ID T0R6X8_SAPDV Unreviewed; 494 AA.
AC T0R6X8;
DT 16-OCT-2013, integrated into UniProtKB/TrEMBL.
DT 16-OCT-2013, sequence version 1.
DT 27-MAR-2024, entry version 42.
DE RecName: Full=ATP synthase subunit beta {ECO:0000256|RuleBase:RU003553};
DE EC=7.1.2.2 {ECO:0000256|RuleBase:RU003553};
GN ORFNames=SDRG_01042 {ECO:0000313|EMBL:EQC42204.1}, SDRG_01043
GN {ECO:0000313|EMBL:EQC42205.1};
OS Saprolegnia diclina (strain VS20).
OC Eukaryota; Sar; Stramenopiles; Oomycota; Saprolegniales; Saprolegniaceae;
OC Saprolegnia.
OX NCBI_TaxID=1156394 {ECO:0000313|EMBL:EQC42205.1, ECO:0000313|Proteomes:UP000030762};
RN [1] {ECO:0000313|EMBL:EQC42205.1, ECO:0000313|Proteomes:UP000030762}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=VS20 {ECO:0000313|EMBL:EQC42205.1,
RC ECO:0000313|Proteomes:UP000030762};
RG The Broad Institute Genome Sequencing Platform;
RA Russ C., Nusbaum C., Tyler B., van West P., Dieguez-Uribeondo J.,
RA de Bruijn I., Tripathy S., Jiang R., Young S.K., Zeng Q., Gargeya S.,
RA Fitzgerald M., Haas B., Abouelleil A., Alvarado L., Arachchi H.M.,
RA Berlin A., Chapman S.B., Goldberg J., Griggs A., Gujja S., Hansen M.,
RA Howarth C., Imamovic A., Larimer J., McCowen C., Montmayeur A., Murphy C.,
RA Neiman D., Pearson M., Priest M., Roberts A., Saif S., Shea T., Sisk P.,
RA Sykes S., Wortman J., Nusbaum C., Birren B.;
RT "The Genome Sequence of Saprolegnia declina VS20.";
RL Submitted (APR-2012) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Produces ATP from ADP in the presence of a proton gradient
CC across the membrane. {ECO:0000256|RuleBase:RU003553}.
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|RuleBase:RU003553};
CC -!- SUBUNIT: F-type ATPases have 2 components, CF(1) - the catalytic core
CC - and CF(0) - the membrane proton channel. CF(1) has five subunits:
CC alpha(3), beta(3), gamma(1), delta(1), epsilon(1). CF(0) has three main
CC subunits: a, b and c. {ECO:0000256|RuleBase:RU003553}.
CC -!- SIMILARITY: Belongs to the ATPase alpha/beta chains family.
CC {ECO:0000256|ARBA:ARBA00008936}.
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DR EMBL; JH767133; EQC42204.1; -; Genomic_DNA.
DR EMBL; JH767133; EQC42205.1; -; Genomic_DNA.
DR RefSeq; XP_008604773.1; XM_008606551.1.
DR RefSeq; XP_008604774.1; XM_008606552.1.
DR AlphaFoldDB; T0R6X8; -.
DR STRING; 1156394.T0R6X8; -.
DR EnsemblProtists; EQC42204; EQC42204; SDRG_01042.
DR EnsemblProtists; EQC42205; EQC42205; SDRG_01043.
DR GeneID; 19941769; -.
DR GeneID; 19941770; -.
DR VEuPathDB; FungiDB:SDRG_01042; -.
DR VEuPathDB; FungiDB:SDRG_01043; -.
DR eggNOG; KOG1350; Eukaryota.
DR InParanoid; T0R6X8; -.
DR OMA; GFNMIMD; -.
DR OrthoDB; 3420200at2759; -.
DR Proteomes; UP000030762; Unassembled WGS sequence.
DR GO; GO:0045261; C:proton-transporting ATP synthase complex, catalytic core F(1); IEA:UniProtKB-KW.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016887; F:ATP hydrolysis activity; IEA:InterPro.
DR GO; GO:0046933; F:proton-transporting ATP synthase activity, rotational mechanism; IEA:UniProtKB-EC.
DR GO; GO:0046961; F:proton-transporting ATPase activity, rotational mechanism; IEA:UniProtKB-EC.
DR CDD; cd18110; ATP-synt_F1_beta_C; 1.
DR CDD; cd18115; ATP-synt_F1_beta_N; 1.
DR CDD; cd01133; F1-ATPase_beta_CD; 1.
DR Gene3D; 2.40.10.170; -; 1.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1.
DR HAMAP; MF_01347; ATP_synth_beta_bact; 1.
DR InterPro; IPR003593; AAA+_ATPase.
DR InterPro; IPR005722; ATP_synth_F1_bsu.
DR InterPro; IPR020003; ATPase_a/bsu_AS.
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; IPR024034; ATPase_F1/V1_b/a_C.
DR InterPro; IPR027417; P-loop_NTPase.
DR NCBIfam; TIGR01039; atpD; 1.
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 PIRSF; PIRSF039072; ATPase_subunit_beta; 1.
DR SMART; SM00382; AAA; 1.
DR SUPFAM; SSF47917; C-terminal domain of alpha and beta subunits of F1 ATP synthase; 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.
DR PROSITE; PS00152; ATPASE_ALPHA_BETA; 1.
PE 3: Inferred from homology;
KW ATP synthesis {ECO:0000256|ARBA:ARBA00023310,
KW ECO:0000256|RuleBase:RU003553};
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|RuleBase:RU003553};
KW CF(1) {ECO:0000256|ARBA:ARBA00023196, ECO:0000256|RuleBase:RU003553};
KW Chloroplast {ECO:0000256|ARBA:ARBA00022528};
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 ECO:0000256|RuleBase:RU003553}; Plastid {ECO:0000256|ARBA:ARBA00022528};
KW Reference proteome {ECO:0000313|Proteomes:UP000030762};
KW Translocase {ECO:0000256|ARBA:ARBA00022967};
KW Transport {ECO:0000256|ARBA:ARBA00022448}.
FT DOMAIN 159..433
FT /note="AAA+ ATPase"
FT /evidence="ECO:0000259|SMART:SM00382"
SQ SEQUENCE 494 AA; 52557 MW; 887AE9EA3063CA8F CRC64;
MLSLTRSLTR GFASSGASVG RITQIIGAVV DVQFTNNLPP ILNALEVQNT NDNIRIVLEV
AQHLGENTVR TIAMEGTDGL VRGQECVDTG NPIMVPVGPE TLGRIMNVIG EPVDERGPIH
SATKAPIHCA APLYTEQGSG AEVLVTGLKV VDLLAPYAKG GKIGLFGGAG VGKTVVIMEL
INNVANNHGG VSVFAGVGER TREGNDLYHE MIESGVIKLN ADGTTTGSKA ALVYGQMNEP
PGARARVGLT GLTVAEYFRD VEGQDVLLFV DNIFRFTQAC SEVSALLGRI PSAVGYQPTL
ATDLGALQER ITSTLKGSIT SVQAIYVPAD DLTDPAPATT FSHLDATTVL SRQISELGIY
PAVDPLDSKS RMLDPRVIGD EHYEVARATQ KLLQDYKGLQ DIIAILGMDE LSEDDKLTVA
RARKVQKFMS QPLHVAEVFT GKPGKFVALA ETVSSFKAIL AGEYDDLPEA AFFMVGGIEE
VKEKAKALAS ELDE
//
