ID R5C739_9FIRM Unreviewed; 104 AA.
AC R5C739;
DT 24-JUL-2013, integrated into UniProtKB/TrEMBL.
DT 24-JUL-2013, sequence version 1.
DT 24-JAN-2024, entry version 49.
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 ORFNames=BN785_01008 {ECO:0000313|EMBL:CCX63660.1};
OS Firmicutes bacterium CAG:791.
OC Bacteria; Bacillota.
OX NCBI_TaxID=1262993 {ECO:0000313|EMBL:CCX63660.1, ECO:0000313|Proteomes:UP000018038};
RN [1] {ECO:0000313|EMBL:CCX63660.1, ECO:0000313|Proteomes:UP000018038}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MGS:791 {ECO:0000313|Proteomes:UP000018038};
RA Nielsen H.B., Almeida M., Juncker A.S., Rasmussen S., Li J., Sunagawa S.,
RA Plichta D., Gautier L., Le Chatelier E., Peletier E., Bonde I., Nielsen T.,
RA Manichanh C., Arumugam M., Batto J., Santos M.B.Q.D., Blom N., Borruel N.,
RA Burgdorf K.S., Boumezbeur F., Casellas F., Dore J., Guarner F., Hansen T.,
RA Hildebrand F., Kaas R.S., Kennedy S., Kristiansen K., Kultima J.R.,
RA Leonard P., Levenez F., Lund O., Moumen B., Le Paslier D., Pons N.,
RA Pedersen O., Prifti E., Qin J., Raes J., Tap J., Tims S., Ussery D.W.,
RA Yamada T., MetaHit consortium, Renault P., Sicheritz-Ponten T., Bork P.,
RA Wang J., Brunak S., Ehrlich S.D.;
RT "Dependencies among metagenomic species, viruses, plasmids and units of
RT genetic variation.";
RL Submitted (NOV-2012) 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:CCX63660.1}.
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DR EMBL; CAWT010000018; CCX63660.1; -; Genomic_DNA.
DR AlphaFoldDB; R5C739; -.
DR STRING; 1262993.BN785_01008; -.
DR Proteomes; UP000018038; 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:0008289; F:lipid binding; IEA:UniProtKB-KW.
DR GO; GO:0046933; F:proton-transporting ATP synthase activity, rotational mechanism; IEA:UniProtKB-UniRule.
DR CDD; cd18184; ATP-synt_Fo_c_NaATPase; 1.
DR Gene3D; 1.20.20.10; F1F0 ATP synthase subunit C; 2.
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 Pfam; PF00137; ATP-synt_C; 1.
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};
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:UP000018038};
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 12..32
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01396"
FT TRANSMEM 82..103
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01396"
FT DOMAIN 18..91
FT /note="V-ATPase proteolipid subunit C-like"
FT /evidence="ECO:0000259|Pfam:PF00137"
FT SITE 78
FT /note="Reversibly protonated during proton transport"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01396"
SQ SEQUENCE 104 AA; 10424 MW; C355CFE595F5BF50 CRC64;
MGDFQLLARG IALAGCGIGA GCALIAGIGP GIGEGNAVAK ALEAIGNAVA KAREGFGRQP
ECKSDVTSTM LLGCAIAETT GIYGFVTGLL LIFVAPGMFM NYLK
//
