ID V4LAY0_EUTSA Unreviewed; 271 AA.
AC V4LAY0;
DT 22-JAN-2014, integrated into UniProtKB/TrEMBL.
DT 22-JAN-2014, sequence version 1.
DT 27-MAR-2024, entry version 40.
DE RecName: Full=H(+)-transporting two-sector ATPase {ECO:0000256|ARBA:ARBA00012473};
DE EC=7.1.2.2 {ECO:0000256|ARBA:ARBA00012473};
DE Flags: Fragment;
GN ORFNames=EUTSA_v100131680mg {ECO:0000313|EMBL:ESQ40829.1};
OS Eutrema salsugineum (Saltwater cress) (Sisymbrium salsugineum).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; malvids; Brassicales; Brassicaceae; Eutremeae; Eutrema.
OX NCBI_TaxID=72664 {ECO:0000313|EMBL:ESQ40829.1, ECO:0000313|Proteomes:UP000030689};
RN [1] {ECO:0000313|EMBL:ESQ40829.1, ECO:0000313|Proteomes:UP000030689}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=23518688; DOI=10.3389/fpls.2013.00046;
RA Yang R., Jarvis D.E., Chen H., Beilstein M.A., Grimwood J., Jenkins J.,
RA Shu S., Prochnik S., Xin M., Ma C., Schmutz J., Wing R.A.,
RA Mitchell-Olds T., Schumaker K.S., Wang X.;
RT "The Reference Genome of the Halophytic Plant Eutrema salsugineum.";
RL Front. Plant Sci. 4:46-46(2013).
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. Subunits alpha and
CC beta form the catalytic core in F(1). Rotation of the central stalk
CC against the surrounding alpha(3)beta(3) subunits leads to hydrolysis of
CC ATP in three separate catalytic sites on the beta subunits.
CC {ECO:0000256|ARBA:ARBA00003086}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + 4 H(+)(in) + H2O = ADP + 5 H(+)(out) + phosphate;
CC Xref=Rhea:RHEA:57720, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:456216; EC=7.1.2.2;
CC Evidence={ECO:0000256|ARBA:ARBA00001741};
CC -!- SIMILARITY: Belongs to the ATPase alpha/beta chains family.
CC {ECO:0000256|ARBA:ARBA00008936}.
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DR EMBL; KI517464; ESQ40829.1; -; Genomic_DNA.
DR RefSeq; XP_006399376.1; XM_006399313.1.
DR AlphaFoldDB; V4LAY0; -.
DR STRING; 72664.V4LAY0; -.
DR GeneID; 18019002; -.
DR KEGG; eus:EUTSA_v100131680m; -.
DR OrthoDB; 669029at2759; -.
DR Proteomes; UP000030689; Unassembled WGS sequence.
DR GO; GO:0000275; C:mitochondrial proton-transporting ATP synthase complex, catalytic sector F(1); IEA:EnsemblPlants.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016887; F:ATP hydrolysis activity; IEA:InterPro.
DR GO; GO:0006754; P:ATP biosynthetic process; IEA:InterPro.
DR GO; GO:1902600; P:proton transmembrane transport; IEA:UniProtKB-KW.
DR CDD; cd18115; ATP-synt_F1_beta_N; 1.
DR Gene3D; 2.40.10.170; -; 1.
DR Gene3D; 1.10.10.910; ATP synthase, F1 beta subunit; 1.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1.
DR InterPro; IPR042079; ATP_synt_F1_beta_sf.
DR InterPro; IPR020971; ATP_synth_F1_beta_su.
DR InterPro; IPR004100; ATPase_F1/V1/A1_a/bsu_N.
DR InterPro; IPR036121; ATPase_F1/V1/A1_a/bsu_N_sf.
DR InterPro; IPR000194; ATPase_F1/V1/A1_a/bsu_nucl-bd.
DR InterPro; IPR027417; P-loop_NTPase.
DR PANTHER; PTHR15184; ATP SYNTHASE; 1.
DR PANTHER; PTHR15184:SF71; ATP SYNTHASE SUBUNIT BETA, MITOCHONDRIAL; 1.
DR Pfam; PF00006; ATP-synt_ab; 1.
DR Pfam; PF02874; ATP-synt_ab_N; 1.
DR Pfam; PF11421; Synthase_beta; 1.
DR SUPFAM; SSF50615; N-terminal domain of alpha and beta subunits of F1 ATP synthase; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
PE 3: Inferred from homology;
KW ATP synthesis {ECO:0000256|ARBA:ARBA00023310};
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW CF(1) {ECO:0000256|ARBA:ARBA00023196};
KW Hydrogen ion transport {ECO:0000256|ARBA:ARBA00022781};
KW Ion transport {ECO:0000256|ARBA:ARBA00023065};
KW Membrane {ECO:0000256|ARBA:ARBA00023136};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Reference proteome {ECO:0000313|Proteomes:UP000030689};
KW Transit peptide {ECO:0000256|ARBA:ARBA00022946};
KW Translocase {ECO:0000256|ARBA:ARBA00022967};
KW Transport {ECO:0000256|ARBA:ARBA00022448}.
FT DOMAIN 1..47
FT /note="ATP synthase F1 beta subunit"
FT /evidence="ECO:0000259|Pfam:PF11421"
FT DOMAIN 86..154
FT /note="ATPase F1/V1/A1 complex alpha/beta subunit N-
FT terminal"
FT /evidence="ECO:0000259|Pfam:PF02874"
FT DOMAIN 211..270
FT /note="ATPase F1/V1/A1 complex alpha/beta subunit
FT nucleotide-binding"
FT /evidence="ECO:0000259|Pfam:PF00006"
FT REGION 1..72
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..21
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT NON_TER 271
FT /evidence="ECO:0000313|EMBL:ESQ40829.1"
SQ SEQUENCE 271 AA; 28454 MW; B592282C936BC070 CRC64;
MASRRVLSSL LRSSSGRSAA KFGSRSPRIP SPSPARCASP FGDLLGRVAE YSTSSPASSA
APSSAPAKDE GKKTYDYGGK GAIGKVCQVI GAIVDVRFED QEGLPPIMTS LEVQDHPTRL
VLEVSHHLGQ NVVRTIAMDG TEGLVRGRRV LNTGAPITVP VGRATLGRIM NVLGEPIDER
GEIKTDHYLP IHRDAPALVD LATGQEILAT GIKVVDLLAP YQRGGKIGLF GGAGVGKTVL
IMELINNVAK AHGGFSVFAG VGERTREGND L
//
