ID A0A1V1SQV0_9PEZI Unreviewed; 243 AA.
AC A0A1V1SQV0;
DT 07-JUN-2017, integrated into UniProtKB/TrEMBL.
DT 07-JUN-2017, sequence version 1.
DT 18-JUN-2025, entry version 19.
DE RecName: Full=ATP synthase subunit 4 {ECO:0000256|RuleBase:RU368017};
GN ORFNames=ANO14919_003140 {ECO:0000313|EMBL:GAW10976.1};
OS Xylariales sp. No.14919.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Xylariomycetidae; Xylariales.
OX NCBI_TaxID=1813822 {ECO:0000313|EMBL:GAW10976.1, ECO:0000313|Proteomes:UP000189293};
RN [1] {ECO:0000313|EMBL:GAW10976.1, ECO:0000313|Proteomes:UP000189293}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=No.14919 {ECO:0000313|EMBL:GAW10976.1,
RC ECO:0000313|Proteomes:UP000189293};
RG Technology Reseach Association of Highly Efficient Gene Design;
RA Itoh H., Matsui M., Shibata T.;
RL Submitted (FEB-2017) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:GAW10976.1, ECO:0000313|Proteomes:UP000189293}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=No.14919 {ECO:0000313|EMBL:GAW10976.1,
RC ECO:0000313|Proteomes:UP000189293};
RA Itoh H., Matsui M., Kumagai T., Arita M., Machida M., Shibata T.;
RT "Genome Sequence of Fungus Strain No.14919 Producing HMG-CoA Reductase
RT Inhibitor FR901512.";
RL Submitted (MAR-2017) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Subunit b, of the mitochondrial membrane ATP synthase complex
CC (F(1)F(0) ATP synthase or Complex V) that produces ATP from ADP in the
CC presence of a proton gradient across the membrane which is generated by
CC electron transport complexes of the respiratory chain. ATP synthase
CC complex consist of a soluble F(1) head domain - the catalytic core
CC - and a membrane F(1) domain - the membrane proton channel. These two
CC domains are linked by a central stalk rotating inside the F(1) region
CC and a stationary peripheral stalk. During catalysis, ATP synthesis in
CC the catalytic domain of F(1) is coupled via a rotary mechanism of the
CC central stalk subunits to proton translocation. In vivo, can only
CC synthesize ATP although its ATP hydrolase activity can be activated
CC artificially in vitro. Part of the complex F(0) domain. Part of the
CC complex F(0) domain and the peripheric stalk, which acts as a stator to
CC hold 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. 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. {ECO:0000256|ARBA:ARBA00062152, 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}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:GAW10976.1}.
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DR EMBL; BDMC01000001; GAW10976.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1V1SQV0; -.
DR STRING; 1813822.A0A1V1SQV0; -.
DR OrthoDB; 67388at2759; -.
DR Proteomes; UP000189293; Unassembled WGS sequence.
DR GO; GO:0005743; C:mitochondrial inner membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0045259; C:proton-transporting ATP synthase complex; IEA:UniProtKB-KW.
DR GO; GO:0046933; F:proton-transporting ATP synthase activity, rotational mechanism; IEA:TreeGrafter.
DR FunFam; 1.20.5.2210:FF:000002; ATP synthase subunit 4 mitochondrial; 1.
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:UP000189293};
KW Transport {ECO:0000256|ARBA:ARBA00022448, ECO:0000256|RuleBase:RU368017}.
SQ SEQUENCE 243 AA; 26271 MW; 11C95949DD59FCA7 CRC64;
MASRMATRAL GAARVRPTIS PRAVVPAVTS SLTASRSASN VPEPKAKAQS LVDSLPGNSL
ISKTAILSSA AGLSVYAISS EYYVVNEESV VAFCLLSVWG ALIKFGGPMY KEWAQAQNEK
IKGILNAARV DHTQAVKNRI DNVQQMGGVV DVTKALFEVS KETAQLEAKA YELEQTTALA
AEAKAVLDSW VRYEGQVKQR QQRELAESVI AKVKKELENP KALQQILQQS VSDVERIISS
KAQ
//
