ID   ESPFU_ECO5T             Reviewed;         337 AA.
AC   C6UYI3;
DT   16-NOV-2011, integrated into UniProtKB/Swiss-Prot.
DT   22-SEP-2009, sequence version 1.
DT   25-MAY-2022, entry version 47.
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=ECSP_2584;
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: 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 (By similarity).
CC       {ECO:0000250}.
CC   -!- SUBUNIT: Interacts with host BAIAP2 and host WASL/N-WASP. Can also
CC       interact with host proteins BAIAP2L1 and WAS/WASP (By similarity).
CC       {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000250}. Host cytoplasm
CC       {ECO:0000250}. Note=Secreted via the type III secretion system (TTSS).
CC       In host cells, localizes to the tip of the actin pedestal (By
CC       similarity). {ECO:0000250}.
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 (By
CC       similarity). {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the EspF(U)/TccP family. {ECO:0000305}.
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DR   EMBL; CP001368; ACT72391.1; -; Genomic_DNA.
DR   RefSeq; WP_010917831.1; NC_013008.1.
DR   AlphaFoldDB; C6UYI3; -.
DR   SMR; C6UYI3; -.
DR   KEGG; etw:ECSP_2584; -.
DR   HOGENOM; CLU_936086_0_0_6; -.
DR   OMA; SFHRQST; -.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0030430; C:host cell cytoplasm; ISS:UniProtKB.
DR   Gene3D; 6.10.250.3330; -; 6.
DR   InterPro; IPR006891; T3SS_EspF.
DR   InterPro; IPR044889; TccP2/EspF(U)-like_sf.
DR   Pfam; PF04806; EspF; 6.
PE   3: Inferred from homology;
KW   Host cytoplasm; Repeat; Secreted; Virulence.
FT   CHAIN           1..337
FT                   /note="Secreted effector protein EspF(U)"
FT                   /id="PRO_0000413986"
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   REGION          96..330
FT                   /note="5 X 48 AA approximate tandem repeats"
FT   REGION          291..312
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        296..310
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   337 AA;  37192 MW;  49A1BE2EA220E1C0 CRC64;
     MINNVSSLFP TVNRNITAVY KKSSFSVSPQ KITLNPVKIS SPFSPSSSSI SATTLFRAPN
     AHSASFHRQS TAESSLHQQL PNVRQRLIQH LAEHGIKPAR SMAEHIPPAP NWPAPPPPVQ
     NEQSRPLPDV AQRLVQHLAE HGIQPARNMA EHIPPAPNWP APPLPVQNEQ SRPLPDVAQR
     LVQHLAEHGI QPARSMAEHI PPAPNWPAPP PPVQNEQSRP LPDVAQRLMQ HLAEHGIQPA
     RNMAEHIPPA PNWPAPTPPV QNEQSRPLPD VAQRLMQHLA EHGIQPARNM AEHIPPAPNW
     PAPTPPVQNE QSRPLPDVAQ RLMQHLAEHG INTSKRS