ESFU3_ECO57
ID ESFU3_ECO57 Reviewed; 337 AA.
AC P0DJ89; Q8X2D5;
DT 16-NOV-2011, integrated into UniProtKB/Swiss-Prot.
DT 16-NOV-2011, sequence version 1.
DT 03-AUG-2022, entry version 49.
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;
OS Escherichia coli O157:H7.
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=83334;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=O157:H7 / 980551, O157:H7 / 980706, O157:H7 / 980938,
RC O157:H7 / 981456, O157:H7 / 981795, O157:H7 / 990281, and O157:H7 / 990570;
RX PubMed=17101643; DOI=10.1128/iai.01491-06;
RA Ogura Y., Ooka T., Whale A., Garmendia J., Beutin L., Tennant S.,
RA Krause G., Morabito S., Chinen I., Tobe T., Abe H., Tozzoli R.,
RA Caprioli A., Rivas M., Robins-Browne R., Hayashi T., Frankel G.;
RT "TccP2 of O157:H7 and non-O157 enterohemorrhagic Escherichia coli (EHEC):
RT challenging the dogma of EHEC-induced actin polymerization.";
RL Infect. Immun. 75:604-612(2007).
RN [2]
RP STRUCTURE BY NMR OF 268-300, FUNCTION, INTERACTION WITH HUMAN WAS/WASP, AND
RP DOMAIN.
RX PubMed=18650809; DOI=10.1038/nature07160;
RA Cheng H.C., Skehan B.M., Campellone K.G., Leong J.M., Rosen M.K.;
RT "Structural mechanism of WASP activation by the enterohaemorrhagic E. coli
RT effector EspF(U).";
RL Nature 454:1009-1013(2008).
RN [3]
RP STRUCTURE BY NMR OF 268-314, AND INTERACTION WITH HUMAN BAIAP2L1.
RX PubMed=21098279; DOI=10.1073/pnas.1010243107;
RA Aitio O., Hellman M., Kazlauskas A., Vingadassalom D.F., Leong J.M.,
RA Saksela K., Permi P.;
RT "Recognition of tandem PxxP motifs as a unique Src homology 3-binding mode
RT triggers pathogen-driven actin assembly.";
RL Proc. Natl. Acad. Sci. U.S.A. 107:21743-21748(2010).
RN [4]
RP STRUCTURE BY NMR OF 221-267 IN COMPLEX WITH HOST BAIAP2L1 AND WASL,
RP FUNCTION, INTERACTION WITH HOST BAIAP2L1 AND WASL, AND IDENTIFICATION IN A
RP COMPLEX WITH HOST BAIAP2L1 AND WASL.
RX PubMed=22921828; DOI=10.1016/j.str.2012.07.015;
RA Aitio O., Hellman M., Skehan B., Kesti T., Leong J.M., Saksela K.,
RA Permi P.;
RT "Enterohaemorrhagic Escherichia coli exploits a tryptophan switch to hijack
RT host f-actin assembly.";
RL Structure 20:1692-1703(2012).
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:18650809, ECO:0000269|PubMed:22921828}.
CC -!- SUBUNIT: Interacts with host BAIAP2 and host WASL/N-WASP (By
CC similarity). Can also interact with host proteins BAIAP2L1 and
CC WAS/WASP. Identified in a complex with host proteins BAIAP2L1 and WASL.
CC {ECO:0000250, ECO:0000269|PubMed:18650809, ECO:0000269|PubMed:21098279,
CC ECO:0000269|PubMed:22921828}.
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 (By similarity). The C-terminal
CC region, composed of several highly conserved proline-rich repeats,
CC interacts with the SH3 domain of BAIAP2 and BAIAP2L1, and the GTPase
CC binding domain (GBD) of WASL/N-WASP and WAS/WASP. The N-terminal
CC translocation signal and two proline-rich repeats are sufficient for
CC triggering actin polymerization, but each additional repeat gives
CC higher activity. {ECO:0000250, ECO:0000269|PubMed:18650809}.
CC -!- SIMILARITY: Belongs to the EspF(U)/TccP family. {ECO:0000305}.
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DR EMBL; AB253537; BAF45424.1; -; Genomic_DNA.
DR EMBL; AB253538; BAF45425.1; -; Genomic_DNA.
DR EMBL; AB253539; BAF45426.1; -; Genomic_DNA.
DR EMBL; AB253540; BAF45427.1; -; Genomic_DNA.
DR EMBL; AB253541; BAF45428.1; -; Genomic_DNA.
DR EMBL; AB253542; BAF45429.1; -; Genomic_DNA.
DR EMBL; AB253544; BAF45431.1; -; Genomic_DNA.
DR RefSeq; WP_010917831.1; NZ_SWKA01000005.1.
DR PDB; 2K42; NMR; -; B=268-300.
DR PDB; 2KXC; NMR; -; B=268-314.
DR PDB; 2LNH; NMR; -; C=268-314.
DR PDBsum; 2K42; -.
DR PDBsum; 2KXC; -.
DR PDBsum; 2LNH; -.
DR AlphaFoldDB; P0DJ89; -.
DR SMR; P0DJ89; -.
DR DIP; DIP-59949N; -.
DR EvolutionaryTrace; P0DJ89; -.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0030430; C:host cell cytoplasm; ISS:UniProtKB.
DR DisProt; DP00963; -.
DR Gene3D; 6.10.250.3330; -; 6.
DR IDEAL; IID90008; -.
DR InterPro; IPR006891; T3SS_EspF.
DR InterPro; IPR044889; TccP2/EspF(U)-like_sf.
DR Pfam; PF04806; EspF; 6.
PE 1: Evidence at protein level;
KW 3D-structure; Host cytoplasm; Repeat; Secreted; Virulence.
FT CHAIN 1..337
FT /note="Secreted effector protein EspF(U)"
FT /id="PRO_0000413985"
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"
FT HELIX 269..279
FT /evidence="ECO:0007829|PDB:2LNH"
FT TURN 280..283
FT /evidence="ECO:0007829|PDB:2LNH"
FT HELIX 287..289
FT /evidence="ECO:0007829|PDB:2LNH"
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
