Did you know ? If you order before Friday 14h we deliver 90PCT of the the time next Tuesday, GENTAUR another in time delivery

Adhesin YadA

 YADA1_YEREN             Reviewed;         455 AA.
P31489; O85267;
01-JUL-1993, integrated into UniProtKB/Swiss-Prot.
01-JUL-1993, sequence version 1.
25-OCT-2017, entry version 91.
RecName: Full=Adhesin YadA;
Flags: Precursor;
Name=yadA; Synonyms=invA, yop1, yopA;
Yersinia enterocolitica.
Plasmid pYV6471/76, Plasmid pYV, and Plasmid pYVe227.
Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
Yersiniaceae; Yersinia.
NCBI_TaxID=630;
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
STRAIN=6471/76 / Serotype O:3; PLASMID=pYV6471/76;
PubMed=2761389; DOI=10.1111/j.1365-2958.1989.tb00198.x;
Skurnik M., Wolf-Watz H.;
"Analysis of the yopA gene encoding the Yop1 virulence determinants of
Yersinia spp.";
Mol. Microbiol. 3:517-529(1989).
[2]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
STRAIN=6471/76 / Serotype O:3; PLASMID=pYV6471/76;
PubMed=7934875; DOI=10.1111/j.1365-2958.1993.tb00971.x;
Tamm A., Tarkkanen A., Korhonen T.K., Kuusela P., Toivanen P.,
Skurnik M.;
"Hydrophobic domains affect the collagen-binding specificity and
surface polymerization as well as the virulence potential of the YadA
protein of Yersinia enterocolitica.";
Mol. Microbiol. 10:995-1011(1993).
[3]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
STRAIN=Serotype O:9; PLASMID=pYV;
Iriarte M., Kerbourch C., Lambermont I., Cornelis G.R.;
"YadA and ORF291 of Yersinia enterocolitica O:9.";
Submitted (MAR-1998) to the EMBL/GenBank/DDBJ databases.
[4]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
STRAIN=W22703 / Serotype O:9 / Biotype 2; PLASMID=pYVe227;
Iriarte M., Lambermont I., Kerbourch C., Cornelis G.R.;
"Detailed genetic map of the pYVe227 plasmid of Yersinia
enterocolitica serotype O:9.";
Submitted (OCT-1998) to the EMBL/GenBank/DDBJ databases.
[5]
FUNCTION.
STRAIN=Various strains;
PubMed=2592347; DOI=10.1128/jb.171.12.6674-6679.1989;
Emoedy L., Heesemann J., Wolf-Watz H., Skurnik M., Kapperud G.,
O'Toole P., Wadstroem T.;
"Binding to collagen by Yersinia enterocolitica and Yersinia
pseudotuberculosis: evidence for yopA-mediated and chromosomally
encoded mechanisms.";
J. Bacteriol. 171:6674-6679(1989).
[6]
INDUCTION.
STRAIN=6471/76 / Serotype O:3; PLASMID=pYV6471/76;
PubMed=1548243; DOI=10.1128/jb.174.6.2047-2051.1992;
Skurnik M., Toivanen P.;
"LcrF is the temperature-regulated activator of the yadA gene of
Yersinia enterocolitica and Yersinia pseudotuberculosis.";
J. Bacteriol. 174:2047-2051(1992).
[7]
DOMAIN COLLAGEN-BINDING, AND 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; PLASMID=pYV6471/76;
PubMed=10931316; DOI=10.1046/j.1365-2958.2000.01992.x;
Tahir Y.E., Kuusela P., Skurnik M.;
"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.";
Mol. Microbiol. 37:192-206(2000).
[8]
CRYSTALLIZATION.
STRAIN=6471/76 / Serotype O:3; PLASMID=pYV6471/76;
PubMed=12037311; DOI=10.1107/S0907444902005231;
Nummelin H., El Tahir Y., Ollikka P., Skurnik M., Goldman A.;
"Expression, purification and crystallization of a collagen-binding
fragment of Yersinia adhesin YadA.";
Acta Crystallogr. D 58:1042-1044(2002).
[9]
X-RAY CRYSTALLOGRAPHY (1.55 ANGSTROMS) OF 26-241, AND SUBUNIT.
STRAIN=6471/76 / Serotype O:3;
PubMed=14765110; DOI=10.1038/sj.emboj.7600100;
Nummelin H., Merckel M.C., Leo J.C., Lankinen H., Skurnik M.,
Goldman A.;
"The Yersinia adhesin YadA collagen-binding domain structure is a
novel left-handed parallel beta-roll.";
EMBO J. 23:701-711(2004).
-!- 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.
{ECO:0000269|PubMed:2592347}.
-!- SUBUNIT: Homotrimer. {ECO:0000269|PubMed:14765110}.
-!- SUBCELLULAR LOCATION: Cell surface {ECO:0000250|UniProtKB:P0C2W0}.
Cell outer membrane {ECO:0000250|UniProtKB:P0C2W0}. Note=The C-
terminal translocator domain is localized in the outer membrane
and the passenger domain is at the cell surface.
{ECO:0000250|UniProtKB:P0C2W0}.
-!- INDUCTION: Induced at 37 degrees Celsius by the temperature-
dependent transcriptional activator LcrF (VirF).
{ECO:0000269|PubMed:1548243}.
-!- DOMAIN: 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). {ECO:0000250|UniProtKB:P0C2W0,
ECO:0000269|PubMed:10931316}.
-!- SIMILARITY: Belongs to the autotransporter-2 (AT-2) (TC 1.B.40)
family. {ECO:0000305}.
-----------------------------------------------------------------------
Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
Distributed under the Creative Commons Attribution-NoDerivs License
-----------------------------------------------------------------------
EMBL; X13882; CAA32086.1; -; Genomic_DNA.
EMBL; AF056092; AAC33679.1; -; Genomic_DNA.
EMBL; AF102990; AAD16868.1; -; Genomic_DNA.
PIR; S04912; S04912.
RefSeq; WP_032488477.1; NZ_CTKR01000098.1.
PDB; 1P9H; X-ray; 1.55 A; A=26-241.
PDB; 3LT6; X-ray; 1.80 A; A/B/C/D/E/F=333-396.
PDB; 3LT7; X-ray; 1.50 A; A/B/C/D/E/F=333-396.
PDBsum; 1P9H; -.
PDBsum; 3LT6; -.
PDBsum; 3LT7; -.
ProteinModelPortal; P31489; -.
SMR; P31489; -.
EvolutionaryTrace; P31489; -.
GO; GO:0009279; C:cell outer membrane; IEA:UniProtKB-SubCell.
GO; GO:0009986; C:cell surface; IEA:UniProtKB-SubCell.
GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
GO; GO:0005518; F:collagen binding; IEA:InterPro.
GO; GO:0007155; P:cell adhesion; IEA:UniProtKB-KW.
GO; GO:0009405; P:pathogenesis; IEA:UniProtKB-KW.
Gene3D; 2.150.10.10; -; 1.
InterPro; IPR008640; Adhesin_Head_dom.
InterPro; IPR008635; Coiled_stalk_dom.
InterPro; IPR008126; OM_adhesion_Yersinia.
InterPro; IPR011049; Serralysin-like_metalloprot_C.
InterPro; IPR005594; YadA_C.
Pfam; PF03895; YadA_anchor; 1.
Pfam; PF05658; YadA_head; 1.
Pfam; PF05662; YadA_stalk; 1.
PRINTS; PR01756; OMADHESIN.
1: Evidence at protein level;
3D-structure; Cell adhesion; Cell outer membrane; Coiled coil;
Membrane; Plasmid; Signal; Transmembrane; Transmembrane beta strand;
Virulence.
SIGNAL 1 25
CHAIN 26 455 Adhesin YadA.
/FTId=PRO_0000022699.
REGION 26 363 Surface exposed passenger domain.
{ECO:0000250|UniProtKB:P0C2W0}.
REGION 364 402 Outer membrane translocation of the
passenger domain.
{ECO:0000250|UniProtKB:P0C2W0}.
REGION 403 455 Translocator domain.
{ECO:0000250|UniProtKB:P0C2W0}.
COILED 209 243 {ECO:0000255}.
VARIANT 29 29 D -> N (in strain: Serotype O:9).
VARIANT 49 49 L -> Q (in strain: Serotype O:9).
VARIANT 65 65 A -> C (in strain: Serotype O:9).
VARIANT 228 228 R -> K (in strain: Serotype O:9).
VARIANT 235 236 NA -> KP (in strain: Serotype O:9).
VARIANT 435 440 AGVAYA -> PVWLI (in strain: Serotype
O:9).
MUTAGEN 73 75 IAI->EDE: 8% of wild-type collagen-
binding activity.
{ECO:0000269|PubMed:10931316}.
MUTAGEN 101 103 VAI->DDE: 3% of wild-type collagen-
binding activity.
{ECO:0000269|PubMed:10931316}.
MUTAGEN 155 157 VAI->DDE: Loss of collagen-binding
activity. {ECO:0000269|PubMed:10931316}.
MUTAGEN 155 157 VAI->QST: Less than 0.5% of wild-type
collagen-binding activity.
{ECO:0000269|PubMed:10931316}.
MUTAGEN 155 155 V->D: Less than 1% of wild-type collagen-
binding activity.
{ECO:0000269|PubMed:10931316}.
MUTAGEN 156 156 A->D: Loss of collagen-binding activity.
{ECO:0000269|PubMed:10931316}.
MUTAGEN 171 173 IAI->EDE: Loss of collagen-binding
activity. {ECO:0000269|PubMed:10931316}.
MUTAGEN 185 187 VSI->DDE: Loss of collagen-binding
activity. {ECO:0000269|PubMed:10931316}.
STRAND 37 39 {ECO:0000244|PDB:1P9H}.
TURN 45 47 {ECO:0000244|PDB:1P9H}.
STRAND 73 76 {ECO:0000244|PDB:1P9H}.
STRAND 87 90 {ECO:0000244|PDB:1P9H}.
STRAND 101 104 {ECO:0000244|PDB:1P9H}.
STRAND 115 118 {ECO:0000244|PDB:1P9H}.
STRAND 128 131 {ECO:0000244|PDB:1P9H}.
STRAND 141 144 {ECO:0000244|PDB:1P9H}.
STRAND 155 158 {ECO:0000244|PDB:1P9H}.
STRAND 171 174 {ECO:0000244|PDB:1P9H}.
STRAND 181 183 {ECO:0000244|PDB:1P9H}.
STRAND 185 187 {ECO:0000244|PDB:1P9H}.
HELIX 211 219 {ECO:0000244|PDB:1P9H}.
HELIX 335 385 {ECO:0000244|PDB:3LT7}.
HELIX 387 394 {ECO:0000244|PDB:3LT7}.
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


Related products :

Catalog number Product name Quantity
orb71328 Ac-Adhesin (1025-1044) peptide This is Ac-Adhesin (1025-1044) peptide. For research use only. 1 mg
SP-86487-1 Ac-Adhesin (1025-1044) amide [Ac-Gln-Leu-Lys-Thr-Ala-Asp-Leu-Pro-Ala-Gly-Arg-Asp-Glu-Thr-Thr-Ser-Phe-Val-Leu-Val- NH2 (MW: 2202.51)] 1 mg
SP2138a p1025, Acetyl _ Adhesin Peptide (1025 _ 1044), amide 1mg
SP2138b p1025, Acetyl _ Adhesin Peptide (1025 _ 1044), amide 5mg
SP2138a p1025, Acetyl - Adhesin Peptide (1025 - 1044), amide 0.5 mg
SP2138b p1025, Acetyl - Adhesin Peptide (1025 - 1044), amide 1 mg
SP2138a p1025, Acetyl - Adhesin Peptide (1025 - 1044), amide 2
SP2138b p1025, Acetyl - Adhesin Peptide (1025 - 1044), amide
'AP54814SU-N Cable pili-associated 22 kDa adhesin protein antibody Ab host: Rabbit 0.2 ml


 

GENTAUR Belgium BVBA BE0473327336
Voortstraat 49, 1910 Kampenhout BELGIUM
Tel 0032 16 58 90 45

Fax 0032 16 50 90 45
info@gentaur.com | Gentaur





GENTAUR Ltd.
Howard Frank Turnberry House
1404-1410 High Road
Whetstone London N20 9BH
Tel 020 3393 8531 Fax 020 8445 9411
uk@gentaur.com | Gentaur

 

 




GENTAUR France SARL
9, rue Lagrange, 75005 Paris
Tel 01 43 25 01 50

Fax 01 43 25 01 60
RCS Paris B 484 237 888

SIRET 48423788800017

BNP PARIBAS PARIS PL MAUBERT BIC BNPAFRPPPRG

france@gentaur.com | Gentaur

GENTAUR GmbH
Marienbongard 20
52062 Aachen Deutschland
Support Karolina Elandt
Tel: 0035929830070
Fax: (+49) 241 56 00 47 88

Logistic :0241 40 08 90 86
Bankleitzahl 39050000
IBAN lautet DE8839050000107569353
Handelsregister Aachen HR B 16058
Umsatzsteuer-Identifikationsnummer *** DE 815175831
Steuernummer 201/5961/3925
de@gentaur.com | Gentaur

GENTAUR U.S.A
Genprice Inc, Logistics
547, Yurok Circle
San Jose, CA 95123
CA 95123
Tel (408) 780-0908,
Fax (408) 780-0908,
sales@genprice.com

Genprice Inc, Invoices and accounting
6017 Snell Ave, Ste 357
San Jose, CA 95123




GENTAUR Nederland BV
NL850396268B01 KVK nummer 52327027
Kuiper 1
5521 DG Eersel Nederland
Tel:  0208-080893  Fax: 0497-517897
nl@gentaur.com | Gentaur
IBAN: NL04 RABO 0156 9854 62   SWIFT RABONL2U






GENTAUR Spain
tel:0911876558
spain@gentaur.com | Gentaur






ГЕНТАУЪР БЪЛГАРИЯ
ID # 201 358 931 /BULSTAT
София 1000, ул. "Граф Игнатиев" 53 вх. В, ет. 2
Tel 0035924682280 Fax 0035924808322
e-mail: Sofia@gentaur.com | Gentaur
IBAN: BG11FINV91501014771636
BIC: FINVBGSF

GENTAUR Poland Sp. z o.o.


ul. Grunwaldzka 88/A m.2
81-771 Sopot, Poland
TEL Gdansk 058 710 33 44 FAX  058 710 33 48              

poland@gentaur.com | Gentaur

Other countries

Österreich +43720880899

Canada Montreal +15149077481

Ceská republika Praha +420246019719

Danmark +4569918806

Finland Helsset +358942419041

Magyarország Budapest +3619980547

Ireland Dublin+35316526556

Luxembourg+35220880274

Norge Oslo+4721031366

Sverige Stockholm+46852503438

Schweiz Züri+41435006251

US New York+17185132983

GENTAUR Italy
SRL IVA IT03841300167
Piazza Giacomo Matteotti, 6
24122 Bergamo Tel 02 36 00 65 93
Fax 02 36 00 65 94
italia@gentaur.com | Gentaur