ID A0A1C7GZE3_9BACE Unreviewed; 586 AA.
AC A0A1C7GZE3;
DT 30-NOV-2016, integrated into UniProtKB/TrEMBL.
DT 30-NOV-2016, sequence version 1.
DT 24-JAN-2024, entry version 30.
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=A4V03_10545 {ECO:0000313|EMBL:ANU57958.1};
OS Bacteroides caecimuris.
OC Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Bacteroidaceae;
OC Bacteroides.
OX NCBI_TaxID=1796613 {ECO:0000313|EMBL:ANU57958.1, ECO:0000313|Proteomes:UP000092631};
RN [1] {ECO:0000313|Proteomes:UP000092631}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=I48 {ECO:0000313|Proteomes:UP000092631};
RA Uchimura Y., Wyss M., Brugiroux S., Limenitakis J.P., Stecher B.,
RA McCoy K.D., Macpherson A.J.;
RT "Complete Genome Sequences of Twelve Strains of a Stable Defined Moderately
RT Diverse Mouse Microbiota 2 (sDMDMm2).";
RL Submitted (APR-2016) 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}.
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DR EMBL; CP015401; ANU57958.1; -; Genomic_DNA.
DR RefSeq; WP_065538897.1; NZ_NHMU01000009.1.
DR AlphaFoldDB; A0A1C7GZE3; -.
DR GeneID; 82187582; -.
DR KEGG; bcae:A4V03_10545; -.
DR OrthoDB; 9803053at2; -.
DR Proteomes; UP000092631; Chromosome.
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; cd01426; ATP-synt_F1_V1_A1_AB_FliI_N; 1.
DR CDD; cd01134; V_A-ATPase_A; 1.
DR Gene3D; 2.30.30.650; -; 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; IPR020003; ATPase_a/bsu_AS.
DR InterPro; IPR004100; ATPase_F1/V1/A1_a/bsu_N.
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; 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:UP000092631};
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 15..71
FT /note="ATPase F1/V1/A1 complex alpha/beta subunit N-
FT terminal"
FT /evidence="ECO:0000259|Pfam:PF02874"
FT DOMAIN 87..205
FT /note="ATPsynthase alpha/beta subunit N-terminal extension"
FT /evidence="ECO:0000259|Pfam:PF16886"
FT DOMAIN 215..436
FT /note="ATPase F1/V1/A1 complex alpha/beta subunit
FT nucleotide-binding"
FT /evidence="ECO:0000259|Pfam:PF00006"
FT BINDING 235..242
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00309"
SQ SEQUENCE 586 AA; 66052 MW; 51918BA9E48610A6 CRC64;
MATKGTVSGV IANMVTLVVD GPVAQNEICY ISTGGDKLMA EVIKVVGSHV YVQVFESTRG
LKVGAEAEFT GHMLEVTLGP GMLSKNYDGL QNDLDKMDGV FLKRGQYTYP LDKERIWHFV
PLANVGDKVQ ASAWLGQVDE NFQPLKIMAP FTMKGTATVK TIMPEGDYKI EDTIAILTDE
EGNDISVTMI QRWPVKRAMT NYKEKPRPFK LLETGVRVID TLNPIVEGGT GFIPGPFGTG
KTVLQHAISK QAEADIVIIA ACGERANEVV EIFTEFPELV DPHTGRKLME RTIIIANTSN
MPVAAREASV YTAMTLAEYY RSMGLKVLLM ADSTSRWAQA LREMSNRMEE LPGPDAFPMD
ISAIISNFYG RAGYVKLNND ETGSITFIGT VSPAGGNLKE PVTENTKKVA RCFYALEQDR
ADKKRYPAVN PIDSYSKYIE YPEFEEYIKG HINGEWIRKV NELKTRLQRG KEIAEQINIL
GDDGVPVEYH VIFWKSELID FVILQQDAFD EIDAVTPMER QEDILNMVID ICHTEFEFDN
FNEVMDYFKK IINICKQMNY SKFKSEQYEG FQKQLKELIE ERKLQS
//
