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Protein

Adhesin YadA

Gene

yadA

Organism
Yersinia enterocolitica
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

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.1 Publication

GO - Biological processi

Complete GO annotation...

Keywords - Biological processi

Cell adhesion, Virulence

Names & Taxonomyi

Protein namesi
Recommended name:
Adhesin YadA
Gene namesi
Name:yadA
Synonyms:invA, yop1, yopA
Encoded oniPlasmid pYV6471/765 Publications
Plasmid pYV1 Publication
Plasmid pYVe2271 Publication
OrganismiYersinia enterocolitica
Taxonomic identifieri630 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacteralesYersiniaceaeYersinia

Subcellular locationi

  • Cell surface By similarity
  • Cell outer membrane By similarity

  • Note: The C-terminal translocator domain is localized in the outer membrane and the passenger domain is at the cell surface.By similarity

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cell outer membrane, Membrane

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi73 – 75IAI → EDE: 8% of wild-type collagen-binding activity. 1 Publication3
Mutagenesisi101 – 103VAI → DDE: 3% of wild-type collagen-binding activity. 1 Publication3
Mutagenesisi155 – 157VAI → DDE: Loss of collagen-binding activity. 1 Publication3
Mutagenesisi155 – 157VAI → QST: Less than 0.5% of wild-type collagen-binding activity. 1 Publication3
Mutagenesisi155V → D: Less than 1% of wild-type collagen-binding activity. 1 Publication1
Mutagenesisi156A → D: Loss of collagen-binding activity. 1 Publication1
Mutagenesisi171 – 173IAI → EDE: Loss of collagen-binding activity. 1 Publication3
Mutagenesisi185 – 187VSI → DDE: Loss of collagen-binding activity. 1 Publication3

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Signal peptidei1 – 25Add BLAST25
ChainiPRO_000002269926 – 455Adhesin YadAAdd BLAST430

Expressioni

Inductioni

Induced at 37 degrees Celsius by the temperature-dependent transcriptional activator LcrF (VirF).1 Publication

Interactioni

Subunit structurei

Homotrimer.1 Publication

Structurei

Secondary structure

1455
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi37 – 39Combined sources3
Turni45 – 47Combined sources3
Beta strandi73 – 76Combined sources4
Beta strandi87 – 90Combined sources4
Beta strandi101 – 104Combined sources4
Beta strandi115 – 118Combined sources4
Beta strandi128 – 131Combined sources4
Beta strandi141 – 144Combined sources4
Beta strandi155 – 158Combined sources4
Beta strandi171 – 174Combined sources4
Beta strandi181 – 183Combined sources3
Beta strandi185 – 187Combined sources3
Helixi211 – 219Combined sources9
Helixi335 – 385Combined sources51
Helixi387 – 394Combined sources8

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB 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[»]
ProteinModelPortaliP31489.
SMRiP31489.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP31489.

Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni26 – 363Surface exposed passenger domainBy similarityAdd BLAST338
Regioni364 – 402Outer membrane translocation of the passenger domainBy similarityAdd BLAST39
Regioni403 – 455Translocator domainBy similarityAdd BLAST53

Coiled coil

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Coiled coili209 – 243Sequence analysisAdd BLAST35

Domaini

The signal peptide, cleaved at the inner membrane, guides the autotransporter protein to the periplasmic space. Then, insertion of the C-terminal translocator domain in the outer membrane forms a hydrophilic pore for the translocation of the passenger domain to the bacterial cell surface (By similarity). 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 (PubMed:10931316).By similarity1 Publication

Sequence similaritiesi

Keywords - Domaini

Coiled coil, Signal, Transmembrane, Transmembrane beta strand

Family and domain databases

Gene3Di2.150.10.10. 1 hit.
InterProiIPR008640. Adhesin_Head_dom.
IPR008635. Coiled_stalk_dom.
IPR008126. OM_adhesion_Yersinia.
IPR011049. Serralysin-like_metalloprot_C.
IPR005594. YadA_C.
[Graphical view]
PfamiPF03895. YadA_anchor. 1 hit.
PF05658. YadA_head. 2 hits.
PF05662. YadA_stalk. 1 hit.
[Graphical view]
PRINTSiPR01756. OMADHESIN.

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

P31489-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MTKDFKISVS AALISALFSS PYAFADDYDG IPNLTAVQIS PNADPALGLE
60 70 80 90 100
YPVRPPVPGA GGLNASAKGI HSIAIGATAE AAKGAAVAVG AGSIATGVNS
110 120 130 140 150
VAIGPLSKAL GDSAVTYGAA STAQKDGVAI GARASTSDTG VAVGFNSKAD
160 170 180 190 200
AKNSVAIGHS SHVAANHGYS IAIGDRSKTD RENSVSIGHE SLNRQLTHLA
210 220 230 240 250
AGTKDTDAVN VAQLKKEIEK TQENTNKRSA ELLANANAYA DNKSSSVLGI
260 270 280 290 300
ANNYTDSKSA ETLENARKEA FAQSKDVLNM AKAHSNSVAR TTLETAEEHA
310 320 330 340 350
NSVARTTLET AEEHANKKSA EALASANVYA DSKSSHTLKT ANSYTDVTVS
360 370 380 390 400
NSTKKAIRES NQYTDHKFRQ LDNRLDKLDT RVDKGLASSA ALNSLFQPYG
410 420 430 440 450
VGKVNFTAGV GGYRSSQALA IGSGYRVNEN VALKAGVAYA GSSDVMYNAS

FNIEW
Length:455
Mass (Da):47,136
Last modified:July 1, 1993 - v1
Checksum:iAC12EF68C657DAC0
GO

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural varianti29D → N in strain: Serotype O:9. 1
Natural varianti49L → Q in strain: Serotype O:9. 1
Natural varianti65A → C in strain: Serotype O:9. 1
Natural varianti228R → K in strain: Serotype O:9. 1
Natural varianti235 – 236NA → KP in strain: Serotype O:9. 2
Natural varianti435 – 440AGVAYA → PVWLI in strain: Serotype O:9. 6

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X13882 Genomic DNA. Translation: CAA32086.1.
AF056092 Genomic DNA. Translation: AAC33679.1.
AF102990 Genomic DNA. Translation: AAD16868.1.
PIRiS04912.
RefSeqiWP_032488477.1. NZ_CTKR01000098.1.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X13882 Genomic DNA. Translation: CAA32086.1.
AF056092 Genomic DNA. Translation: AAC33679.1.
AF102990 Genomic DNA. Translation: AAD16868.1.
PIRiS04912.
RefSeqiWP_032488477.1. NZ_CTKR01000098.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB 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[»]
ProteinModelPortaliP31489.
SMRiP31489.
ModBaseiSearch...
MobiDBiSearch...

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Miscellaneous databases

EvolutionaryTraceiP31489.

Family and domain databases

Gene3Di2.150.10.10. 1 hit.
InterProiIPR008640. Adhesin_Head_dom.
IPR008635. Coiled_stalk_dom.
IPR008126. OM_adhesion_Yersinia.
IPR011049. Serralysin-like_metalloprot_C.
IPR005594. YadA_C.
[Graphical view]
PfamiPF03895. YadA_anchor. 1 hit.
PF05658. YadA_head. 2 hits.
PF05662. YadA_stalk. 1 hit.
[Graphical view]
PRINTSiPR01756. OMADHESIN.
ProtoNetiSearch...

Entry informationi

Entry nameiYADA1_YEREN
AccessioniPrimary (citable) accession number: P31489
Secondary accession number(s): O85267
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 1, 1993
Last sequence update: July 1, 1993
Last modified: November 30, 2016
This is version 87 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Plasmid

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.