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ATP6_NOVAD
ID   ATP6_NOVAD              Reviewed;         260 AA.
AC   Q2G8R3;
DT   10-FEB-2009, integrated into UniProtKB/Swiss-Prot.
DT   21-MAR-2006, sequence version 1.
DT   25-MAY-2022, entry version 94.
DE   RecName: Full=ATP synthase subunit a {ECO:0000255|HAMAP-Rule:MF_01393};
DE   AltName: Full=ATP synthase F0 sector subunit a {ECO:0000255|HAMAP-Rule:MF_01393};
DE   AltName: Full=F-ATPase subunit 6 {ECO:0000255|HAMAP-Rule:MF_01393};
GN   Name=atpB {ECO:0000255|HAMAP-Rule:MF_01393}; OrderedLocusNames=Saro_1316;
OS   Novosphingobium aromaticivorans (strain ATCC 700278 / DSM 12444 / CCUG
OS   56034 / CIP 105152 / NBRC 16084 / F199).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Sphingomonadales;
OC   Sphingomonadaceae; Novosphingobium.
OX   NCBI_TaxID=279238;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 700278 / DSM 12444 / CCUG 56034 / CIP 105152 / NBRC 16084 /
RC   F199;
RG   US DOE Joint Genome Institute;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina T.,
RA   Hammon N., Israni S., Pitluck S., Chain P., Malfatti S., Shin M.,
RA   Vergez L., Schmutz J., Larimer F., Land M., Kyrpides N., Ivanova N.,
RA   Fredrickson J., Balkwill D., Romine M.F., Richardson P.;
RT   "Complete sequence of Novosphingobium aromaticivorans DSM 12444.";
RL   Submitted (JAN-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; CP000248; ABD25760.1; -; Genomic_DNA.
DR   RefSeq; WP_011444974.1; NC_007794.1.
DR   AlphaFoldDB; Q2G8R3; -.
DR   SMR; Q2G8R3; -.
DR   STRING; 279238.Saro_1316; -.
DR   EnsemblBacteria; ABD25760; ABD25760; Saro_1316.
DR   KEGG; nar:Saro_1316; -.
DR   eggNOG; COG0356; Bacteria.
DR   HOGENOM; CLU_041018_0_2_5; -.
DR   OMA; FFDQFMS; -.
DR   OrthoDB; 867266at2; -.
DR   Proteomes; UP000009134; 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; IPR000568; ATP_synth_F0_asu.
DR   InterPro; IPR045083; ATP_synth_F0_asu_bact/mt.
DR   InterPro; IPR035908; F0_ATP_A_sf.
DR   PANTHER; PTHR11410; PTHR11410; 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.
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..260
FT                   /note="ATP synthase subunit a"
FT                   /id="PRO_0000362358"
FT   TRANSMEM        30..50
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01393"
FT   TRANSMEM        96..116
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01393"
FT   TRANSMEM        125..145
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01393"
FT   TRANSMEM        151..171
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01393"
FT   TRANSMEM        187..207
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01393"
FT   TRANSMEM        213..233
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01393"
FT   TRANSMEM        234..254
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01393"
SQ   SEQUENCE   260 AA;  27994 MW;  C98E7EB3578754DD CRC64;
     MAEGKVDPVH QFTIETLFGT DHWSIGGYNI AFTNSALWMA ITTAVLIVFV AGGAKRELVP
     GRWQMAVEGL TGFVDNLLQA NIGKAGRKYL PYVFSLFAFI LFANMLGLLP LALVGVHPFT
     ATSHFTVTGV LAIMSFAIVL GVGFAKHGLH FFSLFVPHGT PVPMIPIIFP IELISFMVRP
     FSLGLRLFVA MMAGHVLLEV LSGFVISGTN AGVGTFFLAA VPSFLLMIGI CALELLVAGI
     QAYVFALLTC VYLNDAENLH
 
 
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