P31489 (YADA1_YEREN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Adhesin YadA

Gene names

Name:	yadA
Synonyms:	invA, yop1, yopA

Encoded on

Plasmid pYV6471/76 Ref.1 Ref.2 Ref.6 Ref.7 Ref.8
Plasmid pYV Ref.3
Plasmid pYVe227 Ref.4

Organism

Yersinia enterocolitica

Taxonomic identifier

630 [NCBI]

Taxonomic lineage

cellular organisms › Bacteria › Proteobacteria › Gammaproteobacteria › Enterobacteriales › Enterobacteriaceae › Yersinia

Protein attributes

Sequence length	455 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence 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 process	Cell adhesion Virulence
Cellular component	Cell membrane Cell outer membrane Membrane
Domain	Coiled coil Signal Transmembrane Transmembrane beta strand
Technical term	3D-structure Plasmid
Gene Ontology (GO)
Biological_process	cell adhesion Inferred from electronic annotation. Source: UniProtKB-KW pathogenesis Inferred from electronic annotation. Source: UniProtKB-KW
Cellular_component	cell outer membrane Inferred from electronic annotation. Source: UniProtKB-SubCell integral to membrane Inferred from electronic annotation. Source: UniProtKB-KW plasma membrane Inferred from electronic annotation. Source: UniProtKB-KW
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Signal peptide

1 – 25

25

Chain

26 – 455

430

Adhesin YadA

PRO_0000022699

Regions

Coiled coil

209 – 243

35

Potential

Natural variations

Natural variant

29

1

D → N in strain: Serotype O:9.

Natural variant

49

1

L → Q in strain: Serotype O:9.

Natural variant

65

1

A → C in strain: Serotype O:9.

Natural variant

228

1

R → K in strain: Serotype O:9.

Natural variant

235 – 236

2

NA → KP in strain: Serotype O:9.

Natural variant

435 – 440

6

AGVAYA → PVWLI in strain: Serotype O:9.

Experimental info

Mutagenesis

73 – 75

3

IAI → EDE: 8% of wild-type collagen-binding activity. Ref.7

Mutagenesis

101 – 103

3

VAI → DDE: 3% of wild-type collagen-binding activity. Ref.7

Mutagenesis

155 – 157

3

VAI → DDE: Loss of collagen-binding activity. Ref.7

Mutagenesis

155 – 157

3

VAI → QST: Less than 0.5% of wild-type collagen-binding activity. Ref.7

Mutagenesis

155

1

V → D: Less than 1% of wild-type collagen-binding activity. Ref.7

Mutagenesis

156

1

A → D: Loss of collagen-binding activity. Ref.7

Mutagenesis

171 – 173

3

IAI → EDE: Loss of collagen-binding activity. Ref.7

Mutagenesis

185 – 187

3

VSI → DDE: Loss of collagen-binding activity. Ref.7

Secondary structure

1

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455

Helix Strand Turn

Details...

Beta strand

37 – 39

3

Turn

45 – 47

3

Beta strand

73 – 76

4

Beta strand

87 – 90

4

Beta strand

101 – 104

4

Beta strand

115 – 118

4

Beta strand

128 – 131

4

Beta strand

141 – 144

4

Beta strand

155 – 158

4

Beta strand

171 – 174

4

Beta strand

181 – 183

3

Beta strand

185 – 187

3

Helix

211 – 219

9

Helix

335 – 385

51

Sequences

	Sequence		Length	Mass (Da)
	P31489 [UniParc]. Last modified July 1, 1993. Version 1. Checksum: AC12EF68C657DAC0	FASTA	455	47,136
	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

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.

PIR

S04912.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1P9H	X-ray	1.55	A	26-241	[»]
3LT6	X-ray	1.80	A/B/C/D/E/F	333-396	[»]
3LT7	X-ray	1.50	A/B/C/D/E/F	333-396	[»]

ProteinModelPortal

P31489.

SMR

P31489. Positions 32-220.

ModBase

Search...

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Phylogenomic databases

ProtClustDB

CLSK687512.

Family and domain databases

InterPro

IPR008640. Hep_Hag.
IPR008635. HIM.
IPR008126. OM_adhesion_Yersinia.
IPR005594. YadA_C.
[Graphical view]

Pfam

PF05658. Hep_Hag. 2 hits.
PF05662. HIM. 1 hit.
PF03895. YadA. 1 hit.
[Graphical view]

PRINTS

PR01756. OMADHESIN.

ProtoNet

Search...

Other

EvolutionaryTrace

P31489.

Entry information

Entry name

YADA1_YEREN

Accession

Primary (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:	April 3, 2013
This is version 68 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program