ATP6_TRIRU
ID ATP6_TRIRU Reviewed; 255 AA.
AC Q36835;
DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 94.
DE RecName: Full=ATP synthase subunit a;
DE AltName: Full=F-ATPase protein 6;
DE Flags: Precursor;
GN Name=ATP6;
OS Trichophyton rubrum (Athlete's foot fungus) (Epidermophyton rubrum).
OG Mitochondrion.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Onygenales; Arthrodermataceae; Trichophyton.
OX NCBI_TaxID=5551;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=IP 1817.89;
RX PubMed=8593686; DOI=10.1007/bf00518168;
RA de Bievre C., Dujon B.;
RT "Organisation of the mitochondrial genome of Trichophyton rubrum. DNA
RT sequence analysis of the ND4 gene, the ATPase subunit-6 gene, the ribosomal
RT RNA small-subunit gene, the ND6 gene, the COXIII gene, the ATPase subunit-8
RT gene and six tRNA genes that correspond respectively to the tyrosine,
RT lysine, glutamine, asparagine, isoleucine and tryptophan isoacceptors.";
RL Curr. Genet. 28:553-559(1995).
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 (By similarity). {ECO:0000250}.
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; X88896; CAA61355.1; -; Genomic_DNA.
DR PIR; S65032; S65032.
DR AlphaFoldDB; Q36835; -.
DR SMR; Q36835; -.
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; IEA:InterPro.
DR Gene3D; 1.20.120.220; -; 1.
DR HAMAP; MF_01393; ATP_synth_a_bact; 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 PRINTS; PR00123; ATPASEA.
DR SUPFAM; SSF81336; SSF81336; 1.
DR TIGRFAMs; TIGR01131; ATP_synt_6_or_A; 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; Transmembrane;
KW Transmembrane helix; Transport.
FT PROPEP 1..7
FT /note="Removed in mature form"
FT /evidence="ECO:0000250"
FT /id="PRO_0000002622"
FT CHAIN 8..255
FT /note="ATP synthase subunit a"
FT /id="PRO_0000002623"
FT TRANSMEM 35..55
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 91..111
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 120..140
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 147..167
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 177..197
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 208..228
FT /note="Helical"
FT /evidence="ECO:0000255"
SQ SEQUENCE 255 AA; 28826 MW; D0EBDAF63866DE95 CRC64;
MMFNNIISPL EQFEIKDLFS LNINIINLKM SLTNFGFYII ISTIIILTLH LLITYNNKLI
SNSWTLTKES IYATVHSVVI NQINSKEGQN YFPFIYGLFI FILMNNLLGL IPYSFSSTSH
FILTFFISFT VVLGATILGF QKHQLKFFSL FVPSGCPLGL LPLLVLIELI SYLARNVSLG
LRLSANILSG HMLLVILSDF TFKIMSSGIF YFLIGLIPLA FIFAFSGLEL GIAFIQSQVF
IVLTCSYIRD SLELH