(data stored in ACNUC14238 zone)

HOGENOM: KLLAC1_1_PE3

ID   KLLAC1_1_PE3                         STANDARD;      PRT;   256 AA.
AC   KLLAC1_1_PE3; Q6DN61;
DT   00-JAN-0000 (Rel. 1, Created)
DT   00-JAN-0000 (Rel. 2, Last sequence update)
DT   00-JAN-0000 (Rel. 3, Last annotation update)
DE   RecName: Full=ATP synthase subunit a;AltName: Full=ATP synthase subunit
DE   6;AltName: Full=F-ATPase protein 6;Flags: Precursor; (KLLAC1_1.PE3).
GN   Name=ATP6;
OS   KLUYVEROMYCES LACTIS NRRL Y-1140.
OG   Mitochondrion.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Saccharomycetaceae; Kluyveromyces.
OX   NCBI_TaxID=284590;
RN   [0]
RP   -.;
RG   -.;
RL   -.;
CC   -!- SEQ. DATA ORIGIN: Translated from the HOGENOM CDS KLLAC1_1.PE3.
CC       Kluyveromyces lactis (strain CBS 2359 / WM37 / ATCC 8585 / DSM 70799 /
CC       NRRL Y-1140) mitochondrion, complete sequence.
CC   -!- ANNOTATIONS ORIGIN:ATP6_KLULA
CC   -!- FUNCTION: Mitochondrial membrane ATP synthase (F(1)F(0) ATP
CC       synthase or Complex V) produces ATP from ADP in the presence of a
CC       proton gradient across the membrane which is generated by electron
CC       transport complexes of the respiratory chain. F-type ATPases
CC       consist of two structural domains, F(1) - containing the
CC       extramembraneous catalytic core and F(0) - containing the membrane
CC       proton channel, linked together by a central stalk and a
CC       peripheral stalk. During catalysis, ATP synthesis in the catalytic
CC       domain of F(1) is coupled via a rotary mechanism of the central
CC       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 (By similarity).
CC   -!- SUBUNIT: F-type ATPases have 2 components, CF(1) - the catalytic
CC       core - and CF(0) - the membrane proton channel. CF(1) has five
CC       subunits: alpha(3), beta(3), gamma(1), delta(1), epsilon(1). CF(0)
CC       has three main subunits: a, b and c (By similarity).
CC   -!- SUBCELLULAR LOCATION: Mitochondrion inner membrane; Multi-pass
CC       membrane protein.
CC   -!- SIMILARITY: Belongs to the ATPase A chain family.
CC   -!- GENE_FAMILY: HOG000253874 [ FAMILY / ALN / TREE ]
DR   UniProtKB/Swiss-Prot; Q6DN61; -.
DR   EMBL; AY654900; AAT64951.1; -; Genomic_DNA.
DR   RefSeq; YP_054498.1; NC_006077.1.
DR   ProteinModelPortal; Q6DN61; -.
DR   STRING; Q6DN61; -.
DR   GeneID; 2914052; -.
DR   GenomeReviews; AY654900_GR; ATP6.
DR   KEGG; kla:KllafMp03; -.
DR   OrthoDB; EOG4TTKT0; -.
DR   PhylomeDB; Q6DN61; -.
DR   GO; GO:0016021; C:integral to 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:hydrogen ion transmembrane transporter activity; IEA:InterPro.
DR   GO; GO:0015986; P:ATP synthesis coupled proton transport; IEA:InterPro.
DR   InterPro; IPR000568; ATPase_F0-cplx_asu.
DR   InterPro; IPR023011; ATPase_F0-cplx_asu_AS.
DR   Gene3D; G3DSA:1.20.120.220; ATPase_F0_A; 1.
DR   PANTHER; PTHR11410; ATPase_F0_A; 1.
DR   Pfam; PF00119; ATP-synt_A; 1.
DR   PRINTS; PR00123; ATPASEA.
DR   SUPFAM; SSF81336; ATPase_F0_A; 1.
DR   TIGRFAMs; TIGR01131; ATP_synt_6_or_A; 1.
DR   PROSITE; PS00449; ATPASE_A; 1.
DR   HOGENOMDNA; KLLAC1_1.PE3; -.
KW   AAT64951.1824841755old_1320000031;
KW   ATP synthase subunit a ;
KW   ATP synthesis; CF(0); Complete proteome; Hydrogen ion transport;
KW   Ion transport; Membrane; Mitochondrion; Mitochondrion inner membrane;
KW   Transmembrane; Transmembrane helix; Transport.
SQ   SEQUENCE   256 AA;  UNKNOWN MW;  UNKNOWN CRC64;
     MLNLFITSPL DQFEIRVLMG FTSPLLDFSS LNFTTFSLYT IIVLFTVLGL NLLTTNNNKI
     IGSKWFVSQE AIYDTILNMV KGQIGGKLWG YYFPLVYTFF FFIFVSNLIS MIPYSFALSA
     HLIFIVSLSS VIWLGATIIG LTKHGLVFFS LFVPGGTPLP LVPLLVLIEL LSYFARAISL
     GLRLSSNVLS GHLLLIILGG LLFNLMSMSI ITFVFGLIPG VGLLAIVVLE FAISVIQAYV
     WSILTSSYLK DVLYLH
//

If you have problems or comments...

PBIL Back to PBIL home page