ID C6HTL5_AJECH Unreviewed; 48 AA.
AC C6HTL5;
DT 01-SEP-2009, integrated into UniProtKB/TrEMBL.
DT 01-SEP-2009, sequence version 1.
DT 24-JAN-2024, entry version 37.
DE RecName: Full=ATP synthase protein 8 {ECO:0000256|ARBA:ARBA00019651, ECO:0000256|RuleBase:RU368038};
GN ORFNames=HCDG_12013 {ECO:0000313|EMBL:EER36349.1};
OS Ajellomyces capsulatus (strain H143) (Darling's disease fungus)
OS (Histoplasma capsulatum).
OG Mitochondrion {ECO:0000313|EMBL:EER36349.1}.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Onygenales; Ajellomycetaceae; Histoplasma.
OX NCBI_TaxID=544712 {ECO:0000313|EMBL:EER36349.1, ECO:0000313|Proteomes:UP000002624};
RN [1] {ECO:0000313|Proteomes:UP000002624}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=H143 {ECO:0000313|Proteomes:UP000002624};
RA Champion M., Cuomo C.A., Ma L.-J., Henn M.R., Sil A., Goldman B.,
RA Young S.K., Kodira C.D., Zeng Q., Koehrsen M., Alvarado L., Berlin A.M.,
RA Borenstein D., Chen Z., Engels R., Freedman E., Gellesch M., Goldberg J.,
RA Griggs A., Gujja S., Heiman D.I., Hepburn T.A., Howarth C., Jen D.,
RA Larson L., Lewis B., Mehta T., Park D., Pearson M., Roberts A., Saif S.,
RA Shea T.D., Shenoy N., Sisk P., Stolte C., Sykes S., Walk T., White J.,
RA Yandava C., Klein B., McEwen J.G., Puccia R., Goldman G.H., Felipe M.S.,
RA Nino-Vega G., San-Blas G., Taylor J.W., Mendoza L., Galagan J.E.,
RA Nusbaum C., Birren B.W.;
RT "The genome sequence of Ajellomyces capsulatus strain H143.";
RL Submitted (MAY-2009) to the EMBL/GenBank/DDBJ databases.
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. Minor subunit located with subunit a in the membrane.
CC {ECO:0000256|ARBA:ARBA00024864, ECO:0000256|RuleBase:RU368038}.
CC -!- SUBUNIT: F-type ATPases have 2 components, CF(1) - the catalytic core
CC - and CF(0) - the membrane proton channel.
CC {ECO:0000256|ARBA:ARBA00011291, ECO:0000256|RuleBase:RU368038}.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004167}; Single-
CC pass membrane protein {ECO:0000256|ARBA:ARBA00004167}. Mitochondrion
CC inner membrane {ECO:0000256|RuleBase:RU368038}; Single-pass membrane
CC protein {ECO:0000256|RuleBase:RU368038}. Mitochondrion membrane
CC {ECO:0000256|ARBA:ARBA00004304}; Single-pass membrane protein
CC {ECO:0000256|ARBA:ARBA00004304}.
CC -!- SIMILARITY: Belongs to the ATPase protein 8 family.
CC {ECO:0000256|ARBA:ARBA00008892, ECO:0000256|RuleBase:RU368038}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; GG692467; EER36349.1; -; Genomic_DNA.
DR AlphaFoldDB; C6HTL5; -.
DR STRING; 544712.C6HTL5; -.
DR VEuPathDB; FungiDB:HCDG_12013; -.
DR HOGENOM; CLU_214588_0_0_1; -.
DR Proteomes; UP000002624; Mitochondrion.
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:UniProtKB-UniRule.
DR GO; GO:0015986; P:proton motive force-driven ATP synthesis; IEA:UniProtKB-UniRule.
DR InterPro; IPR009230; ATP_synth_su8_fun.
DR PANTHER; PTHR36101; ATP SYNTHASE PROTEIN 8; 1.
DR PANTHER; PTHR36101:SF1; ATP SYNTHASE PROTEIN 8; 1.
DR Pfam; PF05933; Fun_ATP-synt_8; 1.
PE 3: Inferred from homology;
KW ATP synthesis {ECO:0000256|RuleBase:RU368038};
KW CF(0) {ECO:0000256|ARBA:ARBA00022547, ECO:0000256|RuleBase:RU368038};
KW Hydrogen ion transport {ECO:0000256|ARBA:ARBA00022781,
KW ECO:0000256|RuleBase:RU368038};
KW Ion transport {ECO:0000256|ARBA:ARBA00023065,
KW ECO:0000256|RuleBase:RU368038};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|RuleBase:RU368038};
KW Mitochondrion {ECO:0000256|ARBA:ARBA00023128,
KW ECO:0000256|RuleBase:RU368038};
KW Reference proteome {ECO:0000313|Proteomes:UP000002624};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692,
KW ECO:0000256|RuleBase:RU368038};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|RuleBase:RU368038}; Transport {ECO:0000256|RuleBase:RU368038}.
FT TRANSMEM 12..32
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU368038"
SQ SEQUENCE 48 AA; 5811 MW; 4DB79BB1A7900F50 CRC64;
MPQLVPFFFV NQALFVFILL SFITYTFSKY ILPRLVHLFL TRLFINKL
//
