ATP6_CAEBR
ID ATP6_CAEBR Reviewed; 199 AA.
AC Q8HEC5; B1PE36; B1PE48; B1PED2; B1PEF6; B1PEV0;
DT 21-JUN-2005, integrated into UniProtKB/Swiss-Prot.
DT 13-OCT-2009, sequence version 2.
DT 03-AUG-2022, entry version 81.
DE RecName: Full=ATP synthase subunit a;
DE AltName: Full=F-ATPase protein 6;
GN Name=atp6;
OS Caenorhabditis briggsae.
OG Mitochondrion.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC Caenorhabditis.
OX NCBI_TaxID=6238;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANTS GLY-51; LEU-53; TRP-66;
RP PHE-86; ILE-90; ALA-98 AND ILE-168.
RC STRAIN=BW287, ED3032, ED3033, ED3034, ED3035, ED3036, ED3037, ED3083,
RC ED3092, ED3101, EG4181, EG4207A, HK104, HK105, JU403, JU439, JU516, JU725,
RC JU726, JU793, PB800, PB826, and VT847;
RX PubMed=18302772; DOI=10.1186/1471-2148-8-62;
RA Howe D.K., Denver D.R.;
RT "Muller's Ratchet and compensatory mutation in Caenorhabditis briggsae
RT mitochondrial genome evolution.";
RL BMC Evol. Biol. 8:62-62(2008).
RN [2]
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).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-86.
RC STRAIN=PB800;
RX PubMed=12644560; DOI=10.1093/molbev/msg044;
RA Denver D.R., Morris K., Thomas W.K.;
RT "Phylogenetics in Caenorhabditis elegans: an analysis of divergence and
RT outcrossing.";
RL Mol. Biol. Evol. 20:393-400(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. Key component of the
CC proton channel; it may play a direct role in the translocation of
CC protons across the membrane.
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.
CC -!- SUBCELLULAR LOCATION: Mitochondrion inner membrane; Multi-pass membrane
CC protein.
CC -!- SIMILARITY: Belongs to the ATPase A chain family. {ECO:0000305}.
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DR EMBL; EU407781; ACB06103.1; -; Genomic_DNA.
DR EMBL; EU407782; ACB06115.1; -; Genomic_DNA.
DR EMBL; EU407783; ACB06127.1; -; Genomic_DNA.
DR EMBL; EU407784; ACB06139.1; -; Genomic_DNA.
DR EMBL; EU407785; ACB06151.1; -; Genomic_DNA.
DR EMBL; EU407786; ACB06163.1; -; Genomic_DNA.
DR EMBL; EU407787; ACB06175.1; -; Genomic_DNA.
DR EMBL; EU407788; ACB06187.1; -; Genomic_DNA.
DR EMBL; EU407789; ACB06199.1; -; Genomic_DNA.
DR EMBL; EU407790; ACB06211.1; -; Genomic_DNA.
DR EMBL; EU407791; ACB06223.1; -; Genomic_DNA.
DR EMBL; EU407792; ACB06235.1; -; Genomic_DNA.
DR EMBL; EU407793; ACB06247.1; -; Genomic_DNA.
DR EMBL; EU407794; ACB06259.1; -; Genomic_DNA.
DR EMBL; EU407795; ACB06271.1; -; Genomic_DNA.
DR EMBL; EU407796; ACB06283.1; -; Genomic_DNA.
DR EMBL; EU407797; ACB06295.1; -; Genomic_DNA.
DR EMBL; EU407798; ACB06307.1; -; Genomic_DNA.
DR EMBL; EU407799; ACB06319.1; -; Genomic_DNA.
DR EMBL; EU407800; ACB06331.1; -; Genomic_DNA.
DR EMBL; EU407801; ACB06343.1; -; Genomic_DNA.
DR EMBL; EU407802; ACB06355.1; -; Genomic_DNA.
DR EMBL; EU407803; ACB06367.1; -; Genomic_DNA.
DR EMBL; AC186293; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AY171101; AAO13508.1; -; Genomic_DNA.
DR RefSeq; YP_001504336.1; NC_009885.1.
DR AlphaFoldDB; Q8HEC5; -.
DR GeneID; 5666628; -.
DR KEGG; cbr:ATP6; -.
DR CTD; 4508; -.
DR InParanoid; Q8HEC5; -.
DR Proteomes; UP000008549; Mitochondrion.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005743; C:mitochondrial inner membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0045263; C:proton-transporting ATP synthase complex, coupling factor F(o); 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; 1.20.120.220; -; 1.
DR InterPro; IPR000568; ATP_synth_F0_asu.
DR InterPro; IPR023011; ATP_synth_F0_asu_AS.
DR InterPro; IPR045083; ATP_synth_F0_asu_bact/mt.
DR InterPro; IPR035908; F0_ATP_A_sf.
DR PANTHER; PTHR11410; PTHR11410; 1.
DR Pfam; PF00119; ATP-synt_A; 1.
DR SUPFAM; SSF81336; SSF81336; 1.
DR PROSITE; PS00449; ATPASE_A; 1.
PE 3: Inferred from homology;
KW ATP synthesis; CF(0); Hydrogen ion transport; Ion transport; Membrane;
KW Mitochondrion; Mitochondrion inner membrane; Reference proteome;
KW Transmembrane; Transmembrane helix; Transport.
FT CHAIN 1..199
FT /note="ATP synthase subunit a"
FT /id="PRO_0000082100"
FT TRANSMEM 2..22
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 53..73
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 80..100
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 141..161
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 169..189
FT /note="Helical"
FT /evidence="ECO:0000255"
FT VARIANT 51
FT /note="S -> G (in strain: VT847)"
FT /evidence="ECO:0000269|PubMed:18302772"
FT VARIANT 53
FT /note="V -> L (in strain: VT847)"
FT /evidence="ECO:0000269|PubMed:18302772"
FT VARIANT 66
FT /note="C -> W (in strain: VT847)"
FT /evidence="ECO:0000269|PubMed:18302772"
FT VARIANT 86
FT /note="V -> F (in strain: ED3032 and ED3036)"
FT /evidence="ECO:0000269|PubMed:18302772"
FT VARIANT 90
FT /note="V -> I (in strain: VT847)"
FT /evidence="ECO:0000269|PubMed:18302772"
FT VARIANT 98
FT /note="T -> A (in strain: EG4181)"
FT /evidence="ECO:0000269|PubMed:18302772"
FT VARIANT 168
FT /note="V -> I (in strain: ED3092 and ED3101)"
FT /evidence="ECO:0000269|PubMed:18302772"
FT CONFLICT 11
FT /note="M -> I (in Ref. 2; AC186293)"
FT /evidence="ECO:0000305"
FT CONFLICT 43..45
FT /note="SYS -> RYR (in Ref. 2; AC186293)"
FT /evidence="ECO:0000305"
FT CONFLICT 80
FT /note="M -> I (in Ref. 2; AC186293)"
FT /evidence="ECO:0000305"
FT CONFLICT 102
FT /note="S -> R (in Ref. 2; AC186293)"
FT /evidence="ECO:0000305"
FT CONFLICT 109
FT /note="M -> I (in Ref. 2; AC186293)"
FT /evidence="ECO:0000305"
FT CONFLICT 121..122
FT /note="SM -> RI (in Ref. 2; AC186293)"
FT /evidence="ECO:0000305"
FT CONFLICT 129
FT /note="S -> R (in Ref. 2; AC186293)"
FT /evidence="ECO:0000305"
FT CONFLICT 152..153
FT /note="SM -> RI (in Ref. 2; AC186293)"
FT /evidence="ECO:0000305"
FT CONFLICT 162
FT /note="S -> R (in Ref. 2; AC186293)"
FT /evidence="ECO:0000305"
FT CONFLICT 177
FT /note="M -> I (in Ref. 2; AC186293)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 199 AA; 23045 MW; 31F2715827AA44C1 CRC64;
MNQVYFLDIF MFVFVLQFLF YFKEGMLNTL VKKFLNSLVG VFSYSNTLPL SSVISVFTFI
ILLTCCFGGY FTYSFCPCGM VEFTFVYAAV AWLSTLLTFI SSEKFSVYMS KPGDTYLKTL
SMLLVEIVSE FSRPLALTVR LTVNIMVGHL ISMMLYQGLE LSMGDQYVWL SIFAIMMECF
VFFIQSYIFS RLIFLYLNE
