(data stored in ACNUC9435 zone)

SWISSPROT: YADA_YERPS

ID   YADA_YERPS              Reviewed;         432 AA.
AC   P10858; Q663F4;
DT   01-JUL-1989, integrated into UniProtKB/Swiss-Prot.
DT   23-NOV-2004, sequence version 2.
DT   11-DEC-2019, entry version 115.
DE   RecName: Full=Adhesin YadA;
DE   Flags: Precursor;
GN   Name=yadA; Synonyms=invA, yop1, yopA; OrderedLocusNames=pYV0013;
OS   Yersinia pseudotuberculosis serotype I (strain IP32953).
OG   Plasmid pIB1, and Plasmid pYV.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Yersiniaceae; Yersinia.
OX   NCBI_TaxID=273123;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=YPIII / Serotype O:3; PLASMID=pIB1;
RX   PubMed=3043229; DOI=10.1038/334522a0;
RA   Rosqvist R., Skurnik M., Wolf-Watz H.;
RT   "Increased virulence of Yersinia pseudotuberculosis by two independent
RT   mutations.";
RL   Nature 334:522-525(1988).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=YPIII / Serotype O:3; PLASMID=pIB1;
RX   PubMed=2761389; DOI=10.1111/j.1365-2958.1989.tb00198.x;
RA   Skurnik M., Wolf-Watz H.;
RT   "Analysis of the yopA gene encoding the Yop1 virulence determinants of
RT   Yersinia spp.";
RL   Mol. Microbiol. 3:517-529(1989).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=IP32953; PLASMID=pYV;
RX   PubMed=15358858; DOI=10.1073/pnas.0404012101;
RA   Chain P.S.G., Carniel E., Larimer F.W., Lamerdin J., Stoutland P.O.,
RA   Regala W.M., Georgescu A.M., Vergez L.M., Land M.L., Motin V.L.,
RA   Brubaker R.R., Fowler J., Hinnebusch J., Marceau M., Medigue C.,
RA   Simonet M., Chenal-Francisque V., Souza B., Dacheux D., Elliott J.M.,
RA   Derbise A., Hauser L.J., Garcia E.;
RT   "Insights into the evolution of Yersinia pestis through whole-genome
RT   comparison with Yersinia pseudotuberculosis.";
RL   Proc. Natl. Acad. Sci. U.S.A. 101:13826-13831(2004).
RN   [4]
RP   COLLAGEN-BINDING.
RC   STRAIN=YPIII / Serotype O:3;
RX   PubMed=2592347; DOI=10.1128/jb.171.12.6674-6679.1989;
RA   Emoedy L., Heesemann J., Wolf-Watz H., Skurnik M., Kapperud G., O'Toole P.,
RA   Wadstroem T.;
RT   "Binding to collagen by Yersinia enterocolitica and Yersinia
RT   pseudotuberculosis: evidence for yopA-mediated and chromosomally encoded
RT   mechanisms.";
RL   J. Bacteriol. 171:6674-6679(1989).
RN   [5]
RP   INDUCTION.
RC   STRAIN=YPIII / Serotype O:3;
RX   PubMed=1548243; DOI=10.1128/jb.174.6.2047-2051.1992;
RA   Skurnik M., Toivanen P.;
RT   "LcrF is the temperature-regulated activator of the yadA gene of Yersinia
RT   enterocolitica and Yersinia pseudotuberculosis.";
RL   J. Bacteriol. 174:2047-2051(1992).
RN   [6]
RP   FUNCTION.
RC   STRAIN=YPIII / Serotype O:3;
RX   PubMed=12183532; DOI=10.1128/iai.70.9.4880-4891.2002;
RA   Eitel J., Dersch P.;
RT   "The YadA protein of Yersinia pseudotuberculosis mediates high-efficiency
RT   uptake into human cells under environmental conditions in which invasin is
RT   repressed.";
RL   Infect. Immun. 70:4880-4891(2002).
CC   -!- FUNCTION: Collagen-binding outer membrane protein forming a fibrillar
CC       matrix on the bacterial cell surface. Promotes attachment to eukaryotic
CC       cells and after invasion, is the major adhesin in infected tissue.
CC       Constitutes an alternative uptake pathway under conditions in which
CC       invasin synthesis is repressed. {ECO:0000269|PubMed:12183532}.
CC   -!- SUBUNIT: Homotrimer. {ECO:0000250|UniProtKB:P0C2W0}.
CC   -!- SUBCELLULAR LOCATION: Cell surface {ECO:0000250|UniProtKB:P0C2W0}. Cell
CC       outer membrane {ECO:0000250|UniProtKB:P0C2W0}. Note=The C-terminal
CC       translocator domain is localized in the outer membrane and the
CC       passenger domain is at the cell surface.
CC       {ECO:0000250|UniProtKB:P0C2W0}.
CC   -!- INDUCTION: Induced at 37 degrees Celsius by the temperature-dependent
CC       transcriptional activator LcrF (VirF). {ECO:0000269|PubMed:1548243}.
CC   -!- DOMAIN: The signal peptide, cleaved at the inner membrane, guides the
CC       autotransporter protein to the periplasmic space. Then, insertion of
CC       the C-terminal translocator domain in the outer membrane forms a
CC       hydrophilic pore for the translocation of the passenger domain to the
CC       bacterial cell surface. {ECO:0000250|UniProtKB:P0C2W0}.
CC   -!- SIMILARITY: Belongs to the autotransporter-2 (AT-2) (TC 1.B.40) family.
CC       {ECO:0000305}.
DR   EMBL; X13883; CAA32088.1; -; Genomic_DNA.
DR   EMBL; BX936399; CAF25356.1; -; Genomic_DNA.
DR   PIR; S04534; S04534.
DR   RefSeq; WP_011191362.1; NZ_CP009711.1.
DR   SMR; P10858; -.
DR   EnsemblBacteria; CAF25356; CAF25356; pYV0013.
DR   KEGG; ypo:BZ17_4223; -.
DR   KEGG; yps:pYV0013; -.
DR   PATRIC; fig|273123.14.peg.4456; -.
DR   HOGENOM; HOG000266859; -.
DR   KO; K12341; -.
DR   OMA; GIANNYT; -.
DR   Proteomes; UP000001011; Plasmid pYV.
DR   GO; GO:0009279; C:cell outer membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0009986; C:cell surface; IEA:UniProtKB-SubCell.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005518; F:collagen binding; IEA:InterPro.
DR   GO; GO:0007155; P:cell adhesion; IEA:UniProtKB-KW.
DR   GO; GO:0009405; P:pathogenesis; IEA:UniProtKB-KW.
DR   Gene3D; 2.150.10.10; -; 1.
DR   InterPro; IPR008640; Adhesin_Head_dom.
DR   InterPro; IPR008635; Coiled_stalk_dom.
DR   InterPro; IPR008126; OM_adhesion_Yersinia.
DR   InterPro; IPR011049; Serralysin-like_metalloprot_C.
DR   InterPro; IPR005594; YadA_C.
DR   Pfam; PF03895; YadA_anchor; 1.
DR   Pfam; PF05658; YadA_head; 2.
DR   Pfam; PF05662; YadA_stalk; 1.
DR   PRINTS; PR01756; OMADHESIN.
PE   1: Evidence at protein level;
DR   PRODOM; P10858.
DR   SWISS-2DPAGE; P10858.
KW   Cell adhesion; Cell outer membrane; Coiled coil; Membrane; Plasmid; Signal;
KW   Transmembrane; Transmembrane beta strand; Virulence.
FT   SIGNAL          1..25
FT                   /evidence="ECO:0000255"
FT   CHAIN           26..432
FT                   /note="Adhesin YadA"
FT                   /id="PRO_0000022701"
FT   REGION          26..340
FT                   /note="Surface exposed passenger domain"
FT                   /evidence="ECO:0000250|UniProtKB:P0C2W0"
FT   REGION          341..379
FT                   /note="Outer membrane translocation of the passenger
FT                   domain"
FT                   /evidence="ECO:0000250|UniProtKB:P0C2W0"
FT   REGION          380..432
FT                   /note="Translocator domain"
FT                   /evidence="ECO:0000250|UniProtKB:P0C2W0"
FT   COILED          242..263
FT                   /evidence="ECO:0000255"
FT   CONFLICT        94
FT                   /note="G -> GAG (in Ref. 1 and 2)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        97
FT                   /note="D -> N (in Ref. 1 and 2)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        102..104
FT                   /note="GIH -> DPY (in Ref. 1 and 2)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        124
FT                   /note="A -> S (in Ref. 1 and 2)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        209
FT                   /note="L -> H (in Ref. 1 and 2)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        237..239
FT                   /note="KDN -> EDT (in Ref. 1 and 2)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   432 AA;  44831 MW;  4698FF92AB0D035B CRC64;
     MTKDFKISVS AALISALFSS PYAFAEEPED GNDGIPRLSA VQISPNVDPK LGVGLYPAKP
     ILRQENPKLP PRGPQGPEKK RARLAEAIQP QVLGGLDARA KGIHSIAIGA TAEAAKPAAV
     AVGAGSIATG VNSVAIGPLS KALGDSAVTY GASSTAQKDG VAIGARASAS DTGVAVGFNS
     KVDAQNSVAI GHSSHVAADH GYSIAIGDLS KTDRENSVSI GHESLNRQLT HLAAGTKDND
     AVNVAQLKKE MAETLENARK ETLAQSNDVL DAAKKHSNSV ARTTLETAEE HANKKSAEAL
     VSAKVYADSN SSHTLKTANS YTDVTVSSST KKAISESNQY TDHKFSQLDN RLDKLDKRVD
     KGLASSAALN SLFQPYGVGK VNFTAGVGGY RSSQALAIGS GYRVNESVAL KAGVAYAGSS
     NVMYNASFNI EW
//

If you have problems or comments...

PBIL Back to PBIL home page