(data stored in ACNUC9435 zone)

HOGENOM: YEPSE1_1_PE13

ID   YEPSE1_1_PE13                        STANDARD;      PRT;   432 AA.
AC   YEPSE1_1_PE13; P10858; Q663F4;
DT   00-JAN-0000 (Rel. 1, Created)
DT   00-JAN-0000 (Rel. 2, Last sequence update)
DT   00-JAN-0000 (Rel. 3, Last annotation update)
DE   RecName: Full=Adhesin yadA;Flags: Precursor; (YEPSE1_1.PE13).
GN   Name=yadA; Synonyms=invA, yop1, yopA; OrderedLocusNames=pYV0013;
OS   YERSINIA PSEUDOTUBERCULOSIS IP 32953.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales;
OC   Enterobacteriaceae; Yersinia.
OX   NCBI_TaxID=273123;
RN   [0]
RP   -.;
RG   -.;
RL   -.;
CC   -!- SEQ. DATA ORIGIN: Translated from the HOGENOM CDS YEPSE1_1.PE13.
CC       Yersinia pseudotuberculosis IP 32953 plasmid pYV, complete sequence.
CC       sequence.
CC   -!- ANNOTATIONS ORIGIN:YADA_YERPS
CC   -!- FUNCTION: Collagen-binding outer membrane protein forming a
CC       fibrillar matrix on the bacterial cell surface. Promotes
CC       attachment to eukaryotic cells and after invasion, is the major
CC       adhesin in infected tissue. Constitutes an alternative uptake
CC       pathway under conditions in which invasin synthesis is repressed.
CC   -!- SUBUNIT: Homotrimer.
CC   -!- SUBCELLULAR LOCATION: Cell outer membrane.
CC   -!- INDUCTION: Induced at 37 degrees Celsius by the temperature-
CC       dependent transcriptional activator lcrF (virF).
CC   -!- SIMILARITY: Belongs to the autotransporter-2 (TC 1.B.40) /
CC       oligomeric coiled-coil adhesin (Oca) family.
CC   -!- GENE_FAMILY: HOG000266859 [ FAMILY / ALN / TREE ]
DR   UniProtKB/Swiss-Prot; P10858; Q663F4; -.
DR   EMBL; X13883; CAA32088.1; -; Genomic_DNA.
DR   EMBL; BX936399; CAF25356.1; -; Genomic_DNA.
DR   PIR; S04534; S04534.
DR   RefSeq; YP_068426.1; NC_006153.2.
DR   ProteinModelPortal; P10858; -.
DR   SMR; P10858; 36-251.
DR   GeneID; 2952906; -.
DR   GenomeReviews; BX936399_GR; pYV0013.
DR   KEGG; yps:pYV0013; -.
DR   NMPDR; fig|273123.1.peg.13; -.
DR   OMA; AFANNDE; -.
DR   ProtClustDB; CLSK687512; -.
DR   BioCyc; YPSE273123:PYV0013-MON; -.
DR   GO; GO:0009279; C:cell outer membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0016021; C:integral to membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005886; C:plasma 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:0009405; P:pathogenesis; IEA:UniProtKB-KW.
DR   InterPro; IPR008640; Hep_Hag.
DR   InterPro; IPR008635; HIM.
DR   InterPro; IPR008126; OM_adhesion_Yersinia.
DR   InterPro; IPR005594; YadA_C.
DR   Pfam; PF05658; Hep_Hag; 2.
DR   Pfam; PF05662; HIM; 1.
DR   Pfam; PF03895; YadA; 1.
DR   PRINTS; PR01756; OMADHESIN.
DR   HOGENOMDNA; YEPSE1_1.PE13; -.
KW   hypothetical protein;
KW   Cell adhesion; Cell membrane; Cell outer membrane; Coiled coil;
KW   Complete proteome; Membrane; Plasmid; Signal; Transmembrane;
KW   Transmembrane beta strand; Virulence.
SQ   SEQUENCE   432 AA;  UNKNOWN MW;  UNKNOWN CRC64;
     MTKDFKISVS AALISALFSS PYAFAEEPED GNDGIPRLSA VQISPNVDPK LGVGLYPAKP
     ILRQENPKLP PRGPQGPEKK RARLAEAIQP QVLGGLDARA KGIHSIAIGA TAEAAKPAAV
     AVGAGSIATG VNSVAIGPLS KALGDSAVTY GASSTAQKDG VAIGARASAS DTGVAVGFNS
     KVDAQNSVAI GHSSHVAADH GYSIAIGDLS KTDRENSVSI GHESLNRQLT HLAAGTKDND
     AVNVAQLKKE MAETLENARK ETLAQSNDVL DAAKKHSNSV ARTTLETAEE HANKKSAEAL
     VSAKVYADSN SSHTLKTANS YTDVTVSSST KKAISESNQY TDHKFSQLDN RLDKLDKRVD
     KGLASSAALN SLFQPYGVGK VNFTAGVGGY RSSQALAIGS GYRVNESVAL KAGVAYAGSS
     NVMYNASFNI EW
//

If you have problems or comments...

PBIL Back to PBIL home page