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 25-MAY-2022, entry version 124.
DE RecName: Full=Adhesin YadA;
DE AltName: Full=Type 5 secretion system autotransporter YadA {ECO:0000305};
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}.
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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 AlphaFoldDB; P10858; -.
DR SMR; P10858; -.
DR EnsemblBacteria; CAF25356; CAF25356; pYV0013.
DR GeneID; 66841073; -.
DR KEGG; ypo:BZ17_4223; -.
DR KEGG; yps:pYV0013; -.
DR PATRIC; fig|273123.14.peg.4456; -.
DR OMA; GIANNYT; -.
DR PHI-base; PHI:7901; -.
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:0015031; P:protein transport; 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; IPR045584; Pilin-like.
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.
DR SUPFAM; SSF101967; SSF101967; 1.
DR SUPFAM; SSF54523; SSF54523; 1.
PE 1: Evidence at protein level;
KW Cell adhesion; Cell outer membrane; Coiled coil; Membrane; Plasmid;
KW Protein transport; Signal; Transmembrane; Transmembrane beta strand;
KW Transport; Virulence.
FT SIGNAL 1..25
FT /evidence="ECO:0000255"
FT CHAIN 26..432
FT /note="Adhesin YadA"
FT /id="PRO_0000022701"
FT TRANSMEM 379..389
FT /note="Beta stranded"
FT /evidence="ECO:0000250|UniProtKB:A1JUB7"
FT TRANSMEM 393..404
FT /note="Beta stranded"
FT /evidence="ECO:0000250|UniProtKB:A1JUB7"
FT TRANSMEM 411..417
FT /note="Beta stranded"
FT /evidence="ECO:0000250|UniProtKB:A1JUB7"
FT TRANSMEM 421..432
FT /note="Beta stranded"
FT /evidence="ECO:0000250|UniProtKB:A1JUB7"
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 VARIANT 95..104
FT /note="GLDARAKGIH -> AGGLNARAKDPY (in strain: YPIII)"
FT /evidence="ECO:0000305"
FT VARIANT 124
FT /note="A -> S (in strain: YPIII)"
FT /evidence="ECO:0000305"
FT VARIANT 209
FT /note="L -> H (in strain: YPIII)"
FT /evidence="ECO:0000305"
FT VARIANT 237..239
FT /note="KDN -> EDT (in strain: YPIII)"
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
