ID   ATPJ_PICAN              Reviewed;          89 AA.
AC   C0HK61;
DT   10-OCT-2018, integrated into UniProtKB/Swiss-Prot.
DT   10-OCT-2018, sequence version 1.
DT   03-AUG-2022, entry version 8.
DE   RecName: Full=ATP synthase subunit e, mitochondrial {ECO:0000250|UniProtKB:P81449};
DE            Short=ATPase subunit e {ECO:0000250|UniProtKB:P81449};
DE   AltName: Full=Translocase of the inner membrane protein 11 {ECO:0000250|UniProtKB:P81449};
GN   Name=TIM11 {ECO:0000250|UniProtKB:P81449};
GN   Synonyms=ATP21 {ECO:0000250|UniProtKB:P81449};
OS   Pichia angusta (Yeast) (Hansenula polymorpha).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Pichiaceae; Ogataea.
OX   NCBI_TaxID=870730;
RN   [1] {ECO:0000305}
RP   PARTIAL PROTEIN SEQUENCE.
RC   STRAIN=A16 / NCYC 2310 {ECO:0000303|Ref.1};
RA   Fearnley I.M.;
RL   Submitted (AUG-2016) to UniProtKB.
RN   [2] {ECO:0000305}
RP   PROTEIN SEQUENCE OF 1-7, IDENTIFICATION IN ATP SYNTHASE COMPLEX, FUNCTION
RP   OF ATPASE COMPLEX, SUBUNIT, SUBCELLULAR LOCATION, MASS SPECTROMETRY,
RP   IDENTIFICATION BY MASS SPECTROMETRY, AND ACETYLATION AT SER-1.
RC   STRAIN=A16 / NCYC 2310 {ECO:0000303|PubMed:25759169};
RX   PubMed=25759169; DOI=10.1042/bj20150197;
RA   Liu S., Charlesworth T.J., Bason J.V., Montgomery M.G., Harbour M.E.,
RA   Fearnley I.M., Walker J.E.;
RT   "The purification and characterization of ATP synthase complexes from the
RT   mitochondria of four fungal species.";
RL   Biochem. J. 468:167-175(2015).
RN   [3] {ECO:0000305}
RP   STRUCTURE BY ELECTRON MICROSCOPY (7.0 ANGSTROMS) OF MONOMERIC ATP SYNTHASE
RP   COMPLEX IN COMPLEX WITH BOVINE ATPIF1, FUNCTION, SUBUNIT, AND SUBCELLULAR
RP   LOCATION.
RX   PubMed=27791192; DOI=10.1073/pnas.1615902113;
RA   Vinothkumar K.R., Montgomery M.G., Liu S., Walker J.E.;
RT   "Structure of the mitochondrial ATP synthase from Pichia angusta determined
RT   by electron cryo-microscopy.";
RL   Proc. Natl. Acad. Sci. U.S.A. 113:12709-12714(2016).
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 (PubMed:25759169). F-type ATP synthases
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 peripheral
CC       stalk (PubMed:27791192). 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 (By similarity). Part of
CC       the complex F(0) domain (By similarity). Minor subunit located with
CC       subunit a/ATP6 in the membrane (By similarity). Together with subunit
CC       g/ATP20, probably contributes to membrane curvature at the site of the
CC       ATP synthase dimer, ultimately contributing to formation of cristae (By
CC       similarity). {ECO:0000250|UniProtKB:B5FVG3,
CC       ECO:0000269|PubMed:25759169, ECO:0000269|PubMed:27791192}.
CC   -!- SUBUNIT: F-type ATP synthases have 2 components, the catalytic core
CC       F(1) and the membrane-embedded component F(0), linked together by a
CC       central stalk and a peripheral stalk (PubMed:27791192). The central
CC       stalk, also called rotor shaft, is often seen as part of F(1)
CC       (PubMed:27791192). The peripheral stalk is seen as part of F(0). F(0)
CC       contains the membrane channel next to the rotor (PubMed:27791192). F-
CC       type ATP synthases form dimers but each monomer functions independently
CC       in ATP generation (By similarity). The dimer consists of 18 different
CC       polypeptides: ATP1 (subunit alpha, part of F(1), 3 molecules per
CC       monomer), ATP2 (subunit beta, part of F(1), 3 molecules per monomer),
CC       ATP3 (subunit gamma, part of the central stalk), ATP4 (subunit b, part
CC       of the peripheral stalk), ATP5/OSCP (subunit 5/OSCP, part of the
CC       peripheral stalk), ATP6 (subunit a, part of the peripheral stalk), ATP7
CC       (subunit d, part of the peripheral stalk), ATP8 (subunit 8, part of the
CC       peripheral stalk), OLI1 (subunit c, part of the rotor, 10 molecules per
CC       monomer), ATP14 (subunit h, part of the peripheral stalk), ATP15
CC       (subunit epsilon, part of the central stalk), ATP16 (subunit delta,
CC       part of the central stalk), ATP17 (subunit f, part of the peripheral
CC       stalk), ATP18 (subunit i/j, part of the peripheral stalk)
CC       (PubMed:27791192, PubMed:25759169). Dimer-specific subunits are ATP19
CC       (subunit k, at interface between monomers), ATP20 (subunit g, at
CC       interface between monomers), TIM11 (subunit e, at interface between
CC       monomers) (By similarity). Also contains subunit L (PubMed:25759169).
CC       {ECO:0000250|UniProtKB:B5FVG3, ECO:0000269|PubMed:25759169,
CC       ECO:0000269|PubMed:27791192}.
CC   -!- SUBCELLULAR LOCATION: Mitochondrion inner membrane
CC       {ECO:0000305|PubMed:27791192}; Single-pass membrane protein
CC       {ECO:0000255}. Note=The F-type ATP synthase complex is anchored in the
CC       mitochondrial inner membrane via the F(0) domain with the F(1) domain
CC       and the peripheral stalk extending into the mitochondrial matrix.
CC       {ECO:0000305|PubMed:27791192}.
CC   -!- MASS SPECTROMETRY: Mass=9987; Method=MALDI;
CC       Evidence={ECO:0000269|PubMed:25759169};
CC   -!- SIMILARITY: Belongs to the ATPase e subunit family. {ECO:0000305}.
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DR   AlphaFoldDB; C0HK61; -.
DR   SMR; C0HK61; -.
DR   iPTMnet; C0HK61; -.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0000276; C:mitochondrial proton-transporting ATP synthase complex, coupling factor F(o); IEA:InterPro.
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   InterPro; IPR008386; ATP_synth_F0_esu_mt.
DR   Pfam; PF05680; ATP-synt_E; 1.
PE   1: Evidence at protein level;
KW   Acetylation; ATP synthesis; CF(0); Direct protein sequencing;
KW   Hydrogen ion transport; Ion transport; Membrane; Mitochondrion;
KW   Mitochondrion inner membrane; Transmembrane; Transmembrane helix;
KW   Transport.
FT   CHAIN           1..89
FT                   /note="ATP synthase subunit e, mitochondrial"
FT                   /evidence="ECO:0000269|Ref.1"
FT                   /id="PRO_0000445319"
FT   TRANSMEM        8..25
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   MOD_RES         1
FT                   /note="N-acetylserine"
FT                   /evidence="ECO:0000269|PubMed:25759169"
SQ   SEQUENCE   89 AA;  9945 MW;  3173CEE9C3136B85 CRC64;
     STLNVLRYSS LAAGIVYGAY HTYTLKLEGE KKQELYDYQK KLKLVEAAKA EYRKLNPPKQ
     AASTEAVNLD DPEFDFGKFI LGAVEKLGS