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VATA_HALVD
ID   VATA_HALVD              Reviewed;         586 AA.
AC   Q48332; D4GZU5;
DT   01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1996, sequence version 1.
DT   03-AUG-2022, entry version 122.
DE   RecName: Full=V-type ATP synthase alpha chain;
DE            EC=7.1.2.2;
DE   AltName: Full=V-ATPase subunit A;
GN   Name=atpA; OrderedLocusNames=HVO_0316;
OS   Haloferax volcanii (strain ATCC 29605 / DSM 3757 / JCM 8879 / NBRC 14742 /
OS   NCIMB 2012 / VKM B-1768 / DS2) (Halobacterium volcanii).
OC   Archaea; Euryarchaeota; Stenosarchaea group; Halobacteria; Haloferacales;
OC   Haloferacaceae; Haloferax.
OX   NCBI_TaxID=309800;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND CHARACTERIZATION.
RC   STRAIN=DS2 / WR 340;
RX   PubMed=7599166; DOI=10.1016/0167-4838(95)00033-q;
RA   Steinert K., Kroth-Pancic P.G., Bickel-Sandkoetter S.;
RT   "Nucleotide sequence of the ATPase A- and B-subunits of the halophilic
RT   archaebacterium Haloferax volcanii and characterization of the enzyme.";
RL   Biochim. Biophys. Acta 1249:137-144(1995).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 29605 / DSM 3757 / JCM 8879 / NBRC 14742 / NCIMB 2012 / VKM
RC   B-1768 / DS2;
RX   PubMed=20333302; DOI=10.1371/journal.pone.0009605;
RA   Hartman A.L., Norais C., Badger J.H., Delmas S., Haldenby S., Madupu R.,
RA   Robinson J., Khouri H., Ren Q., Lowe T.M., Maupin-Furlow J.,
RA   Pohlschroder M., Daniels C., Pfeiffer F., Allers T., Eisen J.A.;
RT   "The complete genome sequence of Haloferax volcanii DS2, a model
RT   archaeon.";
RL   PLoS ONE 5:E9605-E9605(2010).
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   -!- 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   -!- SIMILARITY: Belongs to the ATPase alpha/beta chains family.
CC       {ECO:0000305}.
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DR   EMBL; X79516; CAA56051.1; -; Genomic_DNA.
DR   EMBL; CP001956; ADE04665.1; -; Genomic_DNA.
DR   PIR; S55895; S45144.
DR   RefSeq; WP_004044607.1; NC_013967.1.
DR   AlphaFoldDB; Q48332; -.
DR   SMR; Q48332; -.
DR   STRING; 309800.C498_17108; -.
DR   EnsemblBacteria; ADE04665; ADE04665; HVO_0316.
DR   GeneID; 8924169; -.
DR   KEGG; hvo:HVO_0316; -.
DR   eggNOG; arCOG00868; Archaea.
DR   HOGENOM; CLU_008162_3_1_2; -.
DR   OMA; RIVKTFW; -.
DR   OrthoDB; 6736at2157; -.
DR   Proteomes; UP000008243; 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   Gene3D; 1.10.1140.10; -; 1.
DR   Gene3D; 2.40.30.20; -; 1.
DR   Gene3D; 3.40.50.300; -; 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; 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   SUPFAM; SSF50615; SSF50615; 1.
DR   SUPFAM; SSF52540; SSF52540; 1.
DR   TIGRFAMs; TIGR01043; ATP_syn_A_arch; 1.
DR   PROSITE; PS00152; ATPASE_ALPHA_BETA; 1.
PE   1: Evidence at protein level;
KW   ATP synthesis; ATP-binding; Hydrogen ion transport; Ion transport;
KW   Nucleotide-binding; Reference proteome; Translocase; Transport.
FT   CHAIN           1..586
FT                   /note="V-type ATP synthase alpha chain"
FT                   /id="PRO_0000144595"
FT   BINDING         238..245
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   586 AA;  64515 MW;  AAB574C9837B44A0 CRC64;
     MSQATQDSVR EDGVIASVSG PVVTARGLDA RMNDVVYVGD EGLMGEVIEI EGDLTTIQVY
     EETSGVGPGE PVESTGEPLT VDLGPGMMDA IYDGVQRPLD VLESKMDSAF LDRGVDAPGI
     DLDEKWEFEP TVSEGDEVAP GDVVGTVPET VTIEHKVMVP PDFGGGEVVA VEEGEFSVTE
     AVVELDSGEE ITMHQEWPVR QARPAAEKKT PREPLVSGQR ILDGLFPIAK GGTAAIPGPF
     GSGKTVTQHQ LAKWADADIV VYVGCGERGN EMTEVIEDFP ELDDPKTGNP LMARTCLIAN
     TSNMPVAARE SCIYTGITIA EYYRDMGYDV ALMADSTSRW AEAMREISSR LEEMPGEEGY
     PAYLAARLSE FYERAGYFTT VNGEEGSVSV IGAVSPPGGD FSEPVTQNTL RIVKTFWALD
     ADLAERRHFP AINWNESYSL YQEQLDPWFV ENVEDDWAEE RQWAVDVLDE ENELQEIVQL
     VGKDALPEDQ QLTLEIARYL REAYLQQNAF HPTDTYCSPE KTYGILTAIH AFNDEAFKAL
     EAGVPVEEIQ AIEAAPRLNR IGVQEDWEAY IEDLKAEITE QLRELY
 
 
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