ID U2PZG0_9CLOT Unreviewed; 591 AA.
AC U2PZG0;
DT 13-NOV-2013, integrated into UniProtKB/TrEMBL.
DT 13-NOV-2013, sequence version 1.
DT 03-MAY-2023, entry version 38.
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=CINTURNW_0935 {ECO:0000313|EMBL:ERK31910.1};
OS Clostridium intestinale URNW.
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Clostridiaceae;
OC Clostridium.
OX NCBI_TaxID=1294142 {ECO:0000313|EMBL:ERK31910.1, ECO:0000313|Proteomes:UP000016721};
RN [1] {ECO:0000313|EMBL:ERK31910.1, ECO:0000313|Proteomes:UP000016721}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=URNW {ECO:0000313|EMBL:ERK31910.1,
RC ECO:0000313|Proteomes:UP000016721};
RX PubMed=24136853;
RA Lal S., Ramachandran U., Zhang X., Sparling R., Levin D.B.;
RT "Draft Genome Sequence of the Hydrogen- and Ethanol-Producing Bacterium
RT Clostridium intestinale Strain URNW.";
RL Genome Announc. 1:e00871-13(2013).
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:ERK31910.1}.
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; APJA01000009; ERK31910.1; -; Genomic_DNA.
DR RefSeq; WP_021800970.1; NZ_KI273145.1.
DR AlphaFoldDB; U2PZG0; -.
DR STRING; 1294142.CINTURNW_0935; -.
DR PATRIC; fig|1294142.3.peg.934; -.
DR eggNOG; COG1155; Bacteria.
DR HOGENOM; CLU_008162_3_1_9; -.
DR OrthoDB; 9803053at2; -.
DR Proteomes; UP000016721; 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:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
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; cd18119; ATP-synt_V_A-type_alpha_N; 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; 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.
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 Hydrolase {ECO:0000313|EMBL:ERK31910.1};
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:UP000016721};
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 6..68
FT /note="ATPase F1/V1/A1 complex alpha/beta subunit N-
FT terminal"
FT /evidence="ECO:0000259|Pfam:PF02874"
FT DOMAIN 84..203
FT /note="ATPsynthase alpha/beta subunit N-terminal extension"
FT /evidence="ECO:0000259|Pfam:PF16886"
FT DOMAIN 212..435
FT /note="ATPase F1/V1/A1 complex alpha/beta subunit
FT nucleotide-binding"
FT /evidence="ECO:0000259|Pfam:PF00006"
FT BINDING 232..239
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00309"
SQ SEQUENCE 591 AA; 64857 MW; 929E95BA64A2669E CRC64;
MKTGSIIKVS GPLVVAEGMD EANVYDVCKV GAKGLIGEII EMRGDKASIQ VYEETSGIGP
GDPVVTTGEP LSVELGPGLI ESMFDGIQRP LDAFMEAANS SFLVKGISIP SLNREKVWGF
NPTVSVGDEV DAGDVIGTVQ ESPVVLHKIM VPYGLKGKVK EIKEGEFTIT DVICVLETEK
GDKEVSMLQK WPVRKGRPYA RKLNPVEPMV TGQRVVDTFF PVAKGGAAAV PGPFGAGKTV
VQHQIAKWGD TEIVVYVGCG ERGNEMTDVL NEFPELKDPR TGESLMKRTV LIANTSNMPV
AAREASIYTG ITIAEYFRDM GYSVAIMADS TSRWAEALRE MSGRLEEMPG DEGYPAYLGS
RLADYYERAG KVVCLGNEGR QGAITAIGAV SPPGGDISEP VTQSTLRIVK VFWGLDAQLA
YRRHFPSVNW LSSYSLYLEK MGVWMNDNVA PDWSKIRTDA MALLQEEASL DEIVRLIGID
ALSEKDRLKL EVAKSIREDY LQQNAFHEVD TYASLDKQYK MLKLILKFYD EAIRALEVGV
YLDKILALEV RDKIARSKYI AEEEILKMDD ISNELNKAVT DLINEGGVLN A
//
