(data stored in SCRATCH zone)

SWISSPROT: D3UY05_XENBS

ID   D3UY05_XENBS            Unreviewed;       275 AA.
AC   D3UY05;
DT   20-APR-2010, integrated into UniProtKB/TrEMBL.
DT   20-APR-2010, sequence version 1.
DT   16-JAN-2019, entry version 57.
DE   RecName: Full=ATP synthase subunit a {ECO:0000256|HAMAP-Rule:MF_01393, ECO:0000256|RuleBase:RU000483};
DE   AltName: Full=ATP synthase F0 sector subunit a {ECO:0000256|HAMAP-Rule:MF_01393};
DE   AltName: Full=F-ATPase subunit 6 {ECO:0000256|HAMAP-Rule:MF_01393};
GN   Name=atpB {ECO:0000256|HAMAP-Rule:MF_01393,
GN   ECO:0000313|EMBL:CBJ79183.1};
GN   OrderedLocusNames=XBJ1_0028 {ECO:0000313|EMBL:CBJ79183.1};
OS   Xenorhabdus bovienii (strain SS-2004).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Morganellaceae; Xenorhabdus.
OX   NCBI_TaxID=406818 {ECO:0000313|EMBL:CBJ79183.1, ECO:0000313|Proteomes:UP000002045};
RN   [1] {ECO:0000313|Proteomes:UP000002045}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SS-2004 {ECO:0000313|Proteomes:UP000002045};
RA   Goodrich-Blair H., Barbazuk B., Bode H.B., Darby C., Du Z., Forst S.,
RA   Gaudriault S., Goldman B.S., Goodner B., Henkhaus J., Latreille P.,
RA   Medigue C., Miller N., Norton S., Ogier J.C., Rouy Z., Slater S.,
RA   Suen G.;
RT   "Complete genome sequence of Xenorhabdus nematophila (strain ATCC
RT   19061 / DSM 3370 / LMG 1036 / NCIB 9965 / AN6).";
RL   Submitted (FEB-2010) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:CBJ79183.1, ECO:0000313|Proteomes:UP000002045}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SS-2004 {ECO:0000313|EMBL:CBJ79183.1,
RC   ECO:0000313|Proteomes:UP000002045};
RX   PubMed=22125637; DOI=10.1371/journal.pone.0027909;
RA   Chaston J.M., Suen G., Tucker S.L., Andersen A.W., Bhasin A., Bode E.,
RA   Bode H.B., Brachmann A.O., Cowles C.E., Cowles K.N., Darby C.,
RA   de Leon L., Drace K., Du Z., Givaudan A., Herbert Tran E.E.,
RA   Jewell K.A., Knack J.J., Krasomil-Osterfeld K.C., Kukor R., Lanois A.,
RA   Latreille P., Leimgruber N.K., Lipke C.M., Liu R., Lu X.,
RA   Martens E.C., Marri P.R., Medigue C., Menard M.L., Miller N.M.,
RA   Morales-Soto N., Norton S., Ogier J.C., Orchard S.S., Park D.,
RA   Park Y., Qurollo B.A., Sugar D.R., Richards G.R., Rouy Z.,
RA   Slominski B., Slominski K., Snyder H., Tjaden B.C., van der Hoeven R.,
RA   Welch R.D., Wheeler C., Xiang B., Barbazuk B., Gaudriault S.,
RA   Goodner B., Slater S.C., Forst S., Goldman B.S., Goodrich-Blair H.;
RT   "The entomopathogenic bacterial endosymbionts xenorhabdus and
RT   photorhabdus: convergent lifestyles from divergent genomes.";
RL   PLoS ONE 6:e27909-e27909(2011).
CC   -!- FUNCTION: Key component of the proton channel; it plays a direct
CC       role in the translocation of protons across the membrane.
CC       {ECO:0000256|HAMAP-Rule:MF_01393, ECO:0000256|RuleBase:RU000483}.
CC   -!- SUBUNIT: F-type ATPases have 2 components, CF(1) - the catalytic
CC       core - and CF(0) - the membrane proton channel. CF(1) has five
CC       subunits: alpha(3), beta(3), gamma(1), delta(1), epsilon(1). CF(0)
CC       has three main subunits: a(1), b(2) and c(9-12). The alpha and
CC       beta chains form an alternating ring which encloses part of the
CC       gamma chain. CF(1) is attached to CF(0) by a central stalk formed
CC       by the gamma and epsilon chains, while a peripheral stalk is
CC       formed by the delta and b chains. {ECO:0000256|HAMAP-
CC       Rule:MF_01393}.
CC   -!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000256|HAMAP-
CC       Rule:MF_01393}; Multi-pass membrane protein {ECO:0000256|HAMAP-
CC       Rule:MF_01393}. Cell membrane {ECO:0000256|RuleBase:RU000483};
CC       Multi-pass membrane protein {ECO:0000256|RuleBase:RU000483}.
CC   -!- SIMILARITY: Belongs to the ATPase A chain family.
CC       {ECO:0000256|HAMAP-Rule:MF_01393, ECO:0000256|RuleBase:RU000483}.
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DR   EMBL; FN667741; CBJ79183.1; -; Genomic_DNA.
DR   RefSeq; WP_012986656.1; NC_013892.1.
DR   STRING; 406818.XBJ1_0028; -.
DR   EnsemblBacteria; CBJ79183; CBJ79183; XBJ1_0028.
DR   GeneID; 8829655; -.
DR   KEGG; xbo:XBJ1_0028; -.
DR   eggNOG; ENOG4105EE4; Bacteria.
DR   eggNOG; COG0356; LUCA.
DR   HOGENOM; HOG000253872; -.
DR   KO; K02108; -.
DR   OMA; QVFLTSW; -.
DR   BioCyc; XBOV406818:XBJ1_RS00120-MONOMER; -.
DR   Proteomes; UP000002045; 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   GO; GO:0015986; P:ATP synthesis coupled proton transport; 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; IPR023011; ATP_synth_F0_asu_AS.
DR   InterPro; IPR035908; F0_ATP_A_sf.
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;
DR   PRODOM; D3UY05.
DR   SWISS-2DPAGE; D3UY05.
KW   ATP synthesis {ECO:0000256|HAMAP-Rule:MF_01393};
KW   Cell inner membrane {ECO:0000256|HAMAP-Rule:MF_01393};
KW   Cell membrane {ECO:0000256|HAMAP-Rule:MF_01393};
KW   CF(0) {ECO:0000256|HAMAP-Rule:MF_01393,
KW   ECO:0000256|RuleBase:RU000483};
KW   Complete proteome {ECO:0000313|Proteomes:UP000002045};
KW   Hydrogen ion transport {ECO:0000256|HAMAP-Rule:MF_01393,
KW   ECO:0000256|RuleBase:RU000483};
KW   Hydrolase {ECO:0000313|EMBL:CBJ79183.1};
KW   Ion transport {ECO:0000256|HAMAP-Rule:MF_01393,
KW   ECO:0000256|RuleBase:RU000483};
KW   Membrane {ECO:0000256|HAMAP-Rule:MF_01393};
KW   Reference proteome {ECO:0000313|Proteomes:UP000002045};
KW   Transmembrane {ECO:0000256|HAMAP-Rule:MF_01393,
KW   ECO:0000256|RuleBase:RU000483};
KW   Transmembrane helix {ECO:0000256|HAMAP-Rule:MF_01393};
KW   Transport {ECO:0000256|HAMAP-Rule:MF_01393,
KW   ECO:0000256|RuleBase:RU000483}.
FT   TRANSMEM     42     64       Helical. {ECO:0000256|HAMAP-Rule:
FT                                MF_01393}.
FT   TRANSMEM    104    125       Helical. {ECO:0000256|HAMAP-Rule:
FT                                MF_01393}.
FT   TRANSMEM    145    170       Helical. {ECO:0000256|HAMAP-Rule:
FT                                MF_01393}.
FT   TRANSMEM    215    237       Helical. {ECO:0000256|HAMAP-Rule:
FT                                MF_01393}.
FT   TRANSMEM    243    268       Helical. {ECO:0000256|HAMAP-Rule:
FT                                MF_01393}.
SQ   SEQUENCE   275 AA;  30955 MW;  9B6CB71D6D2D94FB CRC64;
     MSASGEVLTS QEYISHHLKH LQLDLRTFEL VNPHASGYET TFWTLNIDSL FFSVILGILF
     LFVFRRVAVR ATDGVPGKLQ TAVEMVFGFV DNTVRDMYHG KSKVIAPLAL TVFVWVLLMN
     ALDLLPIDLI PLIGERYFGL PALRIVPTAD VSVTLSMALG VFVLILFYSI KMKGIRGFAK
     ELTLQPFNHP LFIPINLILE GVSLLSKPIS LALRLFGNMY AGELIFILIT ALLPFWSQWL
     LSLPWAIFHI LIITLQAFIF MVLTVVYLSM ASEEH
//

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