YADA2_YEREN
ID YADA2_YEREN Reviewed; 422 AA.
AC P0C2W0; Q56930; Q84GR6; Q93KR4;
DT 01-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2007, sequence version 1.
DT 25-MAY-2022, entry version 67.
DE RecName: Full=Adhesin YadA;
DE AltName: Full=Type 5 secretion system autotransporter YadA {ECO:0000305};
DE Flags: Precursor;
GN Name=yadA;
OS Yersinia enterocolitica.
OG Plasmid pYVa127/90, and Plasmid pYVO8.
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Yersiniaceae; Yersinia.
OX NCBI_TaxID=630;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=A127/90 / Serotype O:8 / Biotype 1B; PLASMID=pYVa127/90;
RX PubMed=14527656; DOI=10.1016/s0923-2508(03)00147-5;
RA Foultier B., Cornelis G.R.;
RT "DNA sequence and analysis of the pYVa127/90 virulence plasmid of Yersinia
RT enterocolitica strain A127/90.";
RL Res. Microbiol. 154:553-557(2003).
RN [2]
RP FUNCTION.
RC STRAIN=Various strains;
RX PubMed=2592347; DOI=10.1128/jb.171.12.6674-6679.1989;
RA Emoedy L., Heesemann J., Wolf-Watz H., Skurnik M., Kapperud G., O'Toole P.,
RA Wadstroem T.;
RT "Binding to collagen by Yersinia enterocolitica and Yersinia
RT pseudotuberculosis: evidence for yopA-mediated and chromosomally encoded
RT mechanisms.";
RL J. Bacteriol. 171:6674-6679(1989).
RN [3]
RP FUNCTION, SUBUNIT, SUBCELLULAR LOCATION, DOMAIN, AND MUTAGENESIS BY DOMAIN
RP DELETION.
RC STRAIN=ATCC 51871 / WA-314 / Serotype O:8; PLASMID=pYVO8;
RX PubMed=12813066; DOI=10.1128/jb.185.13.3735-3744.2003;
RA Roggenkamp A., Ackermann N., Jacobi C.A., Truelzsch K., Hoffmann H.,
RA Heesemann J.;
RT "Molecular analysis of transport and oligomerization of the Yersinia
RT enterocolitica adhesin YadA.";
RL J. Bacteriol. 185:3735-3744(2003).
RN [4]
RP MUTAGENESIS OF HIS-156 AND HIS-159, AND MUTAGENESIS BY DOMAIN DELETION.
RC STRAIN=ATCC 51871 / WA-314 / Serotype O:8; PLASMID=pYVO8;
RX PubMed=11080146; DOI=10.1093/emboj/19.22.5989;
RA Hoiczyk E., Roggenkamp A., Reichenbecher M., Lupas A., Heesemann J.;
RT "Structure and sequence analysis of Yersinia YadA and Moraxella UspAs
RT reveal a novel class of adhesins.";
RL EMBO J. 19:5989-5999(2000).
RN [5]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RC STRAIN=ATCC 51871 / WA-314 / Serotype O:8;
RX PubMed=21536788; DOI=10.1128/iai.01309-10;
RA Mueller N.F., Kaiser P.O., Linke D., Schwarz H., Riess T., Schaefer A.,
RA Eble J.A., Kempf V.A.;
RT "Trimeric autotransporter adhesin-dependent adherence of Bartonella
RT henselae, Bartonella quintana, and Yersinia enterocolitica to matrix
RT components and endothelial cells under static and dynamic flow
RT conditions.";
RL Infect. Immun. 79:2544-2553(2011).
RN [6] {ECO:0007744|PDB:3H7X, ECO:0007744|PDB:3H7Z, ECO:0007744|PDB:3LT6, ECO:0007744|PDB:3LT7}
RP X-RAY CRYSTALLOGRAPHY (1.50 ANGSTROMS) OF 333-396 OF WILD-TYPE AND MUTANTS,
RP SUBUNIT, AND DOMAIN.
RC STRAIN=Serotype O:8;
RX PubMed=20178846; DOI=10.1016/j.jsb.2010.02.009;
RA Alvarez B.H., Gruber M., Ursinus A., Dunin-Horkawicz S., Lupas A.N.,
RA Zeth K.;
RT "A transition from strong right-handed to canonical left-handed
RT supercoiling in a conserved coiled-coil segment of trimeric autotransporter
RT adhesins.";
RL J. Struct. Biol. 170:236-245(2010).
CC -!- FUNCTION: Collagen-binding outer membrane protein forming a fibrillar
CC matrix on the bacterial cell surface. Promotes initial attachment and
CC invasion of eukaryotic cells. Also protects the bacteria by being
CC responsible for agglutination, serum resistance, complement
CC inactivation and phagocytosis resistance. {ECO:0000269|PubMed:12813066,
CC ECO:0000269|PubMed:21536788, ECO:0000269|PubMed:2592347}.
CC -!- SUBUNIT: Homotrimer. {ECO:0000269|PubMed:12813066,
CC ECO:0000269|PubMed:20178846}.
CC -!- SUBCELLULAR LOCATION: Cell surface {ECO:0000269|PubMed:12813066}. Cell
CC outer membrane {ECO:0000269|PubMed:12813066}. Note=The C-terminal
CC translocator domain is localized in the outer membrane and the
CC passenger domain is at the cell surface. {ECO:0000269|PubMed:12813066}.
CC -!- DOMAIN: The signal peptide, cleaved at the inner membrane, guides the
CC autotransporter protein to the periplasmic space. Then, insertion of
CC the C-terminal translocator domain in the outer membrane forms a
CC hydrophilic pore for the translocation of the passenger domain to the
CC bacterial cell surface (PubMed:12813066). The crystallized section of
CC the passenger domain is an entwined trimer, and forms a bent coiled
CC coil 8 nm long and 2.2 nm in diameter. It includes a transition from a
CC right-handed to left-handed coiled coil which occurs over 14 residues
CC (PubMed:20178846). {ECO:0000269|PubMed:12813066,
CC ECO:0000269|PubMed:20178846}.
CC -!- DISRUPTION PHENOTYPE: Decreased binding to host cells and to host
CC collagen I under dynamic flow conditions.
CC {ECO:0000269|PubMed:21536788}.
CC -!- SIMILARITY: Belongs to the autotransporter-2 (AT-2) (TC 1.B.40) family.
CC {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AY150843; AAN37524.1; -; Genomic_DNA.
DR RefSeq; NP_783714.1; NC_004564.1.
DR RefSeq; WP_011100755.1; NZ_NWMR01000033.1.
DR PDB; 3H7X; X-ray; 2.00 A; A/B/C/D/E/F=299-362.
DR PDB; 3H7Z; X-ray; 2.51 A; A=303-362.
DR PDB; 3LT6; X-ray; 1.80 A; A/B/C/D/E/F=333-396.
DR PDB; 3LT7; X-ray; 1.50 A; A/B/C/D/E/F=333-396.
DR PDBsum; 3H7X; -.
DR PDBsum; 3H7Z; -.
DR PDBsum; 3LT6; -.
DR PDBsum; 3LT7; -.
DR AlphaFoldDB; P0C2W0; -.
DR BMRB; P0C2W0; -.
DR SMR; P0C2W0; -.
DR TCDB; 1.B.40.1.1; the autotransporter-2 (at-2) family.
DR EvolutionaryTrace; P0C2W0; -.
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; 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; 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_0000022700"
FT TRANSMEM 369..379
FT /note="Beta stranded"
FT /evidence="ECO:0000250|UniProtKB:A1JUB7"
FT TRANSMEM 383..394
FT /note="Beta stranded"
FT /evidence="ECO:0000250|UniProtKB:A1JUB7"
FT TRANSMEM 401..407
FT /note="Beta stranded"
FT /evidence="ECO:0000250|UniProtKB:A1JUB7"
FT TRANSMEM 411..422
FT /note="Beta stranded"
FT /evidence="ECO:0000250|UniProtKB:A1JUB7"
FT REGION 26..330
FT /note="Surface exposed passenger domain"
FT /evidence="ECO:0000305|PubMed:12813066"
FT REGION 331..369
FT /note="Outer membrane translocation of the passenger
FT domain"
FT /evidence="ECO:0000305|PubMed:12813066"
FT REGION 370..422
FT /note="Translocator domain"
FT /evidence="ECO:0000305|PubMed:12813066"
FT COILED 216..362
FT /evidence="ECO:0000305|PubMed:20178846"
FT MUTAGEN 156
FT /note="H->Y: Loss of collagen-binding activity."
FT /evidence="ECO:0000269|PubMed:11080146"
FT MUTAGEN 159
FT /note="H->Y: Loss of collagen-binding activity."
FT /evidence="ECO:0000269|PubMed:11080146"
FT HELIX 302..352
FT /evidence="ECO:0007829|PDB:3LT7"
FT HELIX 354..361
FT /evidence="ECO:0007829|PDB:3LT7"
SQ SEQUENCE 422 AA; 44155 MW; 38639DD2FEFA23F9 CRC64;
MTKDFKISVS AALISALFSS PYAFANNDEV HFTAVQISPN SDPDSHVMIF QPEVRAPGGT
NALAKGTHSI AVGASAEAAE RAAVAVGAGS IATGVNSVAI GPLSKALGDS AVTYGAGSTA
QKDGVAIGAR ASTSDTGVAV GFNSKVDAKN SVSIGHSSHV AVDHDYSIAI GDRSKTDRKN
SVSIGHESLN RQLTHLAAGT KDTDAVNVAQ LKKEIEKTQE NANKKSAEVL GIANNYTDSK
SAETLENARK EAFDLSNDAL DMAKKHSNSV ARTTLETAEE HTNKKSAETL ASANVYADSK
SSHTLKTANS YTDVTVSNST KKAIRESNQY TDHKFHQLDN RLDKLDTRVD KGLASSAALN
SLFQPYGVGK VNFTAGVGGY RSSQALAIGS GYRVNESVAL KAGVAYAGSS DVMYNASFNI
EW
