ATPA_CAEEL
ID ATPA_CAEEL Reviewed; 538 AA.
AC Q9XXK1; Q7K7K6; Q7YTU5; Q7YTU6;
DT 13-JUN-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1999, sequence version 1.
DT 03-AUG-2022, entry version 156.
DE RecName: Full=ATP synthase subunit alpha, mitochondrial;
DE AltName: Full=ATP synthase subunit atp-1 {ECO:0000312|WormBase:H28O16.1a};
DE Flags: Precursor;
GN Name=atp-1 {ECO:0000312|WormBase:H28O16.1a};
GN ORFNames=H28O16.1 {ECO:0000312|WormBase:H28O16.1a};
OS Caenorhabditis elegans.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC Caenorhabditis.
OX NCBI_TaxID=6239;
RN [1] {ECO:0000312|EMBL:CAA19429.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Bristol N2;
RX PubMed=9851916; DOI=10.1126/science.282.5396.2012;
RG The C. elegans sequencing consortium;
RT "Genome sequence of the nematode C. elegans: a platform for investigating
RT biology.";
RL Science 282:2012-2018(1998).
RN [2] {ECO:0000305, ECO:0000312|EMBL:CAA19429.1}
RP PROTEIN SEQUENCE OF 59-68; 119-134; 168-189; 193-199 AND 204-215 (ISOFORMS
RP A/D), AND IDENTIFICATION BY MASS SPECTROMETRY.
RA Bienvenut W.V.;
RL Submitted (MAR-2006) to UniProtKB.
RN [3]
RP FUNCTION, DISRUPTION PHENOTYPE, IDENTIFICATION BY MASS SPECTROMETRY,
RP SUBCELLULAR LOCATION, TISSUE SPECIFICITY, MUTAGENESIS OF 198-ASP--ALA-205
RP AND 228-PHE--LEU-248, AND MISCELLANEOUS.
RX PubMed=30146159; DOI=10.1016/j.cell.2018.07.032;
RA Qi B., Han M.;
RT "Microbial Siderophore Enterobactin Promotes Mitochondrial Iron Uptake and
RT Development of the Host via Interaction with ATP Synthase.";
RL Cell 175:571-582(2018).
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
CC 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. Subunits alpha and
CC beta form the catalytic core in F(1). Rotation of the central stalk
CC against the surrounding subunits leads to hydrolysis of ATP in three
CC separate catalytic sites on the beta subunits (Probable). Subunit alpha
CC does not bear the catalytic high-affinity ATP-binding sites (By
CC similarity). Binds the bacterial siderophore enterobactin and is
CC required for the assimilation of enterobactin-bound iron from non-
CC pathogenic bacteria. Promotes mitochondrial accumulation of
CC enterobactin-derived iron ions (PubMed:30146159).
CC {ECO:0000250|UniProtKB:P19483, ECO:0000269|PubMed:30146159,
CC ECO:0000305}.
CC -!- SUBUNIT: Subunit of the F-type ATPase which has 2 components, CF(1)
CC - the catalytic core - and CF(0) - the membrane proton channel.
CC {ECO:0000305}.
CC -!- SUBCELLULAR LOCATION: Mitochondrion {ECO:0000269|PubMed:30146159}.
CC Mitochondrion inner membrane {ECO:0000250|UniProtKB:P19483}; Peripheral
CC membrane protein {ECO:0000250|UniProtKB:P19483}; Matrix side
CC {ECO:0000250|UniProtKB:P19483}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=a {ECO:0000312|WormBase:H28O16.1a};
CC IsoId=Q9XXK1-1; Sequence=Displayed;
CC Name=d {ECO:0000312|WormBase:H28O16.1d};
CC IsoId=Q9XXK1-4; Sequence=VSP_052061;
CC -!- TISSUE SPECIFICITY: Ubiquitous (at protein level).
CC {ECO:0000269|PubMed:30146159}.
CC -!- DISRUPTION PHENOTYPE: RNAi-mediated knockdown of the protein leads to
CC impaired growth and development. In addition, it impairs the
CC assimilation of enterobactin-bound iron. {ECO:0000269|PubMed:30146159}.
CC -!- MISCELLANEOUS: The siderophore enterobactin (Ent) produced by enteric
CC bacteria binds Fe(3+) and helps them scavenge iron ions from the
CC environment. Enterobactin produced by non-pathogenic E.coli strains
CC facilitates iron assimilation in C.elegans (PubMed:30146159). Other
CC siderophores, such as ferrichrome and pyoverdine that is produced by
CC pathogenic bacteria, do not facilitate intestinal iron absorption in
CC C.elegans (PubMed:30146159). {ECO:0000269|PubMed:30146159}.
CC -!- SIMILARITY: Belongs to the ATPase alpha/beta chains family.
CC {ECO:0000255}.
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DR EMBL; BX284601; CAA19429.1; -; Genomic_DNA.
DR EMBL; BX284601; CAF31480.1; -; Genomic_DNA.
DR PIR; T23128; T23128.
DR RefSeq; NP_001021526.1; NM_001026355.3. [Q9XXK1-1]
DR RefSeq; NP_001021529.1; NM_001026358.4.
DR AlphaFoldDB; Q9XXK1; -.
DR SMR; Q9XXK1; -.
DR BioGRID; 38531; 70.
DR DIP; DIP-25446N; -.
DR IntAct; Q9XXK1; 2.
DR STRING; 6239.H28O16.1a; -.
DR iPTMnet; Q9XXK1; -.
DR World-2DPAGE; 0020:Q9XXK1; -.
DR EPD; Q9XXK1; -.
DR PaxDb; Q9XXK1; -.
DR PeptideAtlas; Q9XXK1; -.
DR PRIDE; Q9XXK1; -.
DR EnsemblMetazoa; H28O16.1a.1; H28O16.1a.1; WBGene00010419. [Q9XXK1-1]
DR GeneID; 173134; -.
DR KEGG; cel:CELE_H28O16.1; -.
DR UCSC; H28O16.1a; c. elegans. [Q9XXK1-1]
DR CTD; 173134; -.
DR WormBase; H28O16.1a; CE18826; WBGene00010419; atp-1. [Q9XXK1-1]
DR WormBase; H28O16.1d; CE36263; WBGene00010419; atp-1. [Q9XXK1-4]
DR eggNOG; KOG1353; Eukaryota.
DR GeneTree; ENSGT00550000074846; -.
DR InParanoid; Q9XXK1; -.
DR OMA; LQAPGVM; -.
DR OrthoDB; 470054at2759; -.
DR PhylomeDB; Q9XXK1; -.
DR Reactome; R-CEL-163210; Formation of ATP by chemiosmotic coupling.
DR Reactome; R-CEL-8949613; Cristae formation.
DR SignaLink; Q9XXK1; -.
DR PRO; PR:Q9XXK1; -.
DR Proteomes; UP000001940; Chromosome I.
DR Bgee; WBGene00010419; Expressed in adult organism and 4 other tissues.
DR GO; GO:0005754; C:mitochondrial proton-transporting ATP synthase, catalytic core; IBA:GO_Central.
DR GO; GO:0005739; C:mitochondrion; IDA:UniProtKB.
DR GO; GO:0045261; C:proton-transporting ATP synthase complex, catalytic core F(1); IBA:GO_Central.
DR GO; GO:0043531; F:ADP binding; IBA:GO_Central.
DR GO; GO:0005524; F:ATP binding; IBA:GO_Central.
DR GO; GO:1903981; F:enterobactin binding; IDA:UniProtKB.
DR GO; GO:0046933; F:proton-transporting ATP synthase activity, rotational mechanism; IEA:InterPro.
DR GO; GO:0033212; P:iron import into cell; IMP:UniProtKB.
DR GO; GO:0055072; P:iron ion homeostasis; IDA:UniProtKB.
DR GO; GO:0015986; P:proton motive force-driven ATP synthesis; IBA:GO_Central.
DR CDD; cd18113; ATP-synt_F1_alpha_C; 1.
DR CDD; cd01132; F1_ATPase_alpha; 1.
DR Gene3D; 1.20.150.20; -; 1.
DR Gene3D; 2.40.30.20; -; 1.
DR Gene3D; 3.40.50.300; -; 1.
DR HAMAP; MF_01346; ATP_synth_alpha_bact; 1.
DR InterPro; IPR023366; ATP_synth_asu-like_sf.
DR InterPro; IPR000793; ATP_synth_asu_C.
DR InterPro; IPR038376; ATP_synth_asu_C_sf.
DR InterPro; IPR033732; ATP_synth_F1_a.
DR InterPro; IPR005294; ATP_synth_F1_asu.
DR InterPro; IPR020003; ATPase_a/bsu_AS.
DR InterPro; IPR004100; ATPase_F1/V1/A1_a/bsu_N.
DR InterPro; IPR036121; ATPase_F1/V1/A1_a/bsu_N_sf.
DR InterPro; IPR000194; ATPase_F1/V1/A1_a/bsu_nucl-bd.
DR InterPro; IPR027417; P-loop_NTPase.
DR Pfam; PF00006; ATP-synt_ab; 1.
DR Pfam; PF00306; ATP-synt_ab_C; 1.
DR Pfam; PF02874; ATP-synt_ab_N; 1.
DR PIRSF; PIRSF039088; F_ATPase_subunit_alpha; 1.
DR SUPFAM; SSF50615; SSF50615; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
DR TIGRFAMs; TIGR00962; atpA; 1.
DR PROSITE; PS00152; ATPASE_ALPHA_BETA; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; ATP synthesis; ATP-binding; CF(1);
KW Direct protein sequencing; Hydrogen ion transport; Ion transport; Membrane;
KW Mitochondrion; Mitochondrion inner membrane; Nucleotide-binding;
KW Phosphoprotein; Reference proteome; Transit peptide; Transport.
FT TRANSIT 1..?
FT /note="Mitochondrion"
FT /evidence="ECO:0000255"
FT CHAIN ?..538
FT /note="ATP synthase subunit alpha, mitochondrial"
FT /id="PRO_0000239935"
FT REGION 228..248
FT /note="Essential and sufficient for enterobactin binding"
FT /evidence="ECO:0000269|PubMed:30146159"
FT BINDING 197..204
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00499"
FT SITE 398
FT /note="Required for activity"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10106"
FT VAR_SEQ 1..27
FT /note="Missing (in isoform d)"
FT /evidence="ECO:0000305"
FT /id="VSP_052061"
FT MUTAGEN 198..205
FT /note="Missing: No effect on enterobactin binding and iron
FT uptake."
FT /evidence="ECO:0000269|PubMed:30146159"
FT MUTAGEN 228..248
FT /note="Missing: Loss of enterobactin binding."
FT /evidence="ECO:0000269|PubMed:30146159"
SQ SEQUENCE 538 AA; 57788 MW; CC0358C33A4D66D2 CRC64;
MLSKRIVTAL NTAVKVQNAG IATTARGMAG ASGSEVSKIL EERILGTETG INLEETGKVL
SIGDGIARVY GLKNIQAEEM VEFDSGIKGM AMNLDVDNVG VVVFGNDKVI REGDIVKRTG
AIVDVPVGDG LLGRVVDALG NPIDGKGPIA NARRSRVEVK APGIIPRLSV REPMVTGVKA
VDSLVPIGRG QRELIIGDRQ TGKTAIAIDT IINQKRFNDA GDDKKKLFCI YVAVGQKRST
VAQIVKRLTD AGAMDYTIVV SATASDAAPL QFLAPYSGCA MGEHFRDNGK HALIIFDDLS
KQAVAYRQMS LLLRRPPGRE AYPGDVFYLH SRLLERAAKM NNSLGGGSLT ALPVIETQAG
DVSAYIPTNV ISITDGQIFL ETELFYKGVR PAINVGLSVS RVGSAAQTKA MKQVAGSMKL
ELAQYREVAA FAQFGSDLDA STQQLLNRGV RLTELLKQGQ YVPMGIEEQV GVIYAGVKGY
LDKVDPSAIT KFEKEFLAHL RSSQQALLKT IREEGQISPQ TDAQLKDVVV NFLATFKP
