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Database: UniProt
Entry: A0A087Y6Y0_POEFO
LinkDB: A0A087Y6Y0_POEFO
Original site: A0A087Y6Y0_POEFO 
ID   A0A087Y6Y0_POEFO        Unreviewed;       252 AA.
AC   A0A087Y6Y0;
DT   29-OCT-2014, integrated into UniProtKB/TrEMBL.
DT   29-OCT-2014, sequence version 1.
DT   27-MAR-2024, entry version 39.
DE   RecName: Full=ATP synthase subunit b {ECO:0000256|RuleBase:RU368017};
OS   Poecilia formosa (Amazon molly) (Limia formosa).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC   Ovalentaria; Atherinomorphae; Cyprinodontiformes; Poeciliidae; Poeciliinae;
OC   Poecilia.
OX   NCBI_TaxID=48698 {ECO:0000313|Ensembl:ENSPFOP00000013783.1, ECO:0000313|Proteomes:UP000028760};
RN   [1] {ECO:0000313|Proteomes:UP000028760}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=female {ECO:0000313|Proteomes:UP000028760};
RA   Schartl M., Warren W.;
RL   Submitted (OCT-2013) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|Ensembl:ENSPFOP00000013783.1}
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (SEP-2023) to UniProtKB.
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|ARBA:ARBA00003411,
CC       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. CF(0) has three main
CC       subunits: a, b and c. {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|ARBA:ARBA00007479, ECO:0000256|RuleBase:RU368017}.
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DR   EMBL; AYCK01013882; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   RefSeq; XP_007570969.1; XM_007570907.2.
DR   AlphaFoldDB; A0A087Y6Y0; -.
DR   STRING; 48698.ENSPFOP00000013783; -.
DR   Ensembl; ENSPFOT00000013802.2; ENSPFOP00000013783.1; ENSPFOG00000013706.2.
DR   GeneID; 103151065; -.
DR   KEGG; pfor:103151065; -.
DR   CTD; 515; -.
DR   eggNOG; KOG3976; Eukaryota.
DR   GeneTree; ENSGT00390000001958; -.
DR   OMA; KHMVDWI; -.
DR   OrthoDB; 5308930at2759; -.
DR   Proteomes; UP000028760; Unassembled WGS sequence.
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:UP000028760};
KW   Transport {ECO:0000256|ARBA:ARBA00022448, ECO:0000256|RuleBase:RU368017}.
SQ   SEQUENCE   252 AA;  28219 MW;  3F2FC850FE36FA77 CRC64;
     MLSRLVFLSA NSLRSSGLIG AGLVQASRSL QTSSQRLAPV PPLPDHGGKV RHGLIPEELF
     EFLYPKTGVT GPYMLGTGLI VYLLSKELYV INHETIYAIC IGTIIVYGVK KYGATVAAFI
     DSINEEKVAK AQAAKDSHIS FLTEAIENEK KEQWRVEGRG MLFDAKRNNV AMLLETNYRE
     RQHMVTNEVK RRLDYQIALQ HLNRRLQQEH MINWVEKNVI SSITPQQEKE SIAKCIADLK
     VLAKTTQAKA AA
//
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