##gff-version 3
P0ADY1	UniProtKB	Chain	1	623	.	.	.	ID=PRO_0000193423;Note=Periplasmic chaperone PpiD	
P0ADY1	UniProtKB	Topological domain	1	15	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000269,ECO:0000305;evidence=ECO:0000269|PubMed:21210718,ECO:0000305|PubMed:9670013;Dbxref=PMID:21210718,PMID:9670013	
P0ADY1	UniProtKB	Transmembrane	16	36	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
P0ADY1	UniProtKB	Topological domain	37	623	.	.	.	Note=Periplasmic;Ontology_term=ECO:0000269,ECO:0000305;evidence=ECO:0000269|PubMed:21210718,ECO:0000305|PubMed:9670013;Dbxref=PMID:21210718,PMID:9670013	
P0ADY1	UniProtKB	Domain	266	355	.	.	.	Note=PpiC;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00278	
P0ADY1	UniProtKB	Mutagenesis	312	312	.	.	.	Note=Cannot complement a surA null mutant or reduce the htrA-lacZ activity induced by periplasmic stresses. G->A%2CR;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:9670013;Dbxref=PMID:9670013	
P0ADY1	UniProtKB	Mutagenesis	313	313	.	.	.	Note=Cannot complement a surA null mutant or reduce the htrA-lacZ activity induced by periplasmic stresses. G->A%2CR;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:9670013;Dbxref=PMID:9670013	
P0ADY1	UniProtKB	Mutagenesis	347	347	.	.	.	Note=Can complement the growth defect of surA skp double deletion mutant. Has originally been reported to eliminate PPIase activity and to result in the loss of its reported surA complementing function. G->A;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:20920237,ECO:0000269|PubMed:9670013;Dbxref=PMID:20920237,PMID:9670013	
P0ADY1	UniProtKB	Mutagenesis	350	350	.	.	.	Note=Can complement the growth defect of surA skp double deletion mutant. Has originally been reported to eliminate PPIase activity and to result in the loss of its reported surA complementing function. I->A;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:20920237,ECO:0000269|PubMed:9670013;Dbxref=PMID:20920237,PMID:9670013	
P0ADY1	UniProtKB	Mutagenesis	350	350	.	.	.	Note=Cannot complement a surA null mutant or reduce the htrA-lacZ activity induced by periplasmic stresses. I->F;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:9670013;Dbxref=PMID:9670013	
P0ADY1	UniProtKB	Beta strand	268	278	.	.	.	Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:2KGJ	
P0ADY1	UniProtKB	Helix	279	291	.	.	.	Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:2KGJ	
P0ADY1	UniProtKB	Helix	295	301	.	.	.	Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:2KGJ	
P0ADY1	UniProtKB	Helix	306	309	.	.	.	Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:2KGJ	
P0ADY1	UniProtKB	Turn	310	312	.	.	.	Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:2KGJ	
P0ADY1	UniProtKB	Beta strand	313	319	.	.	.	Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:2KGJ	
P0ADY1	UniProtKB	Helix	325	328	.	.	.	Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:2KGJ	
P0ADY1	UniProtKB	Beta strand	338	344	.	.	.	Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:2KGJ	
P0ADY1	UniProtKB	Beta strand	347	357	.	.	.	Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:2KGJ