GenomeNet

Database: UniProt
Entry: A0A1C7LXA2_GRIFR
LinkDB: A0A1C7LXA2_GRIFR
Original site: A0A1C7LXA2_GRIFR 
ID   A0A1C7LXA2_GRIFR        Unreviewed;       556 AA.
AC   A0A1C7LXA2;
DT   30-NOV-2016, integrated into UniProtKB/TrEMBL.
DT   30-NOV-2016, sequence version 1.
DT   27-MAR-2024, entry version 24.
DE   RecName: Full=ATP synthase subunit beta {ECO:0000256|RuleBase:RU003553};
DE            EC=7.1.2.2 {ECO:0000256|RuleBase:RU003553};
GN   Name=atp2 {ECO:0000313|EMBL:OBZ69323.1};
GN   ORFNames=A0H81_10946 {ECO:0000313|EMBL:OBZ69323.1};
OS   Grifola frondosa (Maitake) (Polyporus frondosus).
OC   Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC   Polyporales; Grifolaceae; Grifola.
OX   NCBI_TaxID=5627 {ECO:0000313|EMBL:OBZ69323.1, ECO:0000313|Proteomes:UP000092993};
RN   [1] {ECO:0000313|EMBL:OBZ69323.1, ECO:0000313|Proteomes:UP000092993}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=9006-11 {ECO:0000313|EMBL:OBZ69323.1,
RC   ECO:0000313|Proteomes:UP000092993};
RA   Min B., Park H., Kim J.-G., Cho H., Oh Y.-L., Kong W.-S., Choi I.-G.;
RT   "Whole genome sequencing of Grifola frondosa 9006-11.";
RL   Submitted (MAR-2016) 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}.
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:OBZ69323.1}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; LUGG01000018; OBZ69323.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1C7LXA2; -.
DR   STRING; 5627.A0A1C7LXA2; -.
DR   OMA; GFNMIMD; -.
DR   OrthoDB; 3420200at2759; -.
DR   Proteomes; UP000092993; 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   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};
KW   Reference proteome {ECO:0000313|Proteomes:UP000092993};
KW   Translocase {ECO:0000256|ARBA:ARBA00022967};
KW   Transport {ECO:0000256|ARBA:ARBA00022448}.
FT   DOMAIN          194..377
FT                   /note="AAA+ ATPase"
FT                   /evidence="ECO:0000259|SMART:SM00382"
SQ   SEQUENCE   556 AA;  59809 MW;  41A922D080B49DA3 CRC64;
     MLTARGVHRL SRRALNSAKR TNAFFSTAAA APVIARAASI PSSSQRVHAR PARASAQPAR
     SYATEATVAT GHVKTVIGAV VDVTDFHGGR LVLEVAAHLG ENSVRTIAMD GTEGLVRGQK
     VVDTGAPIKI PVGTATLGRI MNVIGEPIDE RGPIKGVKLL PIHAEPPPFV DQSTTAEVLE
     TGIKVVDLLA PYARGGKIGL FGGAGVGKTV LIQELINNVA KAHGGFSIFC GVGERTREGN
     DLYHEMIETG VIKLEGDSKV ALVFGQMNEP PGARARVALT GLTIAEYFRD EEGQDVLLFI
     DNIFRFTQAG SEVSALLGRI PSAVGYQPTL STDMGGMQER ITTTKKGSIT SVQAVYVPAD
     DLTDPAPATT FAHLDATTVL SRSIAELGIY PAVDPLDSKS RMLDPRIVGL EHYEVATAVQ
     KILQDYKSLQ DIIAILGMDE LSEEDKLTVE RARKIQRFMS QPFAVAQVFT GYEGKLVPLK
     DTVRSFKEIL SGAHDNLPES AFYMVGTIED VKTKAEQLAK EWASRHDRSD SVDGLVERWI
     VGLEPFYLRP GTPPIK
//
DBGET integrated database retrieval system