ID   A0A183EET5_9BILA        Unreviewed;       317 AA.
AC   A0A183EET5;
DT   07-SEP-2016, integrated into UniProtKB/TrEMBL.
DT   07-SEP-2016, sequence version 1.
DT   27-MAR-2024, entry version 27.
DE   RecName: Full=ATP synthase subunit b {ECO:0000256|RuleBase:RU368017};
GN   ORFNames=GPUH_LOCUS19476 {ECO:0000313|EMBL:VDN33919.1};
OS   Gongylonema pulchrum.
OC   Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC   Spirurina; Spiruromorpha; Spiruroidea; Gongylonematidae; Gongylonema.
OX   NCBI_TaxID=637853 {ECO:0000313|Proteomes:UP000050760, ECO:0000313|WBParaSite:GPUH_0001950101-mRNA-1};
RN   [1] {ECO:0000313|WBParaSite:GPUH_0001950101-mRNA-1}
RP   IDENTIFICATION.
RG   WormBaseParasite;
RL   Submitted (JUN-2016) to UniProtKB.
RN   [2] {ECO:0000313|EMBL:VDN33919.1, ECO:0000313|Proteomes:UP000271098}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RG   Pathogen Informatics;
RL   Submitted (NOV-2018) 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. 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; UYRT01088598; VDN33919.1; -; Genomic_DNA.
DR   WBParaSite; GPUH_0001950101-mRNA-1; GPUH_0001950101-mRNA-1; GPUH_0001950101.
DR   Proteomes; UP000050760; Unplaced.
DR   Proteomes; UP000271098; 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:UP000271098};
KW   Transport {ECO:0000256|ARBA:ARBA00022448, ECO:0000256|RuleBase:RU368017}.
SQ   SEQUENCE   317 AA;  37159 MW;  126E0340554E57D0 CRC64;
     VLRLLGVVSN ASNESRGGAL KPETSEKVGF FKKLKYRFQE AKTNGKNKNL WTHSLYFQFL
     TGIPLKDELQ APISFMRDIG KQFIPPPLPA LPKDFKEHPE RDLVNYPYPL KQMYPPKLRL
     MIVPDTFMSA FHKYTGTSGP YVFFAMLYAF LHSKGLFEIA HDRVKVLIII FYYYIFSRAF
     DYRWDKFFYE NAKKVEKKYL DIIDNNFKAV RTVQETSKAG KIAYAAVKEH YPAVFKETLA
     LQLEATYRRN VELLASEMKR RLDYLLETQA VKRSFARDHM LKWIIEAVRA EIIANKENIK
     EKYMDNCIEQ LKGISLQ
//