EPEC;
PubMed=9632251; DOI=10.1046/j.1365-2958.1998.00798.x;
Deibel C., Kramer S., Chakraborty T., Ebel F.;
"EspE, a novel secreted protein of attaching and effacing bacteria, is
directly translocated into infected host cells, where it appears as a
tyrosine-phosphorylated 90 kDa protein.";
Mol. Microbiol. 28:463-474(1998).
[5]
INTERACTION WITH INTIMIN.
STRAIN=E2348/69 / EPEC;
PubMed=10225900;
DeVinney R., Stein M., Reinscheid D., Abe A., Ruschkowski S.,
Finlay B.B.;
"Enterohemorrhagic Escherichia coli O157:H7 produces Tir, which is
translocated to the host cell membrane but is not tyrosine
phosphorylated.";
Infect. Immun. 67:2389-2398(1999).
[6]
FUNCTION, SUBCELLULAR LOCATION, TOPOLOGY, DOMAIN, INTERACTION WITH
INTIMIN, PHOSPHORYLATION, AND MUTAGENESIS OF TYR-474 AND TYR-483.
STRAIN=E2348/69 / EPEC;
PubMed=10096089; DOI=10.1046/j.1365-2958.1999.01265.x;
Kenny B.;
"Phosphorylation of tyrosine 474 of the enteropathogenic Escherichia
coli (EPEC) Tir receptor molecule is essential for actin nucleating
activity and is preceded by additional host modifications.";
Mol. Microbiol. 31:1229-1241(1999).
[7]
INTERACTION WITH HOST ALPHA-ACTININ, AND DOMAIN.
STRAIN=EPEC;
PubMed=10873808; DOI=10.1016/S0960-9822(00)00543-1;
Goosney D.L., DeVinney R., Pfuetzner R.A., Frey E.A., Strynadka N.C.,
Finlay B.B.;
"Enteropathogenic E. coli translocated intimin receptor, Tir,
interacts directly with alpha-actinin.";
Curr. Biol. 10:735-738(2000).
[8]
INTERACTION WITH HOST NCK.
STRAIN=E2348/69 / EPEC;
PubMed=11533668; DOI=10.1038/ncb0901-856;
Gruenheid S., DeVinney R., Bladt F., Goosney D., Gelkop S., Gish G.D.,
Pawson T., Finlay B.B.;
"Enteropathogenic E. coli Tir binds Nck to initiate actin pedestal
formation in host cells.";
Nat. Cell Biol. 3:856-859(2001).
[9]
INTERACTION WITH HOST NCK, PHOSPHORYLATION, AND MUTAGENESIS OF
TYR-474.
STRAIN=E2348/69 / EPEC;
PubMed=11918809; DOI=10.1046/j.1365-2958.2002.02817.x;
Campellone K.G., Giese A., Tipper D.J., Leong J.M.;
"A tyrosine-phosphorylated 12-amino-acid sequence of enteropathogenic
Escherichia coli Tir binds the host adaptor protein Nck and is
required for Nck localization to actin pedestals.";
Mol. Microbiol. 43:1227-1241(2002).
[10]
FUNCTION.
STRAIN=E2348/69 / EPEC;
PubMed=14764108; DOI=10.1111/j.1462-5822.2004.00364.x;
Lommel S., Benesch S., Rohde M., Wehland J., Rottner K.;
"Enterohaemorrhagic and enteropathogenic Escherichia coli use
different mechanisms for actin pedestal formation that converge on N-
WASP.";
Cell. Microbiol. 6:243-254(2004).
[11]
FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH INTIMIN AND HOST NCK,
PHOSPHORYLATION, AND DOMAIN.
STRAIN=E2348/69 / EPEC;
PubMed=14757753; DOI=10.1083/jcb.200306032;
Campellone K.G., Rankin S., Pawson T., Kirschner M.W., Tipper D.J.,
Leong J.M.;
"Clustering of Nck by a 12-residue Tir phosphopeptide is sufficient to
trigger localized actin assembly.";
J. Cell Biol. 164:407-416(2004).
[12]
FUNCTION, INTERACTION WITH HOST NCK, PHOSPHORYLATION AT TYR-454 AND
TYR-474, AND MUTAGENESIS OF TYR-454 AND TYR-474.
STRAIN=E2348/69 / EPEC;
PubMed=15813734; DOI=10.1111/j.1365-2958.2005.04558.x;
Campellone K.G., Leong J.M.;
"Nck-independent actin assembly is mediated by two phosphorylated
tyrosines within enteropathogenic Escherichia coli Tir.";
Mol. Microbiol. 56:416-432(2005).
[13]
SUBCELLULAR LOCATION.
STRAIN=EPEC;
PubMed=16436373; DOI=10.1074/jbc.M513532200;
Race P.R., Lakey J.H., Banfield M.J.;
"Insertion of the enteropathogenic Escherichia coli Tir virulence
protein into membranes in vitro.";
J. Biol. Chem. 281:7842-7849(2006).
[14]
FUNCTION, AND MUTAGENESIS OF ASN-452; PRO-453; TYR-454 AND TYR-474.
STRAIN=E2348/69 / EPEC;
PubMed=17521329; DOI=10.1111/j.1462-5822.2007.00954.x;
Brady M.J., Campellone K.G., Ghildiyal M., Leong J.M.;
"Enterohaemorrhagic and enteropathogenic Escherichia coli Tir proteins
trigger a common Nck-independent actin assembly pathway.";
Cell. Microbiol. 9:2242-2253(2007).
[15]
INTERACTION WITH HOST BAIAP2.
STRAIN=E2348/69 / EPEC;
PubMed=19286134; DOI=10.1016/j.chom.2009.02.003;
Weiss S.M., Ladwein M., Schmidt D., Ehinger J., Lommel S., Stading K.,
Beutling U., Disanza A., Frank R., Jansch L., Scita G., Gunzer F.,
Rottner K., Stradal T.E.;
"IRSp53 links the enterohemorrhagic E. coli effectors Tir and EspFU
for actin pedestal formation.";
Cell Host Microbe 5:244-258(2009).
[16]
REVIEW.
PubMed=20477869; DOI=10.1111/j.1742-4658.2010.07653.x;
Campellone K.G.;
"Cytoskeleton-modulating effectors of enteropathogenic and
enterohaemorrhagic Escherichia coli: Tir, EspFU and actin pedestal
assembly.";
FEBS J. 277:2390-2402(2010).
[17]
X-RAY CRYSTALLOGRAPHY (1.45 ANGSTROMS) OF 472-481 IN COMPLEX WITH NCK1
AND NCK2, AND PHOSPHORYLATION AT TYR-474.
PubMed=16636066; DOI=10.1074/jbc.M512917200;
Frese S., Schubert W.D., Findeis A.C., Marquardt T., Roske Y.S.,
Stradal T.E., Heinz D.W.;
"The phosphotyrosine peptide binding specificity of Nck1 and Nck2 Src
homology 2 domains.";
J. Biol. Chem. 281:18236-18245(2006).
-!- FUNCTION: Multifunctional protein that is required for efficient
pedestal formation in host epithelial cells during infection. The
extracellular region acts as a receptor for bacterial intimin,
allowing the bacterium to attach tightly to the host-cell surface.
Simultaneously, the intracellular region initiates a signaling
cascade in the host cell, which leads to actin polymerization and
formation of actin pedestals at the sites of bacterial adhesion.
In strain E2348/69, acts mainly via the host adaptor proteins NCK1
and NCK2. Once clustered and phosphorylated at Tyr-474, Tir binds
to NCK proteins, which in turn bind and activate host WASL/N-WASP,
leading to actin polymerization. Can also trigger an inefficient,
NCK-independent pedestal formation. This pathway involves
phosphorylation of Tyr-454 and probably a putative host adaptor.
Acts also via direct binding to the host cytoskeletal protein
alpha-actinin in a NCK- and phosphotyrosine-independent manner.
This interaction may stabilize the pedestal, but is not essential
for its formation. {ECO:0000269|PubMed:10096089,
ECO:0000269|PubMed:14757753, ECO:0000269|PubMed:14764108,
ECO:0000269|PubMed:15813734, ECO:0000269|PubMed:17521329,
ECO:0000269|PubMed:9390560}.
-!- SUBUNIT: Interacts with intimin. Interacts with host proteins
NCK1, NCK2, alpha-actinin and BAIAP2.
{ECO:0000269|PubMed:10096089, ECO:0000269|PubMed:10225900,
ECO:0000269|PubMed:10873808, ECO:0000269|PubMed:11533668,
ECO:0000269|PubMed:11918809, ECO:0000269|PubMed:14757753,
ECO:0000269|PubMed:15813734, ECO:0000269|PubMed:16636066,
ECO:0000269|PubMed:19286134, ECO:0000269|PubMed:9390560}.
-!- INTERACTION:
Q9UQB8-4:BAIAP2 (xeno); NbExp=3; IntAct=EBI-2504426, EBI-6174091;
P21244:cesT; NbExp=6; IntAct=EBI-2504426, EBI-2504434;
Q14247:CTTN (xeno); NbExp=3; IntAct=EBI-2504426, EBI-351886;
P29350:PTPN6 (xeno); NbExp=4; IntAct=EBI-2504426, EBI-78260;
P29351:Ptpn6 (xeno); NbExp=2; IntAct=EBI-2504426, EBI-2620699;
-!- SUBCELLULAR LOCATION: Secreted. Host cell membrane; Multi-pass
membrane protein. Note=Secreted via the type III secretion system
(TTSS). Released into the host cytoplasm via TTSS and then
independently inserts into the plasma membrane from a cytoplasmic
location. In host cells, localizes to the tip of the actin
pedestal.
-!- DOMAIN: The intracellular N-terminal region interacts with host
alpha-actinin and is not required for pedestal formation. The
central extracellular region (amino acids 277-332) is involved in
bacterial intimin binding. The intracellular C-terminal region
binds to host NCK. {ECO:0000269|PubMed:10096089,
ECO:0000269|PubMed:10873808, ECO:0000269|PubMed:14757753}.
-!- PTM: Phosphorylated on Tyr-474 by host kinases. Tyr-454 can also
be phosphorylated, although at lower efficiency. Phosphorylation
is stimulated by clustering of Tir by intimin.
{ECO:0000269|PubMed:10096089, ECO:0000269|PubMed:11918809,
ECO:0000269|PubMed:14757753, ECO:0000269|PubMed:15813734,
ECO:0000269|PubMed:16636066, ECO:0000269|PubMed:9390560}.
-!- SIMILARITY: Belongs to the Tir receptor family. {ECO:0000305}.
-----------------------------------------------------------------------
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Distributed under the Creative Commons Attribution-NoDerivs License
-----------------------------------------------------------------------
EMBL; AF013122; AAB88410.1; -; Genomic_DNA.
EMBL; AF022236; AAC38390.1; -; Genomic_DNA.
EMBL; FM180568; CAS11489.1; -; Genomic_DNA.
RefSeq; WP_001339882.1; NC_011601.1.
PDB; 2CI9; X-ray; 1.50 A; L/M=470-481.
PDB; 2CIA; X-ray; 1.45 A; L=472-481.
PDBsum; 2CI9; -.
PDBsum; 2CIA; -.
ProteinModelPortal; B7UM99; -.
SMR; B7UM99; -.
DIP; DIP-27648N; -.
DIP; DIP-55921N; -.
IntAct; B7UM99; 9.
MINT; MINT-7225953; -.
iPTMnet; B7UM99; -.
EnsemblBacteria; CAS11489; CAS11489; E2348C_3941.
KEGG; ecg:E2348C_3941; -.
HOGENOM; HOG000059321; -.
KO; K12784; -.
OMA; QGIQSTY; -.
EvolutionaryTrace; B7UM99; -.
Proteomes; UP000008205; Chromosome.
GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
GO; GO:0020002; C:host cell plasma membrane; IEA:UniProtKB-SubCell.
GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
GO; GO:0009405; P:pathogenesis; IEA:UniProtKB-KW.
Gene3D; 4.10.820.10; -; 1.
InterPro; IPR037003; Tir_central_sf.
InterPro; IPR022638; Transloc_intimin_rcpt.
InterPro; IPR022639; Transloc_intimin_rcpt_C.
InterPro; IPR003536; Transloc_intimin_rcpt_cen_dom.
InterPro; IPR022633; Transloc_intimin_rcpt_N.
Pfam; PF07489; Tir_receptor_C; 1.
Pfam; PF03549; Tir_receptor_M; 1.
Pfam; PF07490; Tir_receptor_N; 1.
PRINTS; PR01370; TRNSINTIMINR.
1: Evidence at protein level;
3D-structure; Complete proteome; Direct protein sequencing;
Host cell membrane; Host membrane; Membrane; Phosphoprotein; Receptor;
Secreted; Transmembrane; Transmembrane helix; Virulence.
CHAIN 1 550 Translocated intimin receptor Tir.
/FTId=PRO_0000414050.
TOPO_DOM 1 233 Cytoplasmic. {ECO:0000255}.
TRANSMEM 234 254 Helical. {ECO:0000255}.
TOPO_DOM 255 362 Extracellular. {ECO:0000255}.
TRANSMEM 363 383 Helical. {ECO:0000255}.
TOPO_DOM 384 550 Cytoplasmic. {ECO:0000255}.
MOTIF 452 454 Essential for NCK-independent actin
pedestal formation.
MOD_RES 454 454 Phosphotyrosine.
{ECO:0000269|PubMed:15813734}.
MOD_RES 474 474 Phosphotyrosine.
{ECO:0000269|PubMed:15813734,
ECO:0000269|PubMed:16636066}.
MUTAGEN 452 452 N->A: Lack of pedestal formation; when
associated with F-474.
{ECO:0000269|PubMed:17521329}.
MUTAGEN 453 453 P->A: Lack of pedestal formation; when
associated with F-474.
{ECO:0000269|PubMed:17521329}.
MUTAGEN 454 454 Y->A: Lack of pedestal formation; when
associated with F-474.
{ECO:0000269|PubMed:15813734,
ECO:0000269|PubMed:17521329}.
MUTAGEN 454 454 Y->F: Does not inhibit translocation into
the host cell. Almost no change in actin
polymerization. Lack of pedestal
formation; when associated with F-474.
{ECO:0000269|PubMed:15813734,
ECO:0000269|PubMed:17521329}.
MUTAGEN 474 474 Y->D,E: Loss of phosphorylation and
strong decrease in actin polymerization.
{ECO:0000269|PubMed:10096089,
ECO:0000269|PubMed:11918809,
ECO:0000269|PubMed:15813734,
ECO:0000269|PubMed:17521329}.
MUTAGEN 474 474 Y->F: Loss of phosphorylation and strong
decrease in actin polymerization. Lack of
pedestal formation; when associated with
F-454. {ECO:0000269|PubMed:10096089,
ECO:0000269|PubMed:11918809,
ECO:0000269|PubMed:15813734,
ECO:0000269|PubMed:17521329}.
MUTAGEN 474 474 Y->S: Does not inhibit translocation into
the host cell. Loss of phosphorylation
and strong decrease in actin
polymerization.
{ECO:0000269|PubMed:10096089,
ECO:0000269|PubMed:11918809,
ECO:0000269|PubMed:15813734,
ECO:0000269|PubMed:17521329}.
MUTAGEN 483 483 Y->S: Does not inhibit translocation into
the host cell.
{ECO:0000269|PubMed:10096089}.
CONFLICT 412 430 NTPAQGGTDATRAEDASLN -> IPQHKVALMPQERRRFSD
(in Ref. 1; AAB88410). {ECO:0000305}.
CONFLICT 533 533 S -> T (in Ref. 1; AAB88410).
{ECO:0000305}.
SEQUENCE 550 AA; 56510 MW; 19DD08A9BE9251CB CRC64;
MPIGNLGNNV NGNHLIPPAP PLPSQTDGAA RGGTGHLISS TGALGSRSLF SPLRNSMADS
VDSRDIPGLP TNPSRLAAAT SETCLLGGFE VLHDKGPLDI LNTQIGPSAF RVEVQADGTH
AAIGEKNGLE VSVTLSPQEW SSLQSIDTEG KNRFVFTGGR GGSGHPMVTV ASDIAEARTK
ILAKLDPDNH GGRQPKDVDT RSVGVGSASG IDDGVVSETH TSTTNSSVRS DPKFWVSVGA
IAAGLAGLAA TGIAQALALT PEPDDPTTTD PDQAANAAES ATKDQLTQEA FKNPENQKVN
IDANGNAIPS GELKDDIVEQ IAQQAKEAGE VARQQAVESN AQAQQRYEDQ HARRQEELQL
SSGIGYGLSS ALIVAGGIGA GVTTALHRRN QPAEQTTTTT THTVVQQQTG GNTPAQGGTD
ATRAEDASLN RRDSQGSVAS THWSDSSSEV VNPYAEVGGA RNSLSAHQPE EHIYDEVAAD
PGYSVIQNFS GSGPVTGRLI GTPGQGIQST YALLANSGGL RLGMGGLTSG GESAVSSVNA
APTPGPVRFV


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