ID   ATPF_PARBR              Reviewed;         244 AA.
AC   Q870C4;
DT   27-SEP-2004, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2003, sequence version 1.
DT   03-AUG-2022, entry version 61.
DE   RecName: Full=ATP synthase subunit 4, mitochondrial;
DE   Flags: Precursor;
GN   Name=ATP4;
OS   Paracoccidioides brasiliensis.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Onygenales; Onygenales incertae sedis; Paracoccidioides.
OX   NCBI_TaxID=121759;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RA   Castro N.S., Lima T.A., Pereira M., Jesuino R.S.A., Felipe M.S.S.,
RA   Soares C.M.A.;
RT   "The ATP synthase subunit 4, mitochondrial, from the human pathogenic
RT   fungus Paracoccidioides brasiliensis.";
RL   Submitted (APR-2003) 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 (By similarity). {ECO:0000250}.
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 (By similarity). {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Mitochondrion {ECO:0000250}. Mitochondrion inner
CC       membrane {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the eukaryotic ATPase B chain family.
CC       {ECO:0000305}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; AY271747; AAP22959.1; -; mRNA.
DR   AlphaFoldDB; Q870C4; -.
DR   SMR; Q870C4; -.
DR   VEuPathDB; FungiDB:PABG_00180; -.
DR   VEuPathDB; FungiDB:PADG_02578; -.
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; IPR008688; ATP_synth_Bsub_B/MI25.
DR   InterPro; IPR013837; ATP_synth_F0_suB.
DR   PANTHER; PTHR12733; PTHR12733; 1.
DR   Pfam; PF05405; Mt_ATP-synt_B; 1.
PE   2: Evidence at transcript level;
KW   CF(0); Hydrogen ion transport; Ion transport; Membrane; Mitochondrion;
KW   Mitochondrion inner membrane; Transit peptide; Transport.
FT   TRANSIT         1..36
FT                   /note="Mitochondrion"
FT                   /evidence="ECO:0000250"
FT   CHAIN           37..244
FT                   /note="ATP synthase subunit 4, mitochondrial"
FT                   /id="PRO_0000002522"
SQ   SEQUENCE   244 AA;  26508 MW;  8B91C1F79BB3CCFA CRC64;
     MASRLAKSAI CAARVRPVLS SRTIPAAATT LTSTRSVSNV PTEDPKTKAQ SIIDALPGNS
     LVSKTAILSA GAGLSIAAIS NELYVFSEET VAAFCLLSVF AGVAKMAGPM YKEWAETQIQ
     KQKDILNGAR ANHTNAVKQR IENVKQLSGV VDITKALFEV SKETARLEAQ AYELEQRTAL
     AAEAKKVLDS WVQYEGQVKV RQQRELAQTV ISKVQKELEN PKVIQQILQQ SVTDVERIFA
     AKPQ