ID   YADA1_YEREN             Reviewed;         455 AA.
AC   P31489; O85267;
DT   01-JUL-1993, integrated into UniProtKB/Swiss-Prot.
DT   01-JUL-1993, sequence version 1.
DT   03-MAY-2023, entry version 107.
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;
OS   Yersinia enterocolitica.
OG   Plasmid pYV6471/76, Plasmid pYV, and Plasmid pYVe227.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC   Yersiniaceae; Yersinia.
OX   NCBI_TaxID=630;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=6471/76 / Serotype O:3; PLASMID=pYV6471/76;
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   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=6471/76 / Serotype O:3; PLASMID=pYV6471/76;
RX   PubMed=7934875; DOI=10.1111/j.1365-2958.1993.tb00971.x;
RA   Tamm A., Tarkkanen A., Korhonen T.K., Kuusela P., Toivanen P., Skurnik M.;
RT   "Hydrophobic domains affect the collagen-binding specificity and surface
RT   polymerization as well as the virulence potential of the YadA protein of
RT   Yersinia enterocolitica.";
RL   Mol. Microbiol. 10:995-1011(1993).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=Serotype O:9; PLASMID=pYV;
RA   Iriarte M., Kerbourch C., Lambermont I., Cornelis G.R.;
RT   "YadA and ORF291 of Yersinia enterocolitica O:9.";
RL   Submitted (MAR-1998) to the EMBL/GenBank/DDBJ databases.
RN   [4]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=W22703 / Serotype O:9 / Biotype 2; PLASMID=pYVe227;
RA   Iriarte M., Lambermont I., Kerbourch C., Cornelis G.R.;
RT   "Detailed genetic map of the pYVe227 plasmid of Yersinia enterocolitica
RT   serotype O:9.";
RL   Submitted (OCT-1998) to the EMBL/GenBank/DDBJ databases.
RN   [5]
RP   FUNCTION.
RC   STRAIN=Various strains;
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   [6]
RP   INDUCTION.
RC   STRAIN=6471/76 / Serotype O:3; PLASMID=pYV6471/76;
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   [7]
RP   DOMAIN COLLAGEN-BINDING, AND MUTAGENESIS OF 73-ILE--ILE-75;
RP   101-VAL--ILE-103; 155-VAL--ILE-157; VAL-155; ALA-156; 171-ILE--ILE-173 AND
RP   185-VAL--ILE-187.
RC   STRAIN=6471/76 / Serotype O:3; PLASMID=pYV6471/76;
RX   PubMed=10931316; DOI=10.1046/j.1365-2958.2000.01992.x;
RA   Tahir Y.E., Kuusela P., Skurnik M.;
RT   "Functional mapping of the Yersinia enterocolitica adhesin YadA.
RT   Identification of eight NSVAIG - S motifs in the amino-terminal half of the
RT   protein involved in collagen binding.";
RL   Mol. Microbiol. 37:192-206(2000).
RN   [8]
RP   SUBUNIT, SUBCELLULAR LOCATION, AND DOMAIN.
RC   STRAIN=6471/76 / Serotype O:3; PLASMID=pYV6471/76;
RX   PubMed=22155776; DOI=10.1128/jb.05322-11;
RA   Mikula K.M., Leo J.C., Lyskowski A., Kedracka-Krok S., Pirog A.,
RA   Goldman A.;
RT   "The translocation domain in trimeric autotransporter adhesins is necessary
RT   and sufficient for trimerization and autotransportation.";
RL   J. Bacteriol. 194:827-838(2012).
RN   [9]
RP   CRYSTALLIZATION.
RC   STRAIN=6471/76 / Serotype O:3; PLASMID=pYV6471/76;
RX   PubMed=12037311; DOI=10.1107/s0907444902005231;
RA   Nummelin H., El Tahir Y., Ollikka P., Skurnik M., Goldman A.;
RT   "Expression, purification and crystallization of a collagen-binding
RT   fragment of Yersinia adhesin YadA.";
RL   Acta Crystallogr. D 58:1042-1044(2002).
RN   [10] {ECO:0007744|PDB:1P9H}
RP   X-RAY CRYSTALLOGRAPHY (1.55 ANGSTROMS) OF 26-241, AND SUBUNIT.
RC   STRAIN=6471/76 / Serotype O:3;
RX   PubMed=14765110; DOI=10.1038/sj.emboj.7600100;
RA   Nummelin H., Merckel M.C., Leo J.C., Lankinen H., Skurnik M., Goldman A.;
RT   "The Yersinia adhesin YadA collagen-binding domain structure is a novel
RT   left-handed parallel beta-roll.";
RL   EMBO J. 23:701-711(2004).
CC   -!- FUNCTION: Collagen-binding outer membrane protein forming a fibrillar
CC       matrix on the bacterial cell surface. Promotes initial attachment and
CC       invasion of eukaryotic cells. Also protects the bacteria by being
CC       responsible for agglutination, serum resistance, complement
CC       inactivation and phagocytosis resistance. {ECO:0000269|PubMed:2592347}.
CC   -!- SUBUNIT: Homotrimer; in gels migrates as monomers, dimers and
CC       homotrimers (PubMed:22155776, PubMed:14765110). Does not form trimers
CC       with distantly related EibA from E.coli; coexpression was lethal and
CC       one of the genes is eliminated in vivo. If the full translocator domain
CC       (368-455) is exchanged with that of EibA ('299-392'), will form
CC       heterotrimers with EibA and vice-versa (PubMed:22155776).
CC       {ECO:0000269|PubMed:14765110, ECO:0000269|PubMed:22155776}.
CC   -!- SUBCELLULAR LOCATION: Cell surface {ECO:0000269|PubMed:22155776}. Cell
CC       outer membrane {ECO:0000269|PubMed:22155776}. Note=The C-terminal
CC       translocator domain is localized in the outer membrane and the
CC       passenger domain is at the cell surface. {ECO:0000269|PubMed:22155776}.
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 (By similarity). Then,
CC       trimerization and insertion of the C-terminal translocator domain in
CC       the outer membrane forms a hydrophilic pore for the translocation of
CC       the passenger domain to the bacterial cell surface (PubMed:22155776).
CC       Presents a lollipop-shaped form which consists of three domains: a C-
CC       terminal membrane-anchor domain, a coiled-coil stalk domain and an oval
CC       N-terminal head domain. The N-terminal half of the sequence reveals the
CC       presence of repeated motifs with the consensus sequence NSVAIGXXS. They
CC       form the turns and hydrophobic core of the nine-coiled left-handed
CC       parallel beta-roll and trimer structure essential for the collagen-
CC       binding activity (PubMed:10931316). {ECO:0000250|UniProtKB:P0C2W0,
CC       ECO:0000269|PubMed:10931316, ECO:0000269|PubMed:22155776}.
CC   -!- SIMILARITY: Belongs to the autotransporter-2 (AT-2) (TC 1.B.40) family.
CC       {ECO:0000305}.
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DR   EMBL; X13882; CAA32086.1; -; Genomic_DNA.
DR   EMBL; AF056092; AAC33679.1; -; Genomic_DNA.
DR   EMBL; AF102990; AAD16868.1; -; Genomic_DNA.
DR   PIR; S04912; S04912.
DR   RefSeq; WP_032488477.1; NZ_CTKR01000098.1.
DR   PDB; 1P9H; X-ray; 1.55 A; A=26-241.
DR   PDBsum; 1P9H; -.
DR   AlphaFoldDB; P31489; -.
DR   BMRB; P31489; -.
DR   SMR; P31489; -.
DR   EvolutionaryTrace; P31489; -.
DR   PHI-base; PHI:6253; -.
DR   GO; GO:0009279; C:cell outer membrane; IDA:UniProtKB.
DR   GO; GO:0009986; C:cell surface; IDA:UniProtKB.
DR   GO; GO:0005518; F:collagen binding; IDA:UniProtKB.
DR   GO; GO:0007155; P:cell adhesion; IEA:UniProtKB-KW.
DR   GO; GO:0046819; P:protein secretion by the type V secretion system; IMP:UniProtKB.
DR   CDD; cd12820; LbR_YadA-like; 1.
DR   Gene3D; 3.30.1300.30; GSPII I/J protein-like; 1.
DR   Gene3D; 2.150.10.10; Serralysin-like metalloprotease, C-terminal; 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; 6.
DR   Pfam; PF05662; YadA_stalk; 1.
DR   PRINTS; PR01756; OMADHESIN.
DR   SUPFAM; SSF101967; Adhesin YadA, collagen-binding domain; 1.
DR   SUPFAM; SSF54523; Pili subunits; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Cell adhesion; Cell outer membrane; Coiled coil; Membrane;
KW   Plasmid; Protein transport; Signal; Transmembrane;
KW   Transmembrane beta strand; Transport; Virulence.
FT   SIGNAL          1..25
FT                   /evidence="ECO:0000255"
FT   CHAIN           26..455
FT                   /note="Adhesin YadA"
FT                   /id="PRO_0000022699"
FT   TRANSMEM        402..412
FT                   /note="Beta stranded"
FT                   /evidence="ECO:0000250|UniProtKB:A1JUB7"
FT   TRANSMEM        416..427
FT                   /note="Beta stranded"
FT                   /evidence="ECO:0000250|UniProtKB:A1JUB7"
FT   TRANSMEM        434..440
FT                   /note="Beta stranded"
FT                   /evidence="ECO:0000250|UniProtKB:A1JUB7"
FT   TRANSMEM        444..455
FT                   /note="Beta stranded"
FT                   /evidence="ECO:0000250|UniProtKB:A1JUB7"
FT   REGION          26..363
FT                   /note="Surface exposed passenger domain"
FT                   /evidence="ECO:0000250|UniProtKB:P0C2W0"
FT   REGION          364..402
FT                   /note="Outer membrane translocation of the passenger
FT                   domain"
FT                   /evidence="ECO:0000250|UniProtKB:P0C2W0"
FT   REGION          403..455
FT                   /note="Translocator domain"
FT                   /evidence="ECO:0000250|UniProtKB:P0C2W0"
FT   COILED          209..243
FT                   /evidence="ECO:0000255"
FT   VARIANT         29
FT                   /note="D -> N (in strain: Serotype O:9)"
FT   VARIANT         49
FT                   /note="L -> Q (in strain: Serotype O:9)"
FT   VARIANT         65
FT                   /note="A -> C (in strain: Serotype O:9)"
FT   VARIANT         228
FT                   /note="R -> K (in strain: Serotype O:9)"
FT   VARIANT         235..236
FT                   /note="NA -> KP (in strain: Serotype O:9)"
FT   VARIANT         435..440
FT                   /note="AGVAYA -> PVWLI (in strain: Serotype O:9)"
FT   MUTAGEN         73..75
FT                   /note="IAI->EDE: 8% of wild-type collagen-binding
FT                   activity."
FT                   /evidence="ECO:0000269|PubMed:10931316"
FT   MUTAGEN         101..103
FT                   /note="VAI->DDE: 3% of wild-type collagen-binding
FT                   activity."
FT                   /evidence="ECO:0000269|PubMed:10931316"
FT   MUTAGEN         155..157
FT                   /note="VAI->DDE: Loss of collagen-binding activity."
FT                   /evidence="ECO:0000269|PubMed:10931316"
FT   MUTAGEN         155..157
FT                   /note="VAI->QST: Less than 0.5% of wild-type
FT                   collagen-binding activity."
FT                   /evidence="ECO:0000269|PubMed:10931316"
FT   MUTAGEN         155
FT                   /note="V->D: Less than 1% of wild-type collagen-binding
FT                   activity."
FT                   /evidence="ECO:0000269|PubMed:10931316"
FT   MUTAGEN         156
FT                   /note="A->D: Loss of collagen-binding activity."
FT                   /evidence="ECO:0000269|PubMed:10931316"
FT   MUTAGEN         171..173
FT                   /note="IAI->EDE: Loss of collagen-binding activity."
FT                   /evidence="ECO:0000269|PubMed:10931316"
FT   MUTAGEN         185..187
FT                   /note="VSI->DDE: Loss of collagen-binding activity."
FT                   /evidence="ECO:0000269|PubMed:10931316"
FT   STRAND          37..39
FT                   /evidence="ECO:0007829|PDB:1P9H"
FT   TURN            45..47
FT                   /evidence="ECO:0007829|PDB:1P9H"
FT   STRAND          73..76
FT                   /evidence="ECO:0007829|PDB:1P9H"
FT   STRAND          87..90
FT                   /evidence="ECO:0007829|PDB:1P9H"
FT   STRAND          101..104
FT                   /evidence="ECO:0007829|PDB:1P9H"
FT   STRAND          115..118
FT                   /evidence="ECO:0007829|PDB:1P9H"
FT   STRAND          128..131
FT                   /evidence="ECO:0007829|PDB:1P9H"
FT   STRAND          141..144
FT                   /evidence="ECO:0007829|PDB:1P9H"
FT   STRAND          155..158
FT                   /evidence="ECO:0007829|PDB:1P9H"
FT   STRAND          171..174
FT                   /evidence="ECO:0007829|PDB:1P9H"
FT   STRAND          181..183
FT                   /evidence="ECO:0007829|PDB:1P9H"
FT   STRAND          185..187
FT                   /evidence="ECO:0007829|PDB:1P9H"
FT   HELIX           211..219
FT                   /evidence="ECO:0007829|PDB:1P9H"
SQ   SEQUENCE   455 AA;  47136 MW;  AC12EF68C657DAC0 CRC64;
     MTKDFKISVS AALISALFSS PYAFADDYDG IPNLTAVQIS PNADPALGLE YPVRPPVPGA
     GGLNASAKGI HSIAIGATAE AAKGAAVAVG AGSIATGVNS VAIGPLSKAL GDSAVTYGAA
     STAQKDGVAI GARASTSDTG VAVGFNSKAD AKNSVAIGHS SHVAANHGYS IAIGDRSKTD
     RENSVSIGHE SLNRQLTHLA AGTKDTDAVN VAQLKKEIEK TQENTNKRSA ELLANANAYA
     DNKSSSVLGI ANNYTDSKSA ETLENARKEA FAQSKDVLNM AKAHSNSVAR TTLETAEEHA
     NSVARTTLET AEEHANKKSA EALASANVYA DSKSSHTLKT ANSYTDVTVS NSTKKAIRES
     NQYTDHKFRQ LDNRLDKLDT RVDKGLASSA ALNSLFQPYG VGKVNFTAGV GGYRSSQALA
     IGSGYRVNEN VALKAGVAYA GSSDVMYNAS FNIEW
//