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ATP63_PELPD
ID   ATP63_PELPD             Reviewed;         229 AA.
AC   A1AP45;
DT   10-FEB-2009, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 1.
DT   25-MAY-2022, entry version 85.
DE   RecName: Full=ATP synthase subunit a 3 {ECO:0000255|HAMAP-Rule:MF_01393};
DE   AltName: Full=ATP synthase F0 sector subunit a 3 {ECO:0000255|HAMAP-Rule:MF_01393};
DE   AltName: Full=F-ATPase subunit 6 3 {ECO:0000255|HAMAP-Rule:MF_01393};
GN   Name=atpB3 {ECO:0000255|HAMAP-Rule:MF_01393}; OrderedLocusNames=Ppro_1500;
OS   Pelobacter propionicus (strain DSM 2379 / NBRC 103807 / OttBd1).
OC   Bacteria; Proteobacteria; Deltaproteobacteria; Desulfuromonadales;
OC   Desulfuromonadaceae; Pelobacter.
OX   NCBI_TaxID=338966;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 2379 / NBRC 103807 / OttBd1;
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   Saunders E., Brettin T., Bruce D., Han C., Tapia R., Schmutz J.,
RA   Larimer F., Land M., Hauser L., Kyrpides N., Kim E., Lovley D.,
RA   Richardson P.;
RT   "Complete sequence of chromosome of Pelobacter propionicus DSM 2379.";
RL   Submitted (OCT-2006) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Key component of the proton channel; it plays a direct role
CC       in the translocation of protons across the membrane.
CC       {ECO:0000255|HAMAP-Rule:MF_01393}.
CC   -!- SUBUNIT: F-type ATPases have 2 components, CF(1) - the catalytic core
CC       - and CF(0) - the membrane proton channel. CF(1) has five subunits:
CC       alpha(3), beta(3), gamma(1), delta(1), epsilon(1). CF(0) has three main
CC       subunits: a(1), b(2) and c(9-12). The alpha and beta chains form an
CC       alternating ring which encloses part of the gamma chain. CF(1) is
CC       attached to CF(0) by a central stalk formed by the gamma and epsilon
CC       chains, while a peripheral stalk is formed by the delta and b chains.
CC       {ECO:0000255|HAMAP-Rule:MF_01393}.
CC   -!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000255|HAMAP-
CC       Rule:MF_01393}; Multi-pass membrane protein {ECO:0000255|HAMAP-
CC       Rule:MF_01393}.
CC   -!- SIMILARITY: Belongs to the ATPase A chain family. {ECO:0000255|HAMAP-
CC       Rule:MF_01393}.
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DR   EMBL; CP000482; ABK99115.1; -; Genomic_DNA.
DR   RefSeq; WP_011735408.1; NC_008609.1.
DR   AlphaFoldDB; A1AP45; -.
DR   SMR; A1AP45; -.
DR   STRING; 338966.Ppro_1500; -.
DR   EnsemblBacteria; ABK99115; ABK99115; Ppro_1500.
DR   KEGG; ppd:Ppro_1500; -.
DR   eggNOG; COG0356; Bacteria.
DR   HOGENOM; CLU_041018_2_2_7; -.
DR   OMA; FFDQFMS; -.
DR   OrthoDB; 867266at2; -.
DR   Proteomes; UP000006732; Chromosome.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0045263; C:proton-transporting ATP synthase complex, coupling factor F(o); IEA:UniProtKB-KW.
DR   GO; GO:0046933; F:proton-transporting ATP synthase activity, rotational mechanism; IEA:UniProtKB-UniRule.
DR   Gene3D; 1.20.120.220; -; 1.
DR   HAMAP; MF_01393; ATP_synth_a_bact; 1.
DR   InterPro; IPR045082; ATP_syn_F0_a_bact/chloroplast.
DR   InterPro; IPR000568; ATP_synth_F0_asu.
DR   InterPro; IPR023011; ATP_synth_F0_asu_AS.
DR   InterPro; IPR035908; F0_ATP_A_sf.
DR   PANTHER; PTHR42823; PTHR42823; 1.
DR   Pfam; PF00119; ATP-synt_A; 1.
DR   PRINTS; PR00123; ATPASEA.
DR   SUPFAM; SSF81336; SSF81336; 1.
DR   TIGRFAMs; TIGR01131; ATP_synt_6_or_A; 1.
DR   PROSITE; PS00449; ATPASE_A; 1.
PE   3: Inferred from homology;
KW   ATP synthesis; Cell inner membrane; Cell membrane; CF(0);
KW   Hydrogen ion transport; Ion transport; Membrane; Reference proteome;
KW   Transmembrane; Transmembrane helix; Transport.
FT   CHAIN           1..229
FT                   /note="ATP synthase subunit a 3"
FT                   /id="PRO_0000362368"
FT   TRANSMEM        25..45
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01393"
FT   TRANSMEM        86..106
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01393"
FT   TRANSMEM        111..131
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01393"
FT   TRANSMEM        142..162
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01393"
FT   TRANSMEM        181..201
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01393"
FT   TRANSMEM        202..222
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01393"
SQ   SEQUENCE   229 AA;  25296 MW;  8802F52E41623034 CRC64;
     MVHPFLFLEF LRKMLAPLHL SEASADAVSY TWLIIALLLL LSFLATRALK TVPGGLQNFM
     EIIVGGIENM VTETMGEHGR PYFPLVATIG IFVLVSNLIG LIPGFFPPTA NINTTAACAI
     VVFLSTHVVG IKRHGIGYIK HFCGPILWLT PIMFFIEVIG HLSRPVSLTL RLFGNMNGHE
     LVLIIFFGLA PFLVPLPMML MGVLVSFIQA FVFMLLTMIY IQGSLEEAH
 
 
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