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Database: UniProt
Entry: H2J5L7_MARPK
LinkDB: H2J5L7_MARPK
Original site: H2J5L7_MARPK 
ID   H2J5L7_MARPK            Unreviewed;       583 AA.
AC   H2J5L7;
DT   21-MAR-2012, integrated into UniProtKB/TrEMBL.
DT   21-MAR-2012, sequence version 1.
DT   27-MAR-2024, entry version 55.
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   OrderedLocusNames=Marpi_0562 {ECO:0000313|EMBL:AEX85003.1};
OS   Marinitoga piezophila (strain DSM 14283 / JCM 11233 / KA3).
OC   Bacteria; Thermotogota; Thermotogae; Petrotogales; Petrotogaceae;
OC   Marinitoga.
OX   NCBI_TaxID=443254 {ECO:0000313|EMBL:AEX85003.1, ECO:0000313|Proteomes:UP000007161};
RN   [1] {ECO:0000313|EMBL:AEX85003.1, ECO:0000313|Proteomes:UP000007161}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 14283 / JCM 11233 / KA3
RC   {ECO:0000313|Proteomes:UP000007161};
RX   PubMed=23045491; DOI=10.1128/JB.01430-12;
RA   Lucas S., Han J., Lapidus A., Cheng J.F., Goodwin L.A., Pitluck S.,
RA   Peters L., Mikhailova N., Teshima H., Detter J.C., Han C., Tapia R.,
RA   Land M., Hauser L., Kyrpides N.C., Ivanova N., Pagani I., Vannier P.,
RA   Oger P., Bartlett D.H., Noll K.M., Woyke T., Jebbar M.;
RT   "Complete Genome Sequence of the Thermophilic, Piezophilic, Heterotrophic
RT   Bacterium Marinitoga piezophila KA3.";
RL   J. Bacteriol. 194:5974-5975(2012).
RN   [2] {ECO:0000313|Proteomes:UP000007161}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 14283 / JCM 11233 / KA3
RC   {ECO:0000313|Proteomes:UP000007161};
RA   Lucas S., Han J., Lapidus A., Cheng J.-F., Goodwin L., Pitluck S.,
RA   Peters L., Mikhailova N., Teshima H., Detter J.C., Han C., Tapia R.,
RA   Land M., Hauser L., Kyrpides N., Ivanova N., Pagani I., Jebbar M.,
RA   Vannier P., Oger P., Cario A., Bartlett D., Noll K.M., Woyke T.;
RT   "Complete sequence of chromosome of Marinitoga piezophila KA3.";
RL   Submitted (JAN-2012) 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; CP003257; AEX85003.1; -; Genomic_DNA.
DR   RefSeq; WP_014296075.1; NC_016751.1.
DR   AlphaFoldDB; H2J5L7; -.
DR   STRING; 443254.Marpi_0562; -.
DR   KEGG; mpz:Marpi_0562; -.
DR   eggNOG; COG1155; Bacteria.
DR   HOGENOM; CLU_008162_3_1_0; -.
DR   OrthoDB; 9803053at2; -.
DR   Proteomes; UP000007161; Chromosome.
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:UP000007161};
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          3..65
FT                   /note="ATPase F1/V1/A1 complex alpha/beta subunit N-
FT                   terminal"
FT                   /evidence="ECO:0000259|Pfam:PF02874"
FT   DOMAIN          81..201
FT                   /note="ATPsynthase alpha/beta subunit N-terminal extension"
FT                   /evidence="ECO:0000259|Pfam:PF16886"
FT   DOMAIN          210..431
FT                   /note="ATPase F1/V1/A1 complex alpha/beta subunit
FT                   nucleotide-binding"
FT                   /evidence="ECO:0000259|Pfam:PF00006"
FT   BINDING         230..237
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00309"
SQ   SEQUENCE   583 AA;  65622 MW;  3EF688AEABE6D48C CRC64;
     MQIKEINGPV VKVKDAKTLF MNEMVRVGNY KLIGEVIGID GDIATVQVYE ETSMLKPGEP
     VESTGKMLSV ALGPGLLSSI YDGIQRPLNE LIKKSGSFIG RGIDAFGLDT NKYWEVKIIK
     KQGDLVKGGE VIAEVQETEH LVHKIMVFPN LSGKIVEIVN DGNYKVTDII AKIEDNNGNI
     HEIKLYQEWP VKVPRPVKKR LEPSIPLVTG QRVIDIFFPI SKGGTAAIPG GFGTGKTITQ
     HQLAKWSDAD IIVYIGCGER GNEMTEVLEE FPQLKDPRTG APLMNRTVLI ANTSNMPVSA
     REASIYTGIT IAEYFRDMGY NVAIMADSTS RWAEALRELS GRLEEMPAEE GYPSYLASRI
     GQFYERAGIS ENLNGTKGSI TIIGAVSPPG GDFSEPVTQN TRRFVKCFWG LDKNLAYSRH
     YPSINWLTSY SEYTEDLNDW FKENVKSDWN EYRDEAMKLL TEDDRLQQII KIVGEDVLPD
     NQKLTVLIAK MIKIGILQQS AFSEVDSYCP LEKQYYLLKI IMDTYQKAKK YVDRSIALSQ
     VLPPEIISKL LTMKEEIKEI KEFEGIEKML DEHFEKLEST YHD
//
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