##gff-version 3
P0C0S1	UniProtKB	Chain	1	286	.	.	.	ID=PRO_0000110238;Note=Small-conductance mechanosensitive channel	
P0C0S1	UniProtKB	Topological domain	1	30	.	.	.	Note=Periplasmic;Ontology_term=ECO:0000305;evidence=ECO:0000305|PubMed:15919996;Dbxref=PMID:15919996	
P0C0S1	UniProtKB	Transmembrane	31	52	.	.	.	Note=Helical;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:12446901,ECO:0000269|PubMed:26551077;Dbxref=PMID:12446901,PMID:26551077	
P0C0S1	UniProtKB	Topological domain	53	67	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000305;evidence=ECO:0000305|PubMed:15919996;Dbxref=PMID:15919996	
P0C0S1	UniProtKB	Transmembrane	68	88	.	.	.	Note=Helical;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:12446901,ECO:0000269|PubMed:26551077;Dbxref=PMID:12446901,PMID:26551077	
P0C0S1	UniProtKB	Topological domain	89	90	.	.	.	Note=Periplasmic;Ontology_term=ECO:0000305;evidence=ECO:0000305|PubMed:15919996;Dbxref=PMID:15919996	
P0C0S1	UniProtKB	Transmembrane	91	111	.	.	.	Note=Helical;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:12446901,ECO:0000269|PubMed:26551077;Dbxref=PMID:12446901,PMID:26551077	
P0C0S1	UniProtKB	Topological domain	112	286	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000305;evidence=ECO:0000305|PubMed:15919996;Dbxref=PMID:15919996	
P0C0S1	UniProtKB	Mutagenesis	40	40	.	.	.	Note=No detectable phenotype. V->C%2CG%2CN;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:12015316;Dbxref=PMID:12015316	
P0C0S1	UniProtKB	Mutagenesis	40	40	.	.	.	Note=Normal growth stops%2C without cell death%2C due to increased membrane permeability to potassium ions and protons (permeability tested only for D substitutions). V->D%2CK;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:12015316;Dbxref=PMID:12015316	
P0C0S1	UniProtKB	Mutagenesis	58	58	.	.	.	Note=Readily forms disulfide bonds with cross-linkers%2C suggesting that individual S-58 are only 3 Angstroms apart in the closed state%2C versus 33 Angstroms apart in the open state crystal structure. S->C;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:12767977;Dbxref=PMID:12767977	
P0C0S1	UniProtKB	Mutagenesis	158	158	.	.	.	Note=Decreased conductance%2C due to decreased diameter of the channel portal. A->F;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:23074248;Dbxref=PMID:23074248	
P0C0S1	UniProtKB	Mutagenesis	266	286	.	.	.	Note=Normal levels of channels are expressed%3B they recover more slowly than wild-type cells after desensitization. ISFPYPQMDVNFKRVKEDKAA->HHHHHHLE;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:15665866;Dbxref=PMID:15665866	
P0C0S1	UniProtKB	Mutagenesis	266	286	.	.	.	Note=Fewer channels present in the membrane%2C they require slightly more pressure to open and do not recover after desensitization. ISFPYPQMDVNFKRVKEDKAA->LE;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:15665866;Dbxref=PMID:15665866	
P0C0S1	UniProtKB	Mutagenesis	267	267	.	.	.	Note=Provides biochemical evidence for heptameric structure upon cross-linking. S->C;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:12767977;Dbxref=PMID:12767977	
P0C0S1	UniProtKB	Helix	2	6	.	.	.	Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:6PWN	
P0C0S1	UniProtKB	Turn	16	20	.	.	.	Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:6PWN	
P0C0S1	UniProtKB	Helix	23	57	.	.	.	Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:6RLD	
P0C0S1	UniProtKB	Beta strand	58	60	.	.	.	Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:6PWN	
P0C0S1	UniProtKB	Helix	63	89	.	.	.	Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:6RLD	
P0C0S1	UniProtKB	Helix	94	110	.	.	.	Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:6RLD	
P0C0S1	UniProtKB	Helix	112	126	.	.	.	Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:6RLD	
P0C0S1	UniProtKB	Beta strand	135	140	.	.	.	Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:6RLD	
P0C0S1	UniProtKB	Beta strand	142	148	.	.	.	Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:6RLD	
P0C0S1	UniProtKB	Beta strand	150	156	.	.	.	Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:6RLD	
P0C0S1	UniProtKB	Beta strand	158	160	.	.	.	Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:6RLD	
P0C0S1	UniProtKB	Beta strand	162	166	.	.	.	Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:6RLD	
P0C0S1	UniProtKB	Helix	167	171	.	.	.	Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:6RLD	
P0C0S1	UniProtKB	Beta strand	175	192	.	.	.	Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:6RLD	
P0C0S1	UniProtKB	Beta strand	194	196	.	.	.	Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:6PWO	
P0C0S1	UniProtKB	Helix	198	210	.	.	.	Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:6RLD	
P0C0S1	UniProtKB	Beta strand	213	215	.	.	.	Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:6PWN	
P0C0S1	UniProtKB	Beta strand	217	219	.	.	.	Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:6RLD	
P0C0S1	UniProtKB	Beta strand	221	228	.	.	.	Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:6RLD	
P0C0S1	UniProtKB	Beta strand	230	242	.	.	.	Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:6RLD	
P0C0S1	UniProtKB	Turn	243	245	.	.	.	Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:5AJI	
P0C0S1	UniProtKB	Helix	246	263	.	.	.	Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:6RLD	
P0C0S1	UniProtKB	Beta strand	272	278	.	.	.	Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:6RLD