YADA_YERE8
ID YADA_YERE8 Reviewed; 422 AA.
AC A1JUB7; Q56930; Q84GR6; Q93KR4;
DT 01-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT 06-FEB-2007, sequence version 1.
DT 25-MAY-2022, entry version 82.
DE RecName: Full=Adhesin YadA;
DE AltName: Full=Protein Yop1 {ECO:0000303|PubMed:2761389};
DE AltName: Full=Trimeric autotransporter adhesin YadA {ECO:0000303|PubMed:23142870};
DE Short=TAA YadA {ECO:0000303|PubMed:23142870};
DE AltName: Full=Type 5 secretion system autotransporter YadA;
DE Flags: Precursor;
GN Name=yadA {ECO:0000303|PubMed:11402007};
GN Synonyms=yopA {ECO:0000303|PubMed:2761389}; OrderedLocusNames=YEP0066;
OS Yersinia enterocolitica serotype O:8 / biotype 1B (strain NCTC 13174 /
OS 8081).
OG Plasmid pYVe8081.
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Yersiniaceae; Yersinia.
OX NCBI_TaxID=393305;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=NCTC 13174 / 8081; PLASMID=pYVe8081;
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=NCTC 13174 / 8081; PLASMID=pYVe8081;
RX PubMed=11402007; DOI=10.1128/iai.69.7.4627-4638.2001;
RA Snellings N.J., Popek M., Lindler L.E.;
RT "Complete DNA sequence of Yersinia enterocolitica serotype 0:8 low-calcium-
RT response plasmid reveals a new virulence plasmid-associated replicon.";
RL Infect. Immun. 69:4627-4638(2001).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NCTC 13174 / 8081;
RX PubMed=17173484; DOI=10.1371/journal.pgen.0020206;
RA Thomson N.R., Howard S., Wren B.W., Holden M.T.G., Crossman L.,
RA Challis G.L., Churcher C., Mungall K., Brooks K., Chillingworth T.,
RA Feltwell T., Abdellah Z., Hauser H., Jagels K., Maddison M., Moule S.,
RA Sanders M., Whitehead S., Quail M.A., Dougan G., Parkhill J.,
RA Prentice M.B.;
RT "The complete genome sequence and comparative genome analysis of the high
RT pathogenicity Yersinia enterocolitica strain 8081.";
RL PLoS Genet. 2:2039-2051(2006).
RN [4]
RP FUNCTION, EXPRESSION IN E.COLI, SUBUNIT, SUBCELLULAR LOCATION, AND
RP MUTAGENESIS OF GLY-389.
RX PubMed=17921300; DOI=10.1128/jb.00985-07;
RA Grosskinsky U., Schuetz M., Fritz M., Schmid Y., Lamparter M.C.,
RA Szczesny P., Lupas A.N., Autenrieth I.B., Linke D.;
RT "A conserved glycine residue of trimeric autotransporter domains plays a
RT key role in Yersinia adhesin A autotransport.";
RL J. Bacteriol. 189:9011-9019(2007).
RN [5] {ECO:0007744|PDB:2LME}
RP STRUCTURE BY NMR OF 333-422, SUBUNIT, SUBCELLULAR LOCATION, AND DOMAIN.
RX PubMed=23142870; DOI=10.1038/nmeth.2248;
RA Shahid S.A., Bardiaux B., Franks W.T., Krabben L., Habeck M.,
RA van Rossum B.J., Linke D.;
RT "Membrane-protein structure determination by solid-state NMR spectroscopy
RT of microcrystals.";
RL Nat. Methods 9:1212-1217(2012).
CC -!- FUNCTION: Collagen-binding outer membrane protein forming a fibrillar
CC matrix on the bacterial cell surface and phagocytosis resistance (By
CC similarity). Promotes initial attachment and invasion of eukaryotic
CC cells (Probable). Also protects the bacteria by being responsible for
CC agglutination, serum resistance and complement inactivation. Gly-389
CC plays an important role in this protein; replacing it with increasingly
CC large polar residues decreases expression levels and trimer stability.
CC Residues larger than Ser (Thr, Asn or His) significantly decrease
CC serume resistance and bacterial autoagglution without affecting
CC adhesion to host cells or host cell cytokine production
CC (PubMed:17921300). {ECO:0000250|UniProtKB:P0C2W0,
CC ECO:0000269|PubMed:17921300, ECO:0000305|PubMed:17921300}.
CC -!- SUBUNIT: Homotrimer; trimers are very stable, not disrupted by heating
CC at 95 degrees Celsius for 10 minutes in SDS sample buffer.
CC {ECO:0000269|PubMed:17921300, ECO:0000269|PubMed:23142870}.
CC -!- SUBCELLULAR LOCATION: Cell surface {ECO:0000269|PubMed:17921300,
CC ECO:0000305|PubMed:23142870}. Cell outer membrane
CC {ECO:0000269|PubMed:17921300, ECO:0000305|PubMed:23142870}. Note=The C-
CC terminal translocator domain is localized in the outer membrane and the
CC passenger domain is at the cell surface. {ECO:0000305|PubMed:23142870}.
CC -!- DOMAIN: The signal peptide, cleaved at the inner membrane, guides the
CC autotransporter protein to the periplasmic space. Then, insertion of
CC the trimerized C-terminal translocator domain in the outer membrane
CC forms a hydrophilic pore for the translocation of the passenger domain
CC to the bacterial cell surface. The passenger domain is probably
CC exported as a hairpin structure, with all 3 strands of the trimer in
CC the pore simultaneously. {ECO:0000305|PubMed:23142870}.
CC -!- MISCELLANEOUS: Expression of mutant proteins in E.coli is improved in a
CC degP deletion, suggesting the mutants are susceptible to degradation in
CC the periplasm. {ECO:0000269|PubMed:17921300}.
CC -!- SIMILARITY: Belongs to the autotransporter-2 (AT-2) (TC 1.B.40) family.
CC {ECO:0000305}.
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DR EMBL; X13881; CAA32085.1; -; Genomic_DNA.
DR EMBL; AF336309; AAK69254.1; -; Genomic_DNA.
DR EMBL; AM286416; CAL10087.1; -; Genomic_DNA.
DR PIR; S04911; S04911.
DR RefSeq; NP_863557.1; NC_005017.1.
DR RefSeq; WP_011117647.1; NC_008791.1.
DR RefSeq; YP_001004112.1; NC_008791.1.
DR PDB; 2LME; NMR; -; A/B/C=333-422.
DR PDBsum; 2LME; -.
DR AlphaFoldDB; A1JUB7; -.
DR BMRB; A1JUB7; -.
DR SMR; A1JUB7; -.
DR STRING; 393305.YEP0066; -.
DR EnsemblBacteria; CAL10087; CAL10087; YEP0066.
DR KEGG; yen:YEP0066; -.
DR PATRIC; fig|393305.7.peg.65; -.
DR eggNOG; COG1293; Bacteria.
DR eggNOG; COG5295; Bacteria.
DR HOGENOM; CLU_046286_0_0_6; -.
DR OMA; GIANNYT; -.
DR PRO; PR:A1JUB7; -.
DR Proteomes; UP000000642; Plasmid pYVe8081.
DR GO; GO:0009279; C:cell outer membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0009986; C:cell surface; IEA:UniProtKB-SubCell.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005518; F:collagen binding; IEA:InterPro.
DR GO; GO:0007155; P:cell adhesion; IEA:UniProtKB-KW.
DR GO; GO:0015031; P:protein transport; IEA:UniProtKB-KW.
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; 3.
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..422
FT /note="Adhesin YadA"
FT /id="PRO_0000285834"
FT TRANSMEM 369..379
FT /note="Beta stranded"
FT /evidence="ECO:0000305|PubMed:23142870,
FT ECO:0007744|PDB:2LME"
FT TRANSMEM 383..394
FT /note="Beta stranded"
FT /evidence="ECO:0000305|PubMed:23142870,
FT ECO:0007744|PDB:2LME"
FT TRANSMEM 401..407
FT /note="Beta stranded"
FT /evidence="ECO:0000305|PubMed:23142870,
FT ECO:0007744|PDB:2LME"
FT TRANSMEM 411..422
FT /note="Beta stranded"
FT /evidence="ECO:0000305|PubMed:23142870,
FT ECO:0007744|PDB:2LME"
FT REGION 26..330
FT /note="Surface exposed passenger domain"
FT /evidence="ECO:0000305|PubMed:23142870"
FT REGION 331..368
FT /note="Outer membrane translocation of the passenger
FT domain"
FT /evidence="ECO:0000305|PubMed:23142870"
FT REGION 369..422
FT /note="Translocator domain"
FT /evidence="ECO:0000305|PubMed:23142870"
FT COILED 206..236
FT /evidence="ECO:0000255"
FT MUTAGEN 389
FT /note="G->A: Full-length protein behaves like wild-type,
FT the membrane anchor domain (residues 335-422) trimerizes
FT poorly."
FT /evidence="ECO:0000269|PubMed:17921300"
FT MUTAGEN 389
FT /note="G->H,N,T: Loss of resistance to serum complement,
FT loss of autoagglutination, still expressed on bacteria
FT surface, still binds HeLa cells, weakly forms trimers that
FT dissociate fully upon heating, a membrane anchor domain
FT (residues 335-422) cannot be isolated."
FT /evidence="ECO:0000269|PubMed:17921300"
FT MUTAGEN 389
FT /note="G->S: Forms trimers that dissociate fully upon
FT heating, the membrane anchor domain (residues 335-422)
FT trimerizes very poorly."
FT /evidence="ECO:0000269|PubMed:17921300"
FT CONFLICT 282
FT /note="T -> P (in Ref. 1; CAA32085)"
FT /evidence="ECO:0000305"
FT HELIX 333..360
FT /evidence="ECO:0007829|PDB:2LME"
FT STRAND 368..380
FT /evidence="ECO:0007829|PDB:2LME"
FT STRAND 383..398
FT /evidence="ECO:0007829|PDB:2LME"
FT STRAND 401..407
FT /evidence="ECO:0007829|PDB:2LME"
FT TURN 408..410
FT /evidence="ECO:0007829|PDB:2LME"
FT STRAND 411..422
FT /evidence="ECO:0007829|PDB:2LME"
SQ SEQUENCE 422 AA; 44139 MW; FD116472C90B539E CRC64;
MTKDFKISVS AALISALFSS PYAFANNDEV HFTAVQISPN ADPDSHVVIF QPAAEALGGT
NALAKSIHSI AVGASAEAAK QAAVAVGAGS IATGVNSVAI GPLSKALGDS AVTYGAASTA
QKDGVAIGAR AFTSDTGVAV GFNSKVDAKN SVAIGHSSHV AVDHDYSIAI GDRSKTDRKN
SVSIGHESLN RQLTHLAAGT KDTDAVNVAQ LKKEIEKTQV NANKKSAEVL GIANNYTDSK
SAETLENARK EAFDLSNDAL DMAKKHSNSV ARTTLETAEE HTNKKSAETL ARANVYADSK
SSHTLQTANS YTDVTVSNST KKAIRESNQY TDHKFRQLDN RLDKLDTRVD KGLASSAALN
SLFQPYGVGK VNFTAGVGGY RSSQALAIGS GYRVNESVAL KAGVAYAGSS DVMYNASFNI
EW
