ATP6_PENCH
ID ATP6_PENCH Reviewed; 257 AA.
AC Q36918;
DT 15-DEC-1998, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 96.
DE RecName: Full=ATP synthase subunit a;
DE AltName: Full=F-ATPase protein 6;
DE Flags: Precursor;
GN Name=atp6;
OS Penicillium chrysogenum (Penicillium notatum).
OG Mitochondrion.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Penicillium;
OC Penicillium chrysogenum species complex.
OX NCBI_TaxID=5076;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=KCTC 1262;
RX PubMed=8414999; DOI=10.1093/nar/21.18.4393;
RA Sheen J., Kho Y.H., Bae K.S.;
RT "Genomic sequence of mitochondrial genes coding for ATPase subunit 6 and
RT small subunit ribosomal RNA from Penicillium chrysogenum: a key for
RT molecular systematics on fungi.";
RL Nucleic Acids Res. 21:4393-4393(1993).
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; Z23072; CAA80613.1; -; Genomic_DNA.
DR EMBL; L19866; AAA58774.2; -; Genomic_DNA.
DR PIR; S42271; S42271.
DR AlphaFoldDB; Q36918; -.
DR SMR; Q36918; -.
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..8
FT /note="Removed in mature form"
FT /evidence="ECO:0000250"
FT /id="PRO_0000002618"
FT CHAIN 9..257
FT /note="ATP synthase subunit a"
FT /id="PRO_0000002619"
FT TRANSMEM 34..54
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 93..113
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 122..142
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 149..169
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 187..207
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 210..230
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 231..251
FT /note="Helical"
FT /evidence="ECO:0000255"
SQ SEQUENCE 257 AA; 28483 MW; 2F4BF3EE9BA50E98 CRC64;
MRHLDFVLSP LDQFEVRDLF SLNANLLGNL HLSLTNIGLY LTISIFLILT YSLLATNNNK
IIPNNWSISQ ESIYATVHGI VVNQINPNKG QMFFPLMYVL FIFILVNNLI GLVPYSFAST
SHFILTFSIS FTVVLGATIL GFQRHGLKFF SLFVPSGCPL ALLPLLVLIE FISYLSRNVS
LGLRLAANIL SGHMLLSILS GFTYNIMTSG IIFFILGLIP LAFIIAFSGL ELAIAFIQAQ
VFVVLACSYI KDGLDLH