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1A91

SUBUNIT C OF THE F1FO ATP SYNTHASE OF ESCHERICHIA COLI; NMR, 10 STRUCTURES

Functional Information from GO Data
ChainGOidnamespacecontents
A0005886cellular_componentplasma membrane
A0006754biological_processATP biosynthetic process
A0006811biological_processmonoatomic ion transport
A0008289molecular_functionlipid binding
A0015078molecular_functionproton transmembrane transporter activity
A0015986biological_processproton motive force-driven ATP synthesis
A0016020cellular_componentmembrane
A0033177cellular_componentproton-transporting two-sector ATPase complex, proton-transporting domain
A0042777biological_processproton motive force-driven plasma membrane ATP synthesis
A0045259cellular_componentproton-transporting ATP synthase complex
A0045263cellular_componentproton-transporting ATP synthase complex, coupling factor F(o)
A0046933molecular_functionproton-transporting ATP synthase activity, rotational mechanism
A0046961molecular_functionproton-transporting ATPase activity, rotational mechanism
A1902600biological_processproton transmembrane transport
Functional Information from PROSITE/UniProt
site_idPS00605
Number of Residues22
DetailsATPASE_C ATP synthase c subunit signature. ARQPdliplLrTqfFIvmgLvD
ChainResidueDetails
AALA40-ASP61

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues14
DetailsTOPO_DOM: Periplasmic
ChainResidueDetails
AMET1-TYR10
AVAL74-ALA79

site_idSWS_FT_FI2
Number of Residues40
DetailsTRANSMEM: Helical
ChainResidueDetails
AMET11-LEU31
APHE53-TYR73

site_idSWS_FT_FI3
Number of Residues20
DetailsTOPO_DOM: Cytoplasmic
ChainResidueDetails
AGLY32-GLN52

site_idSWS_FT_FI4
Number of Residues1
DetailsSITE: Reversibly protonated during proton transport
ChainResidueDetails
AASP61

site_idSWS_FT_FI5
Number of Residues1
DetailsMOD_RES: N-formylmethionine => ECO:0000250
ChainResidueDetails
AMET1

Catalytic Information from CSA
site_idMCSA1
Number of Residues1
DetailsM-CSA 507
ChainResidueDetails
AASP61electrostatic stabiliser, proton acceptor, proton donor

218853

PDB entries from 2024-04-24

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