AT5G_CAEBR
ID AT5G_CAEBR Reviewed; 116 AA.
AC A8XDX2;
DT 05-OCT-2010, integrated into UniProtKB/Swiss-Prot.
DT 15-JAN-2008, sequence version 1.
DT 03-AUG-2022, entry version 73.
DE RecName: Full=ATP synthase lipid-binding protein, mitochondrial;
DE AltName: Full=ATPase protein 9;
DE AltName: Full=ATPase subunit c;
DE Flags: Precursor;
GN ORFNames=CBG11706;
OS Caenorhabditis briggsae.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC Caenorhabditis.
OX NCBI_TaxID=6238;
RN [1] {ECO:0000312|EMBL:CAP30867.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AF16;
RX PubMed=14624247; DOI=10.1371/journal.pbio.0000045;
RA Stein L.D., Bao Z., Blasiar D., Blumenthal T., Brent M.R., Chen N.,
RA Chinwalla A., Clarke L., Clee C., Coghlan A., Coulson A., D'Eustachio P.,
RA Fitch D.H.A., Fulton L.A., Fulton R.E., Griffiths-Jones S., Harris T.W.,
RA Hillier L.W., Kamath R., Kuwabara P.E., Mardis E.R., Marra M.A.,
RA Miner T.L., Minx P., Mullikin J.C., Plumb R.W., Rogers J., Schein J.E.,
RA Sohrmann M., Spieth J., Stajich J.E., Wei C., Willey D., Wilson R.K.,
RA Durbin R.M., Waterston R.H.;
RT "The genome sequence of Caenorhabditis briggsae: a platform for comparative
RT genomics.";
RL PLoS Biol. 1:166-192(2003).
CC -!- FUNCTION: Mitochondrial membrane ATP synthase (F(1)F(0) ATP synthase or
CC Complex V) produces ATP from ADP in the presence of a proton gradient
CC across the membrane which is generated by electron transport complexes
CC of the respiratory chain. F-type ATPases consist of two structural
CC domains, F(1) - containing the extramembraneous catalytic core and F(0)
CC - containing the membrane proton channel, linked together by a central
CC stalk and a peripheral stalk. During catalysis, ATP synthesis in the
CC catalytic domain of F(1) is coupled via a rotary mechanism of the
CC central stalk subunits to proton translocation. Part of the complex
CC F(0) domain. A homomeric c-ring of probably 10 subunits is part of the
CC complex rotary element (By similarity). {ECO:0000250|UniProtKB:Q06645}.
CC -!- SUBUNIT: F-type ATPases have 2 components, CF(1) - the catalytic core
CC - and CF(0) - the membrane proton channel. CF(1) has five subunits:
CC alpha(3), beta(3), gamma(1), delta(1), epsilon(1). CF(0) has three main
CC subunits: a, b and c (By similarity). {ECO:0000250|UniProtKB:Q06645}.
CC -!- SUBCELLULAR LOCATION: Mitochondrion membrane
CC {ECO:0000250|UniProtKB:Q06645}; Multi-pass membrane protein
CC {ECO:0000250|UniProtKB:Q06645}.
CC -!- PTM: Trimethylated by ATPSCKMT at Lys-84. Methylation may be required
CC for proper incorporation of the C subunit into the ATP synthase complex
CC and mitochondrial respiration. {ECO:0000250|UniProtKB:P05496}.
CC -!- SIMILARITY: Belongs to the ATPase C chain family. {ECO:0000255}.
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DR EMBL; HE601289; CAP30867.1; -; Genomic_DNA.
DR RefSeq; XP_002640963.1; XM_002640917.1.
DR AlphaFoldDB; A8XDX2; -.
DR SMR; A8XDX2; -.
DR STRING; 6238.CBG11706; -.
DR EnsemblMetazoa; CBG11706.1; CBG11706.1; WBGene00032789.
DR GeneID; 8582957; -.
DR KEGG; cbr:CBG_11706; -.
DR CTD; 8582957; -.
DR WormBase; CBG11706; CBP02857; WBGene00032789; -.
DR eggNOG; KOG3025; Eukaryota.
DR HOGENOM; CLU_116822_2_0_1; -.
DR InParanoid; A8XDX2; -.
DR OMA; ACHRPRC; -.
DR OrthoDB; 1564365at2759; -.
DR Proteomes; UP000008549; Chromosome III.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0000276; C:mitochondrial proton-transporting ATP synthase complex, coupling factor F(o); IBA:GO_Central.
DR GO; GO:0045263; C:proton-transporting ATP synthase complex, coupling factor F(o); IBA:GO_Central.
DR GO; GO:0008289; F:lipid binding; IEA:UniProtKB-KW.
DR GO; GO:0015078; F:proton transmembrane transporter activity; IEA:InterPro.
DR GO; GO:0015986; P:proton motive force-driven ATP synthesis; IBA:GO_Central.
DR Gene3D; 1.20.20.10; -; 1.
DR HAMAP; MF_01396; ATP_synth_c_bact; 1.
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 PANTHER; PTHR10031; PTHR10031; 1.
DR Pfam; PF00137; ATP-synt_C; 1.
DR PRINTS; PR00124; ATPASEC.
DR SUPFAM; SSF81333; SSF81333; 1.
DR PROSITE; PS00605; ATPASE_C; 1.
PE 3: Inferred from homology;
KW CF(0); Hydrogen ion transport; Ion transport; Lipid-binding; Membrane;
KW Methylation; Mitochondrion; Reference proteome; Transit peptide;
KW Transmembrane; Transmembrane helix; Transport.
FT TRANSIT 1..24
FT /note="Mitochondrion"
FT /evidence="ECO:0000255"
FT CHAIN 25..116
FT /note="ATP synthase lipid-binding protein, mitochondrial"
FT /id="PRO_0000399029"
FT TRANSMEM 57..77
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 92..112
FT /note="Helical"
FT /evidence="ECO:0000255"
FT SITE 99
FT /note="Reversibly protonated during proton transport"
FT /evidence="ECO:0000250|UniProtKB:P00845"
FT MOD_RES 84
FT /note="N6,N6,N6-trimethyllysine"
FT /evidence="ECO:0000250|UniProtKB:P05496"
SQ SEQUENCE 116 AA; 12108 MW; 857C762174A71F6D CRC64;
MYCQRLALPL TRSLLASRAP LALRMENAVA ARMISTTVAR KDIDSAAKYI GAGAATVGVA
GSGAGIGNVF GALVIGYARN PSLKQQLFSY AILGFALSEA MGLFCLTMGF MILFAL
