ID A0A345Q6W5_9RHOB Unreviewed; 95 AA.
AC A0A345Q6W5;
DT 07-NOV-2018, integrated into UniProtKB/TrEMBL.
DT 07-NOV-2018, sequence version 1.
DT 24-JAN-2024, entry version 18.
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:AXI41052.1};
GN ORFNames=C1J02_03055 {ECO:0000313|EMBL:AXI41052.1};
OS Sulfitobacter sp. SK011.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC Roseobacteraceae; Sulfitobacter.
OX NCBI_TaxID=1389004 {ECO:0000313|EMBL:AXI41052.1, ECO:0000313|Proteomes:UP000253968};
RN [1] {ECO:0000313|EMBL:AXI41052.1, ECO:0000313|Proteomes:UP000253968}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SK011 {ECO:0000313|EMBL:AXI41052.1,
RC ECO:0000313|Proteomes:UP000253968};
RA Pohlner M., Engelen B., Bunk B.;
RT "Comparative analysis of Sulfitobacter strains from the North Sea.";
RL Submitted (JAN-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. {ECO:0000256|HAMAP-
CC 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 ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; CP025803; AXI41052.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A345Q6W5; -.
DR OrthoDB; 5296711at2; -.
DR Proteomes; UP000253968; Chromosome.
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: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; 1.20.120.610; lithium bound rotor ring of v- atpase; 1.
DR HAMAP; MF_01396; ATP_synth_c_bact; 1.
DR InterPro; IPR017708; Alt_ATP_synth_F0_Csu.
DR InterPro; IPR005953; ATP_synth_csu_bac/chlpt.
DR InterPro; IPR000454; ATP_synth_F0_csu.
DR InterPro; IPR002379; ATPase_proteolipid_c-like_dom.
DR InterPro; IPR035921; F/V-ATP_Csub_sf.
DR NCBIfam; TIGR03322; alt_F1F0_F0_C; 1.
DR NCBIfam; TIGR01260; ATP_synt_c; 1.
DR Pfam; PF00137; ATP-synt_C; 1.
DR PRINTS; PR00124; ATPASEC.
DR SUPFAM; SSF81333; F1F0 ATP synthase subunit 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};
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:UP000253968};
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 6..28
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01396"
FT TRANSMEM 55..79
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01396"
FT DOMAIN 13..76
FT /note="V-ATPase proteolipid subunit C-like"
FT /evidence="ECO:0000259|Pfam:PF00137"
FT SITE 63
FT /note="Reversibly protonated during proton transport"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01396"
SQ SEQUENCE 95 AA; 9517 MW; E33E52E2F49FA5D0 CRC64;
MTDLGIIAAI SIFTAGLTVS FGAIGPALGE GRAAATALSA IAQQPDAAPN ISRTLFVSLA
MIESTAIYCF VVAMILIFAN PFWNTAVAAA KAAGG
//