(data stored in ACNUC10043 zone)

SWISSPROT: VATA_METKA

ID   VATA_METKA              Reviewed;         592 AA.
AC   Q8TWL6;
DT   26-JUL-2002, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2002, sequence version 1.
DT   11-DEC-2019, entry version 107.
DE   RecName: Full=V-type ATP synthase alpha chain {ECO:0000255|HAMAP-Rule:MF_00309};
DE            EC=7.1.2.2 {ECO:0000255|HAMAP-Rule:MF_00309};
DE   AltName: Full=V-ATPase subunit A {ECO:0000255|HAMAP-Rule:MF_00309};
GN   Name=atpA {ECO:0000255|HAMAP-Rule:MF_00309}; OrderedLocusNames=MK1017;
OS   Methanopyrus kandleri (strain AV19 / DSM 6324 / JCM 9639 / NBRC 100938).
OC   Archaea; Euryarchaeota; Methanopyri; Methanopyrales; Methanopyraceae;
OC   Methanopyrus.
OX   NCBI_TaxID=190192;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=AV19 / DSM 6324 / JCM 9639 / NBRC 100938;
RX   PubMed=11930014; DOI=10.1073/pnas.032671499;
RA   Slesarev A.I., Mezhevaya K.V., Makarova K.S., Polushin N.N.,
RA   Shcherbinina O.V., Shakhova V.V., Belova G.I., Aravind L., Natale D.A.,
RA   Rogozin I.B., Tatusov R.L., Wolf Y.I., Stetter K.O., Malykh A.G.,
RA   Koonin E.V., Kozyavkin S.A.;
RT   "The complete genome of hyperthermophile Methanopyrus kandleri AV19 and
RT   monophyly of archaeal methanogens.";
RL   Proc. Natl. Acad. Sci. U.S.A. 99:4644-4649(2002).
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:0000255|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:0000255|HAMAP-Rule:MF_00309};
CC   -!- SIMILARITY: Belongs to the ATPase alpha/beta chains family.
CC       {ECO:0000255|HAMAP-Rule:MF_00309}.
DR   EMBL; AE009439; AAM02230.1; -; Genomic_DNA.
DR   SMR; Q8TWL6; -.
DR   PRIDE; Q8TWL6; -.
DR   EnsemblBacteria; AAM02230; AAM02230; MK1017.
DR   KEGG; mka:MK1017; -.
DR   PATRIC; fig|190192.8.peg.1067; -.
DR   eggNOG; arCOG00868; Archaea.
DR   eggNOG; COG1155; LUCA.
DR   HOGENOM; HOG000161057; -.
DR   KO; K02117; -.
DR   OMA; QQLAKWS; -.
DR   Proteomes; UP000001826; Chromosome.
DR   GO; GO:0033180; C:proton-transporting V-type ATPase, V1 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:InterPro.
DR   GO; GO:0042777; P:plasma membrane ATP synthesis coupled proton transport; IEA:UniProtKB-UniRule.
DR   Gene3D; 1.10.1140.10; -; 1.
DR   Gene3D; 2.40.30.20; -; 1.
DR   HAMAP; MF_00309; ATP_synth_A_arch; 1.
DR   InterPro; IPR003593; AAA+_ATPase.
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; IPR005725; ATPase_V1-cplx_asu.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   InterPro; IPR022878; V-ATPase_asu.
DR   PANTHER; PTHR43607; PTHR43607; 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   SMART; SM00382; AAA; 1.
DR   SUPFAM; SSF50615; SSF50615; 1.
DR   SUPFAM; SSF52540; SSF52540; 1.
DR   TIGRFAMs; TIGR01043; ATP_syn_A_arch; 1.
DR   TIGRFAMs; TIGR01042; V-ATPase_V1_A; 1.
DR   PROSITE; PS00152; ATPASE_ALPHA_BETA; 1.
PE   3: Inferred from homology;
DR   PRODOM; Q8TWL6.
DR   SWISS-2DPAGE; Q8TWL6.
KW   ATP synthesis; ATP-binding; Hydrogen ion transport; Ion transport;
KW   Nucleotide-binding; Reference proteome; Translocase; Transport.
FT   CHAIN           1..592
FT                   /note="V-type ATP synthase alpha chain"
FT                   /id="PRO_0000144600"
FT   NP_BIND         236..243
FT                   /note="ATP"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00309"
SQ   SEQUENCE   592 AA;  66494 MW;  3E0E1B54B395B6E1 CRC64;
     MSNSVKGEIV KIAGPVVEAV GCEGAKMYEV FRVGDEGLIG EVINIESDRA TIQVYEETTG
     LQPGEPVKGT GELLSVELGP GLLTQIFDGI QRPLPEIRKE VGDFVERGIL VSALDRKKKW
     EFTPKVKEGE KVEEGDVLGT VPETEFIEHK IMVPPGVSGE VIEIAADGEY TVEDTIAVIE
     DEEGEEHEVT MMQEWPVRKP RPYKRKLDPE EPLITGQRVI DTFFPVAKGG TAAIPGPFGS
     GKTVTQQQLA KWADAQVVVY IGCGERGNEM TEVLEDFPEL EDPRTGRPLM ERTILVANTS
     NMPVAAREAC IYTGITMAEY YRDMGYDVAL MADSTSRWAE ALREISGRLE EMPGEEGYPA
     YLASRLAEFY ERAGRVVCLG SDDRVGSVTV VGAVSPPGGD FSEPVTQNTL RIVKVFWALD
     SKLADRRHFP AINWLQSYSL YLDDVEKWWH EEIGGDWREL RDEAMEILQR ESELEEIVQL
     VGPDALPESE RLILEVARMI REDFLQQNAF HEVDTYCPPE KQYEMLKTIL HFKERAEEAV
     DKGVPVDEIL KLDVIDDIAR MKVIPNEEAK EKIQEIRKKI DEQFEELIEE AS
//

If you have problems or comments...

PBIL Back to PBIL home page