ID ATP9_EMENI Reviewed; 143 AA.
AC P16000; C8VNG9; Q5BCV6;
DT 01-APR-1990, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2007, sequence version 2.
DT 27-MAR-2024, entry version 141.
DE RecName: Full=ATP synthase subunit 9, mitochondrial;
DE AltName: Full=Lipid-binding protein;
DE Flags: Precursor;
GN Name=atp9; Synonyms=oliC; ORFNames=AN1624;
OS Emericella nidulans (strain FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 /
OS M139) (Aspergillus nidulans).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC Aspergillus subgen. Nidulantes.
OX NCBI_TaxID=227321;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=2880279; DOI=10.1007/bf00430447;
RA Ward M., Turner G.;
RT "The ATP synthase subunit 9 gene of Aspergillus nidulans: sequence and
RT transcription.";
RL Mol. Gen. Genet. 205:331-338(1986).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139;
RX PubMed=16372000; DOI=10.1038/nature04341;
RA Galagan J.E., Calvo S.E., Cuomo C., Ma L.-J., Wortman J.R., Batzoglou S.,
RA Lee S.-I., Bastuerkmen M., Spevak C.C., Clutterbuck J., Kapitonov V.,
RA Jurka J., Scazzocchio C., Farman M.L., Butler J., Purcell S., Harris S.,
RA Braus G.H., Draht O., Busch S., D'Enfert C., Bouchier C., Goldman G.H.,
RA Bell-Pedersen D., Griffiths-Jones S., Doonan J.H., Yu J., Vienken K.,
RA Pain A., Freitag M., Selker E.U., Archer D.B., Penalva M.A., Oakley B.R.,
RA Momany M., Tanaka T., Kumagai T., Asai K., Machida M., Nierman W.C.,
RA Denning D.W., Caddick M.X., Hynes M., Paoletti M., Fischer R., Miller B.L.,
RA Dyer P.S., Sachs M.S., Osmani S.A., Birren B.W.;
RT "Sequencing of Aspergillus nidulans and comparative analysis with A.
RT fumigatus and A. oryzae.";
RL Nature 438:1105-1115(2005).
RN [3]
RP GENOME REANNOTATION.
RC STRAIN=FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139;
RX PubMed=19146970; DOI=10.1016/j.fgb.2008.12.003;
RA Wortman J.R., Gilsenan J.M., Joardar V., Deegan J., Clutterbuck J.,
RA Andersen M.R., Archer D., Bencina M., Braus G., Coutinho P., von Dohren H.,
RA Doonan J., Driessen A.J., Durek P., Espeso E., Fekete E., Flipphi M.,
RA Estrada C.G., Geysens S., Goldman G., de Groot P.W., Hansen K.,
RA Harris S.D., Heinekamp T., Helmstaedt K., Henrissat B., Hofmann G.,
RA Homan T., Horio T., Horiuchi H., James S., Jones M., Karaffa L.,
RA Karanyi Z., Kato M., Keller N., Kelly D.E., Kiel J.A., Kim J.M.,
RA van der Klei I.J., Klis F.M., Kovalchuk A., Krasevec N., Kubicek C.P.,
RA Liu B., Maccabe A., Meyer V., Mirabito P., Miskei M., Mos M., Mullins J.,
RA Nelson D.R., Nielsen J., Oakley B.R., Osmani S.A., Pakula T., Paszewski A.,
RA Paulsen I., Pilsyk S., Pocsi I., Punt P.J., Ram A.F., Ren Q., Robellet X.,
RA Robson G., Seiboth B., van Solingen P., Specht T., Sun J.,
RA Taheri-Talesh N., Takeshita N., Ussery D., vanKuyk P.A., Visser H.,
RA van de Vondervoort P.J., de Vries R.P., Walton J., Xiang X., Xiong Y.,
RA Zeng A.P., Brandt B.W., Cornell M.J., van den Hondel C.A., Visser J.,
RA Oliver S.G., Turner G.;
RT "The 2008 update of the Aspergillus nidulans genome annotation: a community
RT effort.";
RL Fungal Genet. Biol. 46:S2-13(2009).
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.
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 membrane {ECO:0000305}; Multi-pass
CC membrane protein {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the ATPase C chain family. {ECO:0000305}.
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DR EMBL; M30144; AAA33296.1; -; Genomic_DNA.
DR EMBL; AACD01000026; EAA64744.1; -; Genomic_DNA.
DR EMBL; BN001307; CBF85243.1; -; Genomic_DNA.
DR PIR; S62677; S62677.
DR RefSeq; XP_659228.1; XM_654136.1.
DR AlphaFoldDB; P16000; -.
DR SMR; P16000; -.
DR STRING; 227321.P16000; -.
DR EnsemblFungi; CBF85243; CBF85243; ANIA_01624.
DR GeneID; 2875595; -.
DR KEGG; ani:AN1624.2; -.
DR VEuPathDB; FungiDB:AN1624; -.
DR eggNOG; KOG3025; Eukaryota.
DR HOGENOM; CLU_116822_0_0_1; -.
DR InParanoid; P16000; -.
DR OMA; MKRQTIQ; -.
DR OrthoDB; 316029at2759; -.
DR Proteomes; UP000000560; Chromosome VII.
DR GO; GO:0000276; C:mitochondrial 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:0071472; P:cellular response to salt stress; IEP:AspGD.
DR GO; GO:0015986; P:proton motive force-driven ATP synthesis; IBA:GO_Central.
DR CDD; cd18182; ATP-synt_Fo_c_ATP5G3; 1.
DR Gene3D; 1.20.20.10; F1F0 ATP synthase subunit C; 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; ATP SYNTHASE LIPID-BINDING PROTEIN, MITOCHONDRIAL; 1.
DR PANTHER; PTHR10031:SF13; ATP SYNTHASE SUBUNIT 9, MITOCHONDRIAL; 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 CF(0); Hydrogen ion transport; Ion transport; Lipid-binding; Membrane;
KW Mitochondrion; Reference proteome; Transit peptide; Transmembrane;
KW Transmembrane helix; Transport.
FT TRANSIT 1..62
FT /note="Mitochondrion"
FT CHAIN 63..143
FT /note="ATP synthase subunit 9, mitochondrial"
FT /id="PRO_0000002572"
FT TRANSMEM 85..105
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 119..139
FT /note="Helical"
FT /evidence="ECO:0000255"
FT SITE 127
FT /note="Reversibly protonated during proton transport"
FT /evidence="ECO:0000250"
FT CONFLICT 94
FT /note="I -> T (in Ref. 1; AAA33296)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 143 AA; 15264 MW; EDA2356DC67C8187 CRC64;
MAASRVFAQR LASTMKVARP AARIQARTLT TQRMATPFQT IKRQQPSMIQ ASARQAFAAR
RQYSSEIADA MVQVSQNIGM GSAAIGLGGA GIGIGVVFGS LLLAVSRNPA LRGQLFSYAI
LGFAFVEAIG LFDLMVAMMC KYV
//
