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P31489 (YADA1_YEREN) Reviewed, UniProtKB/Swiss-Prot

Last modified May 14, 2014. Version 74. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Adhesin YadA
Gene names
Name:yadA
Synonyms:invA, yop1, yopA
Encoded onPlasmid pYV6471/76 Ref.1 Ref.2 Ref.6 Ref.7 Ref.8
Plasmid pYV Ref.3
Plasmid pYVe227 Ref.4
OrganismYersinia enterocolitica
Taxonomic identifier630 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeYersinia

Protein attributes

Sequence length455 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Collagen-binding outer membrane protein forming a fibrillar matrix on the bacterial cell surface. Promotes initial attachment and invasion of eukaryotic cells. Also protects the bacteria by being responsible for agglutination, serum resistance, complement inactivation and phagocytosis resistance. Ref.5

Subunit structure

Homotrimer.

Subcellular location

Cell outer membrane.

Induction

Induced at 37 degrees Celsius by the temperature-dependent transcriptional activator LcrF (VirF). Ref.6

Domain

Presents a lollipop-shaped form which consists of three domains: a C-terminal membrane-anchor domain, a coiled-coil stalk domain and an oval N-terminal head domain. The N-terminal half of the sequence reveals the presence of repeated motifs with the consensus sequence NSVAIGXXS. They form the turns and hydrophobic core of the nine-coiled left-handed parallel beta-roll and trimer structure essential for the collagen-binding activity. Ref.7

Sequence similarities

Belongs to the autotransporter-2 (TC 1.B.40) / oligomeric coiled-coil adhesin (Oca) family. [View classification]

Ontologies

Keywords
   Biological processCell adhesion
Virulence
   Cellular componentCell outer membrane
Membrane
   DomainCoiled coil
Signal
Transmembrane
Transmembrane beta strand
   Technical term3D-structure
Plasmid
Gene Ontology (GO)
   Biological_processcell adhesion

Inferred from electronic annotation. Source: UniProtKB-KW

pathogenesis

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular_componentcell outer membrane

Inferred from electronic annotation. Source: UniProtKB-SubCell

integral component of membrane

Inferred from electronic annotation. Source: UniProtKB-KW

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 2525
Chain26 – 455430Adhesin YadA
PRO_0000022699

Regions

Coiled coil209 – 24335 Potential

Natural variations

Natural variant291D → N in strain: Serotype O:9.
Natural variant491L → Q in strain: Serotype O:9.
Natural variant651A → C in strain: Serotype O:9.
Natural variant2281R → K in strain: Serotype O:9.
Natural variant235 – 2362NA → KP in strain: Serotype O:9.
Natural variant435 – 4406AGVAYA → PVWLI in strain: Serotype O:9.

Experimental info

Mutagenesis73 – 753IAI → EDE: 8% of wild-type collagen-binding activity. Ref.7
Mutagenesis101 – 1033VAI → DDE: 3% of wild-type collagen-binding activity. Ref.7
Mutagenesis155 – 1573VAI → DDE: Loss of collagen-binding activity. Ref.7
Mutagenesis155 – 1573VAI → QST: Less than 0.5% of wild-type collagen-binding activity. Ref.7
Mutagenesis1551V → D: Less than 1% of wild-type collagen-binding activity. Ref.7
Mutagenesis1561A → D: Loss of collagen-binding activity. Ref.7
Mutagenesis171 – 1733IAI → EDE: Loss of collagen-binding activity. Ref.7
Mutagenesis185 – 1873VSI → DDE: Loss of collagen-binding activity. Ref.7

Secondary structure

............................. 455
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P31489 [UniParc].

Last modified July 1, 1993. Version 1.
Checksum: AC12EF68C657DAC0

FASTA45547,136
        10         20         30         40         50         60 
MTKDFKISVS AALISALFSS PYAFADDYDG IPNLTAVQIS PNADPALGLE YPVRPPVPGA 

        70         80         90        100        110        120 
GGLNASAKGI HSIAIGATAE AAKGAAVAVG AGSIATGVNS VAIGPLSKAL GDSAVTYGAA 

       130        140        150        160        170        180 
STAQKDGVAI GARASTSDTG VAVGFNSKAD AKNSVAIGHS SHVAANHGYS IAIGDRSKTD 

       190        200        210        220        230        240 
RENSVSIGHE SLNRQLTHLA AGTKDTDAVN VAQLKKEIEK TQENTNKRSA ELLANANAYA 

       250        260        270        280        290        300 
DNKSSSVLGI ANNYTDSKSA ETLENARKEA FAQSKDVLNM AKAHSNSVAR TTLETAEEHA 

       310        320        330        340        350        360 
NSVARTTLET AEEHANKKSA EALASANVYA DSKSSHTLKT ANSYTDVTVS NSTKKAIRES 

       370        380        390        400        410        420 
NQYTDHKFRQ LDNRLDKLDT RVDKGLASSA ALNSLFQPYG VGKVNFTAGV GGYRSSQALA 

       430        440        450 
IGSGYRVNEN VALKAGVAYA GSSDVMYNAS FNIEW 

« Hide

References

[1]"Analysis of the yopA gene encoding the Yop1 virulence determinants of Yersinia spp."
Skurnik M., Wolf-Watz H.
Mol. Microbiol. 3:517-529(1989) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: 6471/76 / Serotype O:3.
[2]"Hydrophobic domains affect the collagen-binding specificity and surface polymerization as well as the virulence potential of the YadA protein of Yersinia enterocolitica."
Tamm A., Tarkkanen A., Korhonen T.K., Kuusela P., Toivanen P., Skurnik M.
Mol. Microbiol. 10:995-1011(1993) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: 6471/76 / Serotype O:3.
[3]"YadA and ORF291 of Yersinia enterocolitica O:9."
Iriarte M., Kerbourch C., Lambermont I., Cornelis G.R.
Submitted (MAR-1998) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: Serotype O:9.
[4]"Detailed genetic map of the pYVe227 plasmid of Yersinia enterocolitica serotype O:9."
Iriarte M., Lambermont I., Kerbourch C., Cornelis G.R.
Submitted (OCT-1998) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: W22703 / Serotype O:9 / Biotype 2.
[5]"Binding to collagen by Yersinia enterocolitica and Yersinia pseudotuberculosis: evidence for yopA-mediated and chromosomally encoded mechanisms."
Emoedy L., Heesemann J., Wolf-Watz H., Skurnik M., Kapperud G., O'Toole P., Wadstroem T.
J. Bacteriol. 171:6674-6679(1989) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION.
Strain: Various strains.
[6]"LcrF is the temperature-regulated activator of the yadA gene of Yersinia enterocolitica and Yersinia pseudotuberculosis."
Skurnik M., Toivanen P.
J. Bacteriol. 174:2047-2051(1992) [PubMed] [Europe PMC] [Abstract]
Cited for: INDUCTION.
Strain: 6471/76 / Serotype O:3.
[7]"Functional mapping of the Yersinia enterocolitica adhesin YadA. Identification of eight NSVAIG - S motifs in the amino-terminal half of the protein involved in collagen binding."
Tahir Y.E., Kuusela P., Skurnik M.
Mol. Microbiol. 37:192-206(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: DOMAIN COLLAGEN-BINDING, MUTAGENESIS OF 73-ILE--ILE-75; 101-VAL--ILE-103; 155-VAL--ILE-157; VAL-155; ALA-156; 171-ILE--ILE-173 AND 185-VAL--ILE-187.
Strain: 6471/76 / Serotype O:3.
[8]"Expression, purification and crystallization of a collagen-binding fragment of Yersinia adhesin YadA."
Nummelin H., El Tahir Y., Ollikka P., Skurnik M., Goldman A.
Acta Crystallogr. D 58:1042-1044(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: CRYSTALLIZATION.
Strain: 6471/76 / Serotype O:3.
[9]"The Yersinia adhesin YadA collagen-binding domain structure is a novel left-handed parallel beta-roll."
Nummelin H., Merckel M.C., Leo J.C., Lankinen H., Skurnik M., Goldman A.
EMBO J. 23:701-711(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.55 ANGSTROMS) OF 26-241.
Strain: 6471/76 / Serotype O:3.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
X13882 Genomic DNA. Translation: CAA32086.1.
AF056092 Genomic DNA. Translation: AAC33679.1.
AF102990 Genomic DNA. Translation: AAD16868.1.
PIRS04912.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1P9HX-ray1.55A26-241[»]
3LT6X-ray1.80A/B/C/D/E/F333-396[»]
3LT7X-ray1.50A/B/C/D/E/F333-396[»]
ProteinModelPortalP31489.
SMRP31489. Positions 32-220.
ModBaseSearch...
MobiDBSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Family and domain databases

Gene3D2.150.10.10. 1 hit.
InterProIPR008640. Adhesin_Head_dom.
IPR008635. Coiled_stalk_dom.
IPR008126. OM_adhesion_Yersinia.
IPR011049. Serralysin-like_metalloprot_C.
IPR005594. YadA_C.
[Graphical view]
PfamPF03895. YadA_anchor. 1 hit.
PF05658. YadA_head. 2 hits.
PF05662. YadA_stalk. 1 hit.
[Graphical view]
PRINTSPR01756. OMADHESIN.
ProtoNetSearch...

Other

EvolutionaryTraceP31489.

Entry information

Entry nameYADA1_YEREN
AccessionPrimary (citable) accession number: P31489
Secondary accession number(s): O85267
Entry history
Integrated into UniProtKB/Swiss-Prot: July 1, 1993
Last sequence update: July 1, 1993
Last modified: May 14, 2014
This is version 74 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references