ID   A0A2K6VL63_ONCVO        Unreviewed;       329 AA.
AC   A0A2K6VL63;
DT   28-MAR-2018, integrated into UniProtKB/TrEMBL.
DT   28-MAR-2018, sequence version 1.
DT   24-JAN-2024, entry version 18.
DE   RecName: Full=ATP synthase subunit b {ECO:0000256|RuleBase:RU368017};
OS   Onchocerca volvulus.
OC   Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC   Spirurina; Spiruromorpha; Filarioidea; Onchocercidae; Onchocerca.
OX   NCBI_TaxID=6282 {ECO:0000313|EnsemblMetazoa:OVOC12148.1, ECO:0000313|Proteomes:UP000024404};
RN   [1] {ECO:0000313|Proteomes:UP000024404}
RP   NUCLEOTIDE SEQUENCE.
RA   Cotton J., Tsai J., Stanley E., Tracey A., Holroyd N., Lustigman S.,
RA   Berriman M.;
RT   "Genome sequencing of Onchocerca volvulus.";
RL   Submitted (OCT-2013) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EnsemblMetazoa:OVOC12148.1}
RP   IDENTIFICATION.
RG   EnsemblMetazoa;
RL   Submitted (FEB-2018) 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|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; CMVM020000396; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   AlphaFoldDB; A0A2K6VL63; -.
DR   STRING; 6282.A0A2K6VL63; -.
DR   EnsemblMetazoa; OVOC12148.1; OVOC12148.1; WBGene00248957.
DR   Proteomes; UP000024404; 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:UP000024404};
KW   Transport {ECO:0000256|ARBA:ARBA00022448, ECO:0000256|RuleBase:RU368017}.
SQ   SEQUENCE   329 AA;  38863 MW;  47A5E0220A2C5A61 CRC64;
     MLQCSILFLG FMALNRYALA TGTRTQACIL RCSQPIYTVS VLMSTTKEGS DVVGRMDVSE
     KVGFFTKLKY RFQGIPLKGE LHAPISFMRD IGKQYIPPPL PEVPKDFKEY PERDLVNYPY
     PVKRMYPPKL RLMIIPDKFM NNFHKYTGTS GPYVFFAMLY AFLHTKGLFE IAHDRVKILV
     LLFYYYIFSR AFNYRWDKYF YESCKKAEKK YLDIIDNNFK TIRETQETSK AERSAYAAVK
     EYYPIIFKEN LALQLESTYR KNVERLATEM KRRLDYLQET EAVKHSFARD HMLKWIINSV
     QSEIMANKEN IKEKYMDICI EQLKGLSLK
//