ESPFU_ECO57
ID ESPFU_ECO57 Reviewed; 384 AA.
AC Q8X482;
DT 16-NOV-2011, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2002, sequence version 1.
DT 23-FEB-2022, entry version 72.
DE RecName: Full=Secreted effector protein EspF(U);
DE AltName: Full=EspF-like protein encoded on prophage U;
DE AltName: Full=Tir-cytoskeleton coupling protein TccP;
GN Name=espF(U); Synonyms=tccP; OrderedLocusNames=Z3072;
OS Escherichia coli O157:H7.
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=83334;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=O157:H7 / EDL933 / ATCC 700927 / EHEC;
RX PubMed=11206551; DOI=10.1038/35054089;
RA Perna N.T., Plunkett G. III, Burland V., Mau B., Glasner J.D., Rose D.J.,
RA Mayhew G.F., Evans P.S., Gregor J., Kirkpatrick H.A., Posfai G.,
RA Hackett J., Klink S., Boutin A., Shao Y., Miller L., Grotbeck E.J.,
RA Davis N.W., Lim A., Dimalanta E.T., Potamousis K., Apodaca J.,
RA Anantharaman T.S., Lin J., Yen G., Schwartz D.C., Welch R.A.,
RA Blattner F.R.;
RT "Genome sequence of enterohaemorrhagic Escherichia coli O157:H7.";
RL Nature 409:529-533(2001).
RN [2]
RP FUNCTION, INTERACTION WITH WASL/N-WASP, SUBCELLULAR LOCATION, SECRETION VIA
RP TYPE III SECRETION SYSTEM, DISRUPTION PHENOTYPE, AND GENE NAME.
RC STRAIN=O157:H7 / EDL933 / ATCC 700927 / EHEC;
RX PubMed=15527496; DOI=10.1111/j.1462-5822.2004.00459.x;
RA Garmendia J., Phillips A.D., Carlier M.F., Chong Y., Schuller S.,
RA Marches O., Dahan S., Oswald E., Shaw R.K., Knutton S., Frankel G.;
RT "TccP is an enterohaemorrhagic Escherichia coli O157:H7 type III effector
RT protein that couples Tir to the actin-cytoskeleton.";
RL Cell. Microbiol. 6:1167-1183(2004).
RN [3]
RP FUNCTION, INTERACTION WITH WASL/N-WASP, SUBCELLULAR LOCATION, SECRETION VIA
RP TYPE III SECRETION SYSTEM, DOMAIN, DISRUPTION PHENOTYPE, AND GENE NAME.
RC STRAIN=O157:H7 / EDL933 / ATCC 700927 / EHEC;
RX PubMed=15296718; DOI=10.1016/j.devcel.2004.07.004;
RA Campellone K.G., Robbins D., Leong J.M.;
RT "EspFU is a translocated EHEC effector that interacts with Tir and N-WASP
RT and promotes Nck-independent actin assembly.";
RL Dev. Cell 7:217-228(2004).
RN [4]
RP INTERACTION WITH WASL/N-WASP, SECRETION VIA TYPE III SECRETION SYSTEM, AND
RP DOMAIN.
RC STRAIN=O157:H7 / EDL933 / ATCC 700927 / EHEC;
RX PubMed=16922863; DOI=10.1111/j.1462-5822.2006.00723.x;
RA Garmendia J., Carlier M.F., Egile C., Didry D., Frankel G.;
RT "Characterization of TccP-mediated N-WASP activation during
RT enterohaemorrhagic Escherichia coli infection.";
RL Cell. Microbiol. 8:1444-1455(2006).
RN [5]
RP FUNCTION, AND DOMAIN.
RC STRAIN=O157:H7 / EHEC;
RX PubMed=18650806; DOI=10.1038/nature07170;
RA Sallee N.A., Rivera G.M., Dueber J.E., Vasilescu D., Mullins R.D.,
RA Mayer B.J., Lim W.A.;
RT "The pathogen protein EspF(U) hijacks actin polymerization using mimicry
RT and multivalency.";
RL Nature 454:1005-1008(2008).
RN [6]
RP INTERACTION WITH BAIAP2 AND BAIAP2L1, AND DOMAIN.
RC STRAIN=O157:H7 / 86-24 / EHEC, and O157:H7 / EDL933 / ATCC 700927 / EHEC;
RX PubMed=19286134; DOI=10.1016/j.chom.2009.02.003;
RA Weiss S.M., Ladwein M., Schmidt D., Ehinger J., Lommel S., Stading K.,
RA Beutling U., Disanza A., Frank R., Jansch L., Scita G., Gunzer F.,
RA Rottner K., Stradal T.E.;
RT "IRSp53 links the enterohemorrhagic E. coli effectors Tir and EspFU for
RT actin pedestal formation.";
RL Cell Host Microbe 5:244-258(2009).
CC -!- FUNCTION: Required for efficient pedestal formation in host epithelial
CC cells during infection. Acts as an intermediate between Tir (via host
CC BAIAP2) and host WASL/N-WASP. Directly binds and activates WASL/N-WASP,
CC which stimulates actin polymerization and leads to the formation of
CC actin pedestals at the sites of bacterial adhesion.
CC {ECO:0000269|PubMed:15296718, ECO:0000269|PubMed:15527496,
CC ECO:0000269|PubMed:18650806}.
CC -!- SUBUNIT: Interacts with host BAIAP2 and host WASL/N-WASP. Can also
CC interact with host proteins BAIAP2L1 and WAS/WASP.
CC {ECO:0000269|PubMed:15296718, ECO:0000269|PubMed:15527496,
CC ECO:0000269|PubMed:16922863, ECO:0000269|PubMed:19286134}.
CC -!- INTERACTION:
CC Q8X482; Q60598: Cttn; Xeno; NbExp=6; IntAct=EBI-22229752, EBI-397955;
CC Q8X482; Q5T0N5-3: FNBP1L; Xeno; NbExp=3; IntAct=EBI-22229752, EBI-4403262;
CC Q8X482; O00401: WASL; Xeno; NbExp=5; IntAct=EBI-22229752, EBI-957615;
CC Q8X482; O08816: Wasl; Xeno; NbExp=5; IntAct=EBI-22229752, EBI-6142604;
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:15296718,
CC ECO:0000269|PubMed:15527496}. Host cytoplasm
CC {ECO:0000269|PubMed:15527496}. Note=Secreted via the type III secretion
CC system (TTSS) (PubMed:15527496, PubMed:15296718). In host cells,
CC localizes to the tip of the actin pedestal (PubMed:15527496,
CC PubMed:15296718). {ECO:0000269|PubMed:15296718,
CC ECO:0000269|PubMed:15527496}.
CC -!- DOMAIN: The N-terminal 21 amino acids are necessary and sufficient for
CC translocation into the host cell. The C-terminal region, composed of
CC several highly conserved proline-rich repeats, interacts with the SH3
CC domain of BAIAP2 and BAIAP2L1, and the GTPase binding domain (GBD) of
CC WASL/N-WASP and WAS/WASP. The N-terminal translocation signal and two
CC proline-rich repeats are sufficient for triggering actin
CC polymerization, but each additional repeat gives higher activity.
CC {ECO:0000269|PubMed:15296718, ECO:0000269|PubMed:16922863,
CC ECO:0000269|PubMed:18650806, ECO:0000269|PubMed:19286134}.
CC -!- DISRUPTION PHENOTYPE: Mutants show dramatic reduction in the efficiency
CC of pedestal formation and in the intensity of the residual pedestals
CC that are formed. {ECO:0000269|PubMed:15296718,
CC ECO:0000269|PubMed:15527496}.
CC -!- SIMILARITY: Belongs to the EspF(U)/TccP family. {ECO:0000305}.
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DR EMBL; AE005174; AAG56991.1; -; Genomic_DNA.
DR PIR; C85816; C85816.
DR IntAct; Q8X482; 10.
DR MINT; Q8X482; -.
DR EnsemblBacteria; AAG56991; AAG56991; Z3072.
DR KEGG; ece:Z3072; -.
DR Proteomes; UP000002519; Chromosome.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0030430; C:host cell cytoplasm; IDA:UniProtKB.
DR Gene3D; 6.10.250.3330; -; 7.
DR InterPro; IPR006891; T3SS_EspF.
DR InterPro; IPR044889; TccP2/EspF(U)-like_sf.
DR Pfam; PF04806; EspF; 7.
PE 1: Evidence at protein level;
KW Host cytoplasm; Repeat; Secreted; Virulence.
FT CHAIN 1..384
FT /note="Secreted effector protein EspF(U)"
FT /id="PRO_0000413983"
FT REPEAT 96..142
FT /note="1"
FT REPEAT 143..189
FT /note="2"
FT REPEAT 190..236
FT /note="3"
FT REPEAT 237..283
FT /note="4"
FT REPEAT 284..330
FT /note="5"
FT REPEAT 331..377
FT /note="6"
FT REGION 96..377
FT /note="6 X 48 AA approximate tandem repeats"
FT REGION 103..125
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 150..171
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 199..218
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 243..266
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 291..311
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 338..364
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 108..123
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 155..169
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 249..264
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 384 AA; 42474 MW; F8794D8467780135 CRC64;
MINNVSSLFP TVNRNITAVY KKSSFSVSPQ KITLNPVKIS SPFSPSSSSI SATTLFRAPN
AHSASFHRQS TAESSLHQQL PNVRQRLIQH LAEHGIXPAR SMAEHIPPAP KWPAPPPPVQ
NEQSRPLPDV AQRLMQHLAE HGIQPARNMA EHIPPAPNWP APTPPVQNEQ SRPLPDVAQR
LMQHLAEHGI QPARNMAEHI PPAPXWXAPT PPVQNEQSRP LPDVAQRLMQ HLAEHGIZPA
RSMAEHIPPA PNWPAPPPPV QNEQSRPLPD VAQRLXQHLA EHGIQPARNM AEHIPPAPNW
PAPXXPVXNE QSRPLXDVAX RLMQHLAEHG IQPARNMAEH IPPAPNWXAP TPPVQNEQSR
PLPDVAQRLM QHLAEHGINT SKRS
