ID   A0A1G4JMZ1_9SACH        Unreviewed;       236 AA.
AC   A0A1G4JMZ1;
DT   18-JAN-2017, integrated into UniProtKB/TrEMBL.
DT   18-JAN-2017, sequence version 1.
DT   24-JAN-2024, entry version 20.
DE   RecName: Full=ATP synthase subunit 4 {ECO:0000256|RuleBase:RU368017};
GN   ORFNames=LAMI_0E07316G {ECO:0000313|EMBL:SCU91798.1};
OS   Lachancea mirantina.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Saccharomycetaceae; Lachancea.
OX   NCBI_TaxID=1230905 {ECO:0000313|EMBL:SCU91798.1, ECO:0000313|Proteomes:UP000191024};
RN   [1] {ECO:0000313|EMBL:SCU91798.1, ECO:0000313|Proteomes:UP000191024}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CBS 11717 {ECO:0000313|EMBL:SCU91798.1};
RA   Devillers H.;
RL   Submitted (MAR-2016) 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
CC       F(0) - containing the membrane proton channel, linked together by a
CC       central stalk and a peripheral stalk. During catalysis, ATP synthesis
CC       in the catalytic domain of F(1) is coupled via a rotary mechanism of
CC       the central stalk subunits to proton translocation. Part of the complex
CC       F(0) domain and the peripheric stalk, which acts as a stator to hold
CC       the catalytic alpha(3)beta(3) subcomplex and subunit a/ATP6 static
CC       relative to the rotary elements. {ECO:0000256|RuleBase:RU368017}.
CC   -!- SUBUNIT: F-type ATPases have 2 components, CF(1) - the catalytic core
CC       - and CF(0) - the membrane proton channel. In yeast, the dimeric form
CC       of ATP synthase consists of 17 polypeptides: alpha, beta, gamma, delta,
CC       epsilon, 4 (B), 5 (OSCP), 6 (A), 8, 9 (C), d, E (Tim11), f, g, h, i/j
CC       and k. {ECO:0000256|RuleBase:RU368017}.
CC   -!- SUBCELLULAR LOCATION: Mitochondrion {ECO:0000256|RuleBase:RU368017}.
CC       Mitochondrion inner membrane {ECO:0000256|RuleBase:RU368017}.
CC   -!- SIMILARITY: Belongs to the eukaryotic ATPase B chain family.
CC       {ECO:0000256|RuleBase:RU368017}.
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DR   EMBL; LT598465; SCU91798.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1G4JMZ1; -.
DR   STRING; 1230905.A0A1G4JMZ1; -.
DR   OrthoDB; 1330736at2759; -.
DR   Proteomes; UP000191024; Chromosome e.
DR   GO; GO:0000276; C:mitochondrial proton-transporting ATP synthase complex, coupling factor F(o); IEA:UniProtKB-UniRule.
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   Gene3D; 1.20.5.2210; -; 1.
DR   InterPro; IPR008688; ATP_synth_Bsub_B/MI25.
DR   InterPro; IPR013837; ATP_synth_F0_suB.
DR   PANTHER; PTHR12733:SF3; ATP SYNTHASE F(0) COMPLEX SUBUNIT B1, MITOCHONDRIAL; 1.
DR   PANTHER; PTHR12733; MITOCHONDRIAL ATP SYNTHASE B CHAIN; 1.
DR   Pfam; PF05405; Mt_ATP-synt_B; 1.
DR   SUPFAM; SSF161060; ATP synthase B chain-like; 1.
PE   3: Inferred from homology;
KW   CF(0) {ECO:0000256|ARBA:ARBA00022547, ECO:0000256|RuleBase:RU368017};
KW   Hydrogen ion transport {ECO:0000256|ARBA:ARBA00022781,
KW   ECO:0000256|RuleBase:RU368017};
KW   Ion transport {ECO:0000256|ARBA:ARBA00023065,
KW   ECO:0000256|RuleBase:RU368017};
KW   Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|RuleBase:RU368017};
KW   Mitochondrion {ECO:0000256|ARBA:ARBA00023128,
KW   ECO:0000256|RuleBase:RU368017};
KW   Mitochondrion inner membrane {ECO:0000256|ARBA:ARBA00022792,
KW   ECO:0000256|RuleBase:RU368017};
KW   Reference proteome {ECO:0000313|Proteomes:UP000191024};
KW   Transport {ECO:0000256|ARBA:ARBA00022448, ECO:0000256|RuleBase:RU368017}.
SQ   SEQUENCE   236 AA;  25770 MW;  7D55664FAAB310DA CRC64;
     MSFSALSLRA QARPLLALSA RQAPIGVRYM STPAPQDPKS KATSILDALP GNNFLSKTGI
     LATSTAAAIY AISNELYVIN DETILLGTFT GFGIIVAKFL APAYKDFADA RVKQVSDVLN
     ASRTRHVDAV KQRIESVSEL QNVSETTKVL FDVSKETVEL EAKVFELKQK VELAAEAKSV
     LDSWVRYEAS VRQLQQKQLA EGVIAKVKAE LSNPKFQDKV LQQSVSDVEK LLASLK
//