1IJP
Solution Structure of Ala20Pro/Pro64Ala substituted subunit c of Escherichia coli ATP synthase
Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0005886 | cellular_component | plasma membrane |
A | 0006754 | biological_process | ATP biosynthetic process |
A | 0006811 | biological_process | monoatomic ion transport |
A | 0008289 | molecular_function | lipid binding |
A | 0015078 | molecular_function | proton transmembrane transporter activity |
A | 0015986 | biological_process | proton motive force-driven ATP synthesis |
A | 0016020 | cellular_component | membrane |
A | 0033177 | cellular_component | proton-transporting two-sector ATPase complex, proton-transporting domain |
A | 0042777 | biological_process | proton motive force-driven plasma membrane ATP synthesis |
A | 0045259 | cellular_component | proton-transporting ATP synthase complex |
A | 0046933 | molecular_function | proton-transporting ATP synthase activity, rotational mechanism |
A | 0046961 | molecular_function | proton-transporting ATPase activity, rotational mechanism |
A | 1902600 | biological_process | proton transmembrane transport |
Functional Information from PROSITE/UniProt
site_id | PS00605 |
Number of Residues | 22 |
Details | ATPASE_C ATP synthase c subunit signature. ARQPdliplLrTqfFIvmgLvD |
Chain | Residue | Details |
A | ALA40-ASP61 |
Functional Information from SwissProt/UniProt
site_id | SWS_FT_FI1 |
Number of Residues | 14 |
Details | Topological domain: {"description":"Periplasmic"} |
Chain | Residue | Details |
site_id | SWS_FT_FI2 |
Number of Residues | 40 |
Details | Transmembrane: {"description":"Helical"} |
Chain | Residue | Details |
site_id | SWS_FT_FI3 |
Number of Residues | 20 |
Details | Topological domain: {"description":"Cytoplasmic"} |
Chain | Residue | Details |
site_id | SWS_FT_FI4 |
Number of Residues | 1 |
Details | Site: {"description":"Reversibly protonated during proton transport"} |
Chain | Residue | Details |
site_id | SWS_FT_FI5 |
Number of Residues | 1 |
Details | Modified residue: {"description":"N-formylmethionine","evidences":[{"evidenceCode":"ECO:0000250"}]} |
Chain | Residue | Details |
Catalytic Information from CSA
site_id | CSA1 |
Number of Residues | 1 |
Details | Annotated By Reference To The Literature 1c17 |
Chain | Residue | Details |
A | ASP61 |
site_id | MCSA1 |
Number of Residues | 1 |
Details | M-CSA 507 |
Chain | Residue | Details |
A | ASP61 | electrostatic stabiliser, proton acceptor, proton donor |