ID A0A3N4MAL9_9BACT Unreviewed; 87 AA.
AC A0A3N4MAL9;
DT 13-FEB-2019, integrated into UniProtKB/TrEMBL.
DT 13-FEB-2019, sequence version 1.
DT 24-JAN-2024, entry version 17.
DE RecName: Full=ATP synthase subunit c {ECO:0000256|HAMAP-Rule:MF_01396};
DE AltName: Full=ATP synthase F(0) sector subunit c {ECO:0000256|HAMAP-Rule:MF_01396};
DE AltName: Full=F-type ATPase subunit c {ECO:0000256|HAMAP-Rule:MF_01396};
DE Short=F-ATPase subunit c {ECO:0000256|HAMAP-Rule:MF_01396};
DE AltName: Full=Lipid-binding protein {ECO:0000256|HAMAP-Rule:MF_01396};
GN Name=atpE {ECO:0000256|HAMAP-Rule:MF_01396,
GN ECO:0000313|EMBL:RPD38766.1};
GN ORFNames=EG028_23975 {ECO:0000313|EMBL:RPD38766.1};
OS Chitinophaga barathri.
OC Bacteria; Bacteroidota; Chitinophagia; Chitinophagales; Chitinophagaceae;
OC Chitinophaga.
OX NCBI_TaxID=1647451 {ECO:0000313|EMBL:RPD38766.1, ECO:0000313|Proteomes:UP000279089};
RN [1] {ECO:0000313|Proteomes:UP000279089}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=YLT18 {ECO:0000313|Proteomes:UP000279089};
RA Zong Y.;
RT "Chitinophaga lutea sp.nov., isolate from arsenic contaminated soil.";
RL Submitted (NOV-2018) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: F(1)F(0) ATP synthase produces ATP from ADP in the presence
CC of a proton or sodium gradient. F-type ATPases consist of two
CC structural domains, F(1) containing the extramembraneous catalytic core
CC and F(0) containing the membrane proton channel, linked together by a
CC central stalk and a peripheral stalk. During catalysis, ATP synthesis
CC in the catalytic domain of F(1) is coupled via a rotary mechanism of
CC the central stalk subunits to proton translocation.
CC {ECO:0000256|ARBA:ARBA00025198, ECO:0000256|HAMAP-Rule:MF_01396}.
CC -!- FUNCTION: Key component of the F(0) channel; it plays a direct role in
CC translocation across the membrane. A homomeric c-ring of between 10-14
CC subunits forms the central stalk rotor element with the F(1) delta and
CC epsilon subunits. {ECO:0000256|HAMAP-Rule:MF_01396}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000256|HAMAP-Rule:MF_01396};
CC Multi-pass membrane protein {ECO:0000256|HAMAP-Rule:MF_01396}. Membrane
CC {ECO:0000256|ARBA:ARBA00004141}; Multi-pass membrane protein
CC {ECO:0000256|ARBA:ARBA00004141}.
CC -!- SIMILARITY: Belongs to the ATPase C chain family.
CC {ECO:0000256|ARBA:ARBA00006704, ECO:0000256|HAMAP-Rule:MF_01396}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:RPD38766.1}.
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DR EMBL; RMBX01000014; RPD38766.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A3N4MAL9; -.
DR OrthoDB; 5383454at2; -.
DR Proteomes; UP000279089; Unassembled WGS sequence.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0045263; C:proton-transporting ATP synthase complex, coupling factor F(o); IEA:UniProtKB-KW.
DR GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
DR GO; GO:0008289; F:lipid binding; IEA:UniProtKB-KW.
DR GO; GO:0046933; F:proton-transporting ATP synthase activity, rotational mechanism; IEA:UniProtKB-UniRule.
DR CDD; cd18121; ATP-synt_Fo_c; 1.
DR Gene3D; 1.20.20.10; F1F0 ATP synthase subunit C; 1.
DR HAMAP; MF_01396; ATP_synth_c_bact; 1.
DR InterPro; IPR005953; ATP_synth_csu_bac/chlpt.
DR InterPro; IPR000454; ATP_synth_F0_csu.
DR InterPro; IPR020537; ATP_synth_F0_csu_DDCD_BS.
DR InterPro; IPR038662; ATP_synth_F0_csu_sf.
DR InterPro; IPR002379; ATPase_proteolipid_c-like_dom.
DR InterPro; IPR035921; F/V-ATP_Csub_sf.
DR NCBIfam; TIGR01260; ATP_synt_c; 1.
DR PANTHER; PTHR10031; ATP SYNTHASE LIPID-BINDING PROTEIN, MITOCHONDRIAL; 1.
DR PANTHER; PTHR10031:SF0; ATPASE PROTEIN 9; 1.
DR Pfam; PF00137; ATP-synt_C; 1.
DR PRINTS; PR00124; ATPASEC.
DR SUPFAM; SSF81333; F1F0 ATP synthase subunit C; 1.
DR PROSITE; PS00605; ATPASE_C; 1.
PE 3: Inferred from homology;
KW ATP synthesis {ECO:0000256|ARBA:ARBA00023310, ECO:0000256|HAMAP-
KW Rule:MF_01396}; Cell membrane {ECO:0000256|HAMAP-Rule:MF_01396};
KW CF(0) {ECO:0000256|ARBA:ARBA00022547, ECO:0000256|HAMAP-Rule:MF_01396};
KW Hydrogen ion transport {ECO:0000256|ARBA:ARBA00022781, ECO:0000256|HAMAP-
KW Rule:MF_01396}; Hydrolase {ECO:0000313|EMBL:RPD38766.1};
KW Ion transport {ECO:0000256|ARBA:ARBA00023065, ECO:0000256|HAMAP-
KW Rule:MF_01396};
KW Lipid-binding {ECO:0000256|ARBA:ARBA00023121, ECO:0000256|HAMAP-
KW Rule:MF_01396};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|HAMAP-Rule:MF_01396};
KW Reference proteome {ECO:0000313|Proteomes:UP000279089};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|HAMAP-
KW Rule:MF_01396};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989, ECO:0000256|HAMAP-
KW Rule:MF_01396};
KW Transport {ECO:0000256|ARBA:ARBA00022448, ECO:0000256|HAMAP-Rule:MF_01396}.
FT TRANSMEM 23..42
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01396"
FT TRANSMEM 63..86
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01396"
FT DOMAIN 22..83
FT /note="V-ATPase proteolipid subunit C-like"
FT /evidence="ECO:0000259|Pfam:PF00137"
FT SITE 71
FT /note="Reversibly protonated during proton transport"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01396"
SQ SEQUENCE 87 AA; 8296 MW; BDE5E76E318561EC CRC64;
MALLTVLMQA TEAASTGLAQ AGGAIGAGIA AIAAGIGVGN IGKSALESIA RQPEAANDIR
ANMILAAALV EGVALFGVIA GLLAVVL
//