ID   AT5F1_PONAB             Reviewed;         256 AA.
AC   Q5RFH9;
DT   05-JUL-2005, integrated into UniProtKB/Swiss-Prot.
DT   21-DEC-2004, sequence version 1.
DT   03-AUG-2022, entry version 84.
DE   RecName: Full=ATP synthase F(0) complex subunit B1, mitochondrial {ECO:0000305};
DE   AltName: Full=ATP synthase peripheral stalk-membrane subunit b {ECO:0000305};
DE   AltName: Full=ATP synthase subunit b;
DE            Short=ATPase subunit b;
DE   Flags: Precursor;
GN   Name=ATP5PB {ECO:0000250|UniProtKB:P24539}; Synonyms=ATP5F1;
OS   Pongo abelii (Sumatran orangutan) (Pongo pygmaeus abelii).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC   Pongo.
OX   NCBI_TaxID=9601;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Kidney;
RG   The German cDNA consortium;
RL   Submitted (NOV-2004) 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.
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. Component of an ATP synthase complex composed of
CC       ATP5PB, ATP5MC1, ATP5F1E, ATP5PD, ATP5ME, ATP5PF, ATP5MF, MT-ATP6, MT-
CC       ATP8, ATP5F1A, ATP5F1B, ATP5F1D, ATP5F1C, ATP5PO, ATP5MG, ATP5MK and
CC       ATP5MJ (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}.
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DR   EMBL; CR857178; CAH89478.1; -; mRNA.
DR   RefSeq; NP_001124636.1; NM_001131164.2.
DR   AlphaFoldDB; Q5RFH9; -.
DR   SMR; Q5RFH9; -.
DR   STRING; 9601.ENSPPYP00000001201; -.
DR   GeneID; 100171475; -.
DR   KEGG; pon:100171475; -.
DR   CTD; 515; -.
DR   eggNOG; KOG3976; Eukaryota.
DR   InParanoid; Q5RFH9; -.
DR   OrthoDB; 1314411at2759; -.
DR   Proteomes; UP000001595; Unplaced.
DR   GO; GO:0005753; C:mitochondrial proton-transporting ATP synthase complex; ISS:UniProtKB.
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   Acetylation; CF(0); Hydrogen ion transport; Ion transport; Membrane;
KW   Mitochondrion; Mitochondrion inner membrane; Reference proteome;
KW   Transit peptide; Transport.
FT   TRANSIT         1..42
FT                   /note="Mitochondrion"
FT                   /evidence="ECO:0000250"
FT   CHAIN           43..256
FT                   /note="ATP synthase F(0) complex subunit B1, mitochondrial"
FT                   /id="PRO_0000002515"
FT   MOD_RES         131
FT                   /note="N6-succinyllysine"
FT                   /evidence="ECO:0000250|UniProtKB:Q9CQQ7"
FT   MOD_RES         139
FT                   /note="N6-acetyllysine"
FT                   /evidence="ECO:0000250|UniProtKB:Q9CQQ7"
FT   MOD_RES         154
FT                   /note="N6-acetyllysine"
FT                   /evidence="ECO:0000250|UniProtKB:Q9CQQ7"
FT   MOD_RES         162
FT                   /note="N6-acetyllysine"
FT                   /evidence="ECO:0000250|UniProtKB:Q9CQQ7"
FT   MOD_RES         221
FT                   /note="N6-acetyllysine"
FT                   /evidence="ECO:0000250|UniProtKB:P24539"
FT   MOD_RES         233
FT                   /note="N6-acetyllysine"
FT                   /evidence="ECO:0000250|UniProtKB:P24539"
FT   MOD_RES         244
FT                   /note="N6-acetyllysine"
FT                   /evidence="ECO:0000250|UniProtKB:Q9CQQ7"
SQ   SEQUENCE   256 AA;  28894 MW;  08FAA99056A1BA58 CRC64;
     MLSRVVLSAA ATAASSLKNA AFLGPGVLQA TRTFHTGQPH LAPVPPLPEY GGKVRYGLIP
     EEFFQFLYPK TGVTGPYVLG TGLILYALSK EIYVISAETF TALSLIGVMV YGIKKYGPAV
     ADFADKLNEQ KLAQLEEAKQ TSIQQIQNAI DMEKSQQALV QKRHYLFDVQ RNNIAMALEV
     TYRERLYRVY KEVKNRLDYH IYVQNMMRQK EQEHMVNWVE KHVVQSISTQ QEKETIAKCI
     ADLKLLAKKA QAQPVM