TIR_ECOCB
ID TIR_ECOCB Reviewed; 556 AA.
AC D3QW22;
DT 14-DEC-2011, integrated into UniProtKB/Swiss-Prot.
DT 20-APR-2010, sequence version 1.
DT 25-MAY-2022, entry version 42.
DE RecName: Full=Translocated intimin receptor Tir;
DE AltName: Full=Secreted effector protein Tir;
GN Name=tir; Synonyms=espE; OrderedLocusNames=G2583_4416;
OS Escherichia coli O55:H7 (strain CB9615 / EPEC).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=701177;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CB9615 / EPEC;
RX PubMed=20090843; DOI=10.1371/journal.pone.0008700;
RA Zhou Z., Li X., Liu B., Beutin L., Xu J., Ren Y., Feng L., Lan R.,
RA Reeves P.R., Wang L.;
RT "Derivation of Escherichia coli O157:H7 from its O55:H7 precursor.";
RL PLoS ONE 5:E8700-E8700(2010).
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; CP001846; ADD58883.1; -; Genomic_DNA.
DR RefSeq; WP_001359418.1; NC_013941.1.
DR AlphaFoldDB; D3QW22; -.
DR SMR; D3QW22; -.
DR EnsemblBacteria; ADD58883; ADD58883; G2583_4416.
DR KEGG; eok:G2583_4416; -.
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..556
FT /note="Translocated intimin receptor Tir"
FT /id="PRO_0000414058"
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..556
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..449
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 531..556
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 454..456
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 535..550
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 556 AA; 57820 MW; 4A6446923D83A03C 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 TSARTVENKP ANNTPAQGNV
DTPGSEDTME SRRSSMASTS STFFDTSSIG TVQNPYADVK TSLHDSQVPT SNSNTSVQNM
GNTDSVVYST IQHPPRDTTD NGARLLGNPS AGIQSTYARL ALSGGLRHDM GGLTGGSNSA
VNTSNNPPAP GSHRFV
