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Database: UniProt
Entry: A0A426FLU7_9BURK
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ID   A0A426FLU7_9BURK        Unreviewed;        79 AA.
AC   A0A426FLU7;
DT   08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT   08-MAY-2019, sequence version 1.
DT   13-SEP-2023, entry version 15.
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=EHV23_09690 {ECO:0000313|EMBL:RRN43689.1};
OS   Lautropia dentalis.
OC   Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC   Burkholderiaceae; Lautropia.
OX   NCBI_TaxID=2490857 {ECO:0000313|EMBL:RRN43689.1, ECO:0000313|Proteomes:UP000270261};
RN   [1] {ECO:0000313|EMBL:RRN43689.1, ECO:0000313|Proteomes:UP000270261}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=KCOM 2505 {ECO:0000313|EMBL:RRN43689.1,
RC   ECO:0000313|Proteomes:UP000270261};
RA   Kook J.-K., Park S.-N., Lim Y.K.;
RT   "Genome sequencing of Lautropia sp. KCOM 2505 (= ChDC F240).";
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:RRN43689.1}.
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DR   EMBL; RRUE01000002; RRN43689.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A426FLU7; -.
DR   OrthoDB; 9811659at2; -.
DR   Proteomes; UP000270261; 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; cd18185; ATP-synt_Fo_c_ATPE; 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   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:RRN43689.1};
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   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..30
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01396"
FT   TRANSMEM        51..75
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01396"
FT   DOMAIN          9..71
FT                   /note="V-ATPase proteolipid subunit C-like"
FT                   /evidence="ECO:0000259|Pfam:PF00137"
FT   SITE            59
FT                   /note="Reversibly protonated during proton transport"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01396"
SQ   SEQUENCE   79 AA;  7922 MW;  CBF43140C535123A CRC64;
     MTNAAYVAIA CGIIVGLGAL GASIGIALMG GKFLEGSARQ PELMGKLQTS MFVLAGLIDA
     AFLIGVGVAM LFAFANPFA
//
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