位置:首页 > 蛋白库 > VATA_ACET2
VATA_ACET2
ID   VATA_ACET2              Reviewed;         589 AA.
AC   A3DHP0;
DT   05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT   20-MAR-2007, sequence version 1.
DT   03-AUG-2022, entry version 94.
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=Cthe_2267;
OS   Acetivibrio thermocellus (strain ATCC 27405 / DSM 1237 / JCM 9322 / NBRC
OS   103400 / NCIMB 10682 / NRRL B-4536 / VPI 7372) (Clostridium thermocellum).
OC   Bacteria; Firmicutes; Clostridia; Eubacteriales; Oscillospiraceae;
OC   Acetivibrio.
OX   NCBI_TaxID=203119;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 27405 / DSM 1237 / JCM 9322 / NBRC 103400 / NCIMB 10682 / NRRL
RC   B-4536 / VPI 7372;
RG   US DOE Joint Genome Institute;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA   Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S.,
RA   Chertkov O., Brettin T., Bruce D., Han C., Tapia R., Gilna P., Schmutz J.,
RA   Larimer F., Land M., Hauser L., Kyrpides N., Mikhailova N., Wu J.H.D.,
RA   Newcomb M., Richardson P.;
RT   "Complete sequence of Clostridium thermocellum ATCC 27405.";
RL   Submitted (FEB-2007) 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: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}.
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; CP000568; ABN53469.1; -; Genomic_DNA.
DR   RefSeq; WP_003513515.1; NC_009012.1.
DR   AlphaFoldDB; A3DHP0; -.
DR   SMR; A3DHP0; -.
DR   STRING; 203119.Cthe_2267; -.
DR   PRIDE; A3DHP0; -.
DR   EnsemblBacteria; ABN53469; ABN53469; Cthe_2267.
DR   KEGG; cth:Cthe_2267; -.
DR   eggNOG; COG1155; Bacteria.
DR   HOGENOM; CLU_008162_3_1_9; -.
DR   OMA; RIVKTFW; -.
DR   OrthoDB; 875807at2; -.
DR   Proteomes; UP000002145; 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   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; 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   PROSITE; PS00152; ATPASE_ALPHA_BETA; 1.
PE   3: Inferred from homology;
KW   ATP synthesis; ATP-binding; Hydrogen ion transport; Ion transport;
KW   Nucleotide-binding; Reference proteome; Translocase; Transport.
FT   CHAIN           1..589
FT                   /note="V-type ATP synthase alpha chain"
FT                   /id="PRO_1000059340"
FT   BINDING         232..239
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00309"
SQ   SEQUENCE   589 AA;  65364 MW;  4479E74E5C8B1E8D CRC64;
     MSQGTIVKVS GPLVIAEGMR DANMFDVVRV SEHRLIGEII EMHGDRASIQ VYEETAGLGP
     GEPVVSTGAP LSVELGPGLI ENIFDGIQRP LVKMREMVGS NITRGIDVTA LDRSKKWDFQ
     PTVKKGDKVT AGDVIGKVQE TSIVEHRIMV PYGVQGTIEE IKSGSFTVEE TVAKVRTENN
     ELVDICMMQK WPVRIGRPYR EKLPPNAPLV TGQRVIDTLF PLAKGGVAAV PGPFGSGKTV
     VQHQLAKWAD ADIVVYIGCG ERGNEMTDVL KEFPELKDPK TGESLMKRTV LIANTSDMPV
     AAREASIYTG MTIAEYFRDM GYSVALMADS TSRWAEALRE MSGRLEEMPG EEGYPAYLGS
     RLAQFYERAG RVVCLGSDGR EGALTAIGAV SPPGGDLSEP VTQATLRIIK VFWGLDSSLA
     YRRHFPAINW LQSYSLYLDI IGKWISENIS RDWETLRSDT MRILQEEAEL EEIVRLVGVD
     ALSPSDRLTL EAAKSIREDY LHQNAFHEVD TYTSLNKQYR MLKLILGFYY SGKKALEAGV
     SIKELFELPV REKIGRAKYT PEDQVNSHFN EIEKELNEQI EALIAKEVQ
 
 
维奥蛋白资源库 - 中文蛋白资源 CopyRight © 2010-2024