YADA1_YEREN
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 25-MAY-2022, entry version 104.
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; Proteobacteria; 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:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
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 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; 1.
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 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 collagen-
FT 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
