GenomeNet

Database: UniProt
Entry: F3ANI0_9FIRM
LinkDB: F3ANI0_9FIRM
Original site: F3ANI0_9FIRM 
ID   F3ANI0_9FIRM            Unreviewed;       588 AA.
AC   F3ANI0;
DT   28-JUN-2011, integrated into UniProtKB/TrEMBL.
DT   28-JUN-2011, sequence version 1.
DT   24-JAN-2024, entry version 48.
DE   RecName: Full=V-type ATP synthase alpha chain {ECO:0000256|HAMAP-Rule:MF_00309};
DE            EC=7.1.2.2 {ECO:0000256|HAMAP-Rule:MF_00309};
DE   AltName: Full=V-ATPase subunit A {ECO:0000256|HAMAP-Rule:MF_00309};
GN   Name=atpA {ECO:0000256|HAMAP-Rule:MF_00309};
GN   ORFNames=HMPREF0987_01983 {ECO:0000313|EMBL:EGG89867.1};
OS   Lachnospiraceae bacterium 9_1_43BFAA.
OC   Bacteria; Bacillota; Clostridia; Eubacteriales; Lachnospiraceae.
OX   NCBI_TaxID=658088 {ECO:0000313|EMBL:EGG89867.1, ECO:0000313|Proteomes:UP000003620};
RN   [1] {ECO:0000313|EMBL:EGG89867.1, ECO:0000313|Proteomes:UP000003620}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=9_1_43BFAA {ECO:0000313|EMBL:EGG89867.1,
RC   ECO:0000313|Proteomes:UP000003620};
RG   The Broad Institute Genome Sequencing Platform;
RA   Earl A., Ward D., Feldgarden M., Gevers D., Daigneault M., Strauss J.,
RA   Ambrose C., Allen-Vercoe E., Young S.K., Zeng Q., Gargeya S.,
RA   Fitzgerald M., Haas B., Abouelleil A., Alvarado L., Arachchi H.M.,
RA   Berlin A., Brown A., Chapman S.B., Chen Z., Dunbar C., Freedman E.,
RA   Gearin G., Gellesch M., Goldberg J., Griggs A., Gujja S., Heilman E.R.,
RA   Heiman D., Howarth C., Larson L., Lui A., MacDonald P.J.P., Mehta T.,
RA   Montmayeur A., Murphy C., Neiman D., Pearson M., Priest M., Roberts A.,
RA   Saif S., Shea T., Shenoy N., Sisk P., Stolte C., Sykes S., White J.,
RA   Yandava C., Wortman J., Nusbaum C., Birren B.;
RT   "The Genome Sequence of Lachnospiraceae bacterium 9_1_43BFAA.";
RL   Submitted (MAR-2011) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Produces ATP from ADP in the presence of a proton gradient
CC       across the membrane. The V-type alpha chain is a catalytic subunit.
CC       {ECO:0000256|HAMAP-Rule:MF_00309}.
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|HAMAP-Rule:MF_00309};
CC   -!- SIMILARITY: Belongs to the ATPase alpha/beta chains family.
CC       {ECO:0000256|ARBA:ARBA00008936, ECO:0000256|HAMAP-Rule:MF_00309}.
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:EGG89867.1}.
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; ACTX01000011; EGG89867.1; -; Genomic_DNA.
DR   AlphaFoldDB; F3ANI0; -.
DR   eggNOG; COG1155; Bacteria.
DR   HOGENOM; CLU_008162_3_1_9; -.
DR   Proteomes; UP000003620; Unassembled WGS sequence.
DR   GO; GO:0045259; C:proton-transporting ATP synthase complex; IEA:UniProt.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0046933; F:proton-transporting ATP synthase activity, rotational mechanism; IEA:UniProtKB-UniRule.
DR   GO; GO:0046961; F:proton-transporting ATPase activity, rotational mechanism; IEA:UniProtKB-EC.
DR   GO; GO:0042777; P:proton motive force-driven plasma membrane ATP synthesis; IEA:UniProtKB-UniRule.
DR   CDD; cd18111; ATP-synt_V_A-type_alpha_C; 1.
DR   CDD; cd01134; V_A-ATPase_A; 1.
DR   Gene3D; 2.40.30.20; -; 1.
DR   Gene3D; 2.40.50.100; -; 1.
DR   Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1.
DR   HAMAP; MF_00309; ATP_synth_A_arch; 1.
DR   InterPro; IPR031686; ATP-synth_a_Xtn.
DR   InterPro; IPR023366; ATP_synth_asu-like_sf.
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   InterPro; IPR022878; V-ATPase_asu.
DR   PANTHER; PTHR43607; V-TYPE PROTON ATPASE CATALYTIC SUBUNIT A; 1.
DR   PANTHER; PTHR43607:SF1; V-TYPE PROTON ATPASE CATALYTIC SUBUNIT A; 1.
DR   Pfam; PF00006; ATP-synt_ab; 1.
DR   Pfam; PF02874; ATP-synt_ab_N; 1.
DR   Pfam; PF16886; ATP-synt_ab_Xtn; 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|HAMAP-Rule:MF_00309};
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|HAMAP-
KW   Rule:MF_00309}; Hydrogen ion transport {ECO:0000256|HAMAP-Rule:MF_00309};
KW   Ion transport {ECO:0000256|ARBA:ARBA00023065, ECO:0000256|HAMAP-
KW   Rule:MF_00309};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|HAMAP-
KW   Rule:MF_00309}; Reference proteome {ECO:0000313|Proteomes:UP000003620};
KW   Translocase {ECO:0000256|ARBA:ARBA00022967, ECO:0000256|HAMAP-
KW   Rule:MF_00309};
KW   Transport {ECO:0000256|ARBA:ARBA00022448, ECO:0000256|HAMAP-Rule:MF_00309}.
FT   DOMAIN          7..69
FT                   /note="ATPase F1/V1/A1 complex alpha/beta subunit N-
FT                   terminal"
FT                   /evidence="ECO:0000259|Pfam:PF02874"
FT   DOMAIN          85..204
FT                   /note="ATPsynthase alpha/beta subunit N-terminal extension"
FT                   /evidence="ECO:0000259|Pfam:PF16886"
FT   DOMAIN          214..435
FT                   /note="ATPase F1/V1/A1 complex alpha/beta subunit
FT                   nucleotide-binding"
FT                   /evidence="ECO:0000259|Pfam:PF00006"
FT   BINDING         234..241
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00309"
SQ   SEQUENCE   588 AA;  65506 MW;  2684A45B2E5B08D5 CRC64;
     MLRTGKIYGI NGPVVYLKGN TGFKMSEMVY VGKERLVGEV IALDKERTTI QVFEETTGLR
     PGETVEASGD AISVTLAPGI LNNIFDGIER PLERIAENSG AYISRGVSVD SLDKTKKWST
     HMTVSVGDEV HGGHIIAEVP ETAAIVHKCM VPPNISGMIT KVVPDGEYTI DEPLVTVELE
     SGKTIDLTMT QKWPIRVPRP THHRFPASKP LVTGQRILDT MFPIAKGGTA CVPGGFGTGK
     TMTQHQIAKW SDADIIIYIG CGERGNEMTQ VLEEFTQLVD PKSGNPLMDR TTLIANTSNM
     PVAAREASLY AGLTLAEYYR DMGYDVAIMA DSTSRWAEAL RELSGRLEEM PAEEGFPAYL
     ASRLSAFYER AGMMHNLNGT DGSVSIIGAV SPQGGDFSEP VTQNTKRFVR CFWGLDKSLA
     YSRHFPAIHW LTSYSEYLMD LAPWYAKHVS DKFIDYRNQM MALLNQESSL MEIVKLIGSD
     VLPDDQKLVL EIAKVIRLGF LQQNAFHADD TCVSLEKQFK MMEVILHLYD KSKALITMGM
     PISVLKEEDI FERVIAIKYD VPNDKLEMFD DYMKAIDQFY DRIMEKNA
//
DBGET integrated database retrieval system