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Database: UniProt
Entry: C7P2T0_HALMD
LinkDB: C7P2T0_HALMD
Original site: C7P2T0_HALMD 
ID   C7P2T0_HALMD            Unreviewed;       586 AA.
AC   C7P2T0;
DT   13-OCT-2009, integrated into UniProtKB/TrEMBL.
DT   13-OCT-2009, sequence version 1.
DT   27-MAR-2024, entry version 77.
DE   RecName: Full=V-type ATP synthase alpha chain {ECO:0000256|ARBA:ARBA00018003, ECO:0000256|HAMAP-Rule:MF_00309};
DE            EC=7.1.2.2 {ECO:0000256|ARBA:ARBA00012473, ECO:0000256|HAMAP-Rule:MF_00309};
DE   AltName: Full=V-ATPase subunit A {ECO:0000256|ARBA:ARBA00031719, ECO:0000256|HAMAP-Rule:MF_00309};
GN   Name=atpA {ECO:0000256|HAMAP-Rule:MF_00309};
GN   OrderedLocusNames=Hmuk_1281 {ECO:0000313|EMBL:ACV47402.1};
OS   Halomicrobium mukohataei (strain ATCC 700874 / DSM 12286 / JCM 9738 / NCIMB
OS   13541) (Haloarcula mukohataei).
OC   Archaea; Euryarchaeota; Stenosarchaea group; Halobacteria; Halobacteriales;
OC   Haloarculaceae; Halomicrobium.
OX   NCBI_TaxID=485914 {ECO:0000313|EMBL:ACV47402.1, ECO:0000313|Proteomes:UP000001746};
RN   [1] {ECO:0000313|EMBL:ACV47402.1, ECO:0000313|Proteomes:UP000001746}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 700874 / DSM 12286 / JCM 9738 / NCIMB 13541
RC   {ECO:0000313|Proteomes:UP000001746};
RX   PubMed=21304667; DOI=10.4056/sigs.42644;
RA   Tindall B.J., Schneider S., Lapidus A., Copeland A., Glavina Del Rio T.,
RA   Nolan M., Lucas S., Chen F., Tice H., Cheng J.F., Saunders E., Bruce D.,
RA   Goodwin L., Pitluck S., Mikhailova N., Pati A., Ivanova N., Mavrommatis K.,
RA   Chen A., Palaniappan K., Chain P., Land M., Hauser L., Chang Y.J.,
RA   Jeffries C.D., Brettin T., Han C., Rohde M., Goker M., Bristow J.,
RA   Eisen J.A., Markowitz V., Hugenholtz P., Klenk H.P., Kyrpides N.C.,
RA   Detter J.C.;
RT   "Complete genome sequence of Halomicrobium mukohataei type strain (arg-
RT   2).";
RL   Stand. Genomic Sci. 1:270-277(2009).
CC   -!- FUNCTION: Produces ATP from ADP in the presence of a proton gradient
CC       across the membrane. The archaeal alpha chain is a catalytic subunit.
CC       {ECO:0000256|ARBA:ARBA00003912, 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|ARBA:ARBA00001741, ECO:0000256|HAMAP-
CC         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; CP001688; ACV47402.1; -; Genomic_DNA.
DR   RefSeq; WP_015762248.1; NC_013202.1.
DR   AlphaFoldDB; C7P2T0; -.
DR   STRING; 485914.Hmuk_1281; -.
DR   GeneID; 8410801; -.
DR   KEGG; hmu:Hmuk_1281; -.
DR   eggNOG; arCOG00868; Archaea.
DR   HOGENOM; CLU_008162_3_1_2; -.
DR   OrthoDB; 115235at2157; -.
DR   Proteomes; UP000001746; Chromosome.
DR   GO; GO:0033178; C:proton-transporting two-sector ATPase complex, catalytic domain; IEA:InterPro.
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; IPR005726; ATP_synth_asu_arc.
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; IPR001763; Rhodanese-like_dom.
DR   InterPro; IPR022878; V-ATPase_asu.
DR   NCBIfam; TIGR01043; ATP_syn_A_arch; 1.
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.
DR   PROSITE; PS50206; RHODANESE_3; 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:UP000001746};
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          320..349
FT                   /note="Rhodanese"
FT                   /evidence="ECO:0000259|PROSITE:PS50206"
FT   BINDING         238..245
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00309"
SQ   SEQUENCE   586 AA;  64821 MW;  5746F6B39D1E6366 CRC64;
     MSQATESDVR EDGVIDSVSG PVVTATGLDA RMNDVVYVGS EGLMGEVIEI EGDITTIQVY
     EETSDVSPGE PVEGTGSPLS VDLGPGMLDA IYDGVQRPLD VLEEKMGSPY LDRGVDAPGI
     DLEKTWEFEP EVEAGDEVSS GDIVGTVPET PSIDHKVMVP PDSDGGEVVA AESGNFTVEE
     PVVELDTGEE IQMRQEWPVR QQRPSEEKQT PTTPLISGQR VLDGLFPIAK GGTAAIPGPF
     GSGKTVTQHQ LAKWADADIV VYVGCGERGN EMTEVIEDFP ELEDPTTGNA LMDRTCLIAN
     TSNMPVAARE SCVYTGITIA EYFRDMGYDV ALMADSTSRW AEAMREISSR LEEMPGEEGY
     PAYLAARLSE FYERAGYFQN INGSEGSVSV IGAVSPPGGD FSEPVTQNTL RIVKTFWALD
     ADLAERRHFP SINWNESYSL YRDQLDPWFV ENVRDDWPEK RQWGIDTLDE EAELQEIVQL
     VGKDALPEDQ QLTLEVARYL REAWLQQNAF HPTDTYCEPE KTYRILDAIK TYNDEAFDAL
     DAGVPVEELT DLETVPRLNR IGVQEEYNEY IDELEADIES EIQELY
//
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