ESFU2_ECO57
ID ESFU2_ECO57 Reviewed; 337 AA.
AC P0DJ88; 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; OrderedLocusNames=ECs2715;
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 / Sakai / RIMD 0509952 / EHEC;
RX PubMed=11258796; DOI=10.1093/dnares/8.1.11;
RA Hayashi T., Makino K., Ohnishi M., Kurokawa K., Ishii K., Yokoyama K.,
RA Han C.-G., Ohtsubo E., Nakayama K., Murata T., Tanaka M., Tobe T., Iida T.,
RA Takami H., Honda T., Sasakawa C., Ogasawara N., Yasunaga T., Kuhara S.,
RA Shiba T., Hattori M., Shinagawa H.;
RT "Complete genome sequence of enterohemorrhagic Escherichia coli O157:H7 and
RT genomic comparison with a laboratory strain K-12.";
RL DNA Res. 8:11-22(2001).
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 -!- INTERACTION:
CC P0DJ88; Q9UHR4: BAIAP2L1; Xeno; NbExp=9; IntAct=EBI-10039462, EBI-2483278;
CC P0DJ88; P42768: WAS; Xeno; NbExp=3; IntAct=EBI-10039462, EBI-346375;
CC P0DJ88; O00401: WASL; Xeno; NbExp=2; IntAct=EBI-10039462, EBI-957615;
CC P0DJ88; O08816: Wasl; Xeno; NbExp=4; IntAct=EBI-10039462, EBI-6142604;
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; BA000007; BAB36138.1; -; Genomic_DNA.
DR PIR; C90968; C90968.
DR RefSeq; NP_310742.1; NC_002695.1.
DR RefSeq; WP_010917831.1; NZ_SWKA01000005.1.
DR AlphaFoldDB; P0DJ88; -.
DR SMR; P0DJ88; -.
DR IntAct; P0DJ88; 5.
DR STRING; 155864.EDL933_1308; -.
DR EnsemblBacteria; BAB36138; BAB36138; ECs_2715.
DR GeneID; 912330; -.
DR KEGG; ecs:ECs_2715; -.
DR PATRIC; fig|386585.9.peg.2847; -.
DR eggNOG; ENOG5031KP0; Bacteria.
DR HOGENOM; CLU_936086_0_0_6; -.
DR Proteomes; UP000000558; Chromosome.
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 1: Evidence at protein level;
KW Host cytoplasm; Reference proteome; Repeat; Secreted; Virulence.
FT CHAIN 1..337
FT /note="Secreted effector protein EspF(U)"
FT /id="PRO_0000413984"
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