TIR_ECO5T
ID TIR_ECO5T Reviewed; 558 AA.
AC C6UYL8;
DT 14-DEC-2011, integrated into UniProtKB/Swiss-Prot.
DT 22-SEP-2009, sequence version 1.
DT 25-MAY-2022, entry version 57.
DE RecName: Full=Translocated intimin receptor Tir;
DE AltName: Full=Secreted effector protein Tir;
GN Name=tir; Synonyms=espE; OrderedLocusNames=ECSP_4676;
OS Escherichia coli O157:H7 (strain TW14359 / EHEC).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=544404;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=TW14359 / EHEC;
RX PubMed=19564389; DOI=10.1128/iai.00198-09;
RA Kulasekara B.R., Jacobs M., Zhou Y., Wu Z., Sims E., Saenphimmachak C.,
RA Rohmer L., Ritchie J.M., Radey M., McKevitt M., Freeman T.L., Hayden H.,
RA Haugen E., Gillett W., Fong C., Chang J., Beskhlebnaya V., Waldor M.K.,
RA Samadpour M., Whittam T.S., Kaul R., Brittnacher M., Miller S.I.;
RT "Analysis of the genome of the Escherichia coli O157:H7 2006 spinach-
RT associated outbreak isolate indicates candidate genes that may enhance
RT virulence.";
RL Infect. Immun. 77:3713-3721(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; CP001368; ACT74397.1; -; Genomic_DNA.
DR RefSeq; WP_001301454.1; NC_013008.1.
DR PDB; 2YKT; X-ray; 2.11 A; B=452-463.
DR PDBsum; 2YKT; -.
DR AlphaFoldDB; C6UYL8; -.
DR SMR; C6UYL8; -.
DR KEGG; etw:ECSP_4676; -.
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 1: Evidence at protein level;
KW 3D-structure; Host cell membrane; Host membrane; Membrane; Phosphoprotein;
KW Receptor; Secreted; Transmembrane; Transmembrane helix; Virulence.
FT CHAIN 1..558
FT /note="Translocated intimin receptor Tir"
FT /id="PRO_0000414057"
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..558
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..451
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 533..558
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 456..458
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 537..552
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT TURN 457..460
FT /evidence="ECO:0007829|PDB:2YKT"
SQ SEQUENCE 558 AA; 58022 MW; 99C417222D4B4AA1 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 TTTSARTVEN KPANNTPAQG
NVDTPGSEDT MESRRSSMAS TSSTFFDTSS IGTVQNPYAD VKTSLHDSQV PTSNSNTSVQ
NMGNTDSVVY STIQHPPRDT TDNGARLLGN PSAGIQSTYA RLALSGGLRH DMGGLTGGSN
SAVNTSNNPP APGSHRFV
