(data stored in SCRATCH zone)

SWISSPROT: D3VG34_XENNA

ID   D3VG34_XENNA            Unreviewed;       274 AA.
AC   D3VG34;
DT   20-APR-2010, integrated into UniProtKB/TrEMBL.
DT   20-APR-2010, sequence version 1.
DT   16-JAN-2019, entry version 54.
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:CBJ88124.1};
GN   OrderedLocusNames=XNC1_0031 {ECO:0000313|EMBL:CBJ88124.1};
OS   Xenorhabdus nematophila (strain ATCC 19061 / DSM 3370 / LMG 1036 /
OS   NCIB 9965 / AN6).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Morganellaceae; Xenorhabdus.
OX   NCBI_TaxID=406817 {ECO:0000313|EMBL:CBJ88124.1, ECO:0000313|Proteomes:UP000008075};
RN   [1] {ECO:0000313|Proteomes:UP000008075}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 19061 / DSM 3370 / LMG 1036 / NCIB 9965 / AN6
RC   {ECO:0000313|Proteomes:UP000008075};
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:CBJ88124.1, ECO:0000313|Proteomes:UP000008075}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 19061 / DSM 3370 / LMG 1036 / NCIB 9965 / AN6
RC   {ECO:0000313|Proteomes:UP000008075};
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; FN667742; CBJ88124.1; -; Genomic_DNA.
DR   RefSeq; WP_013183045.1; NC_014228.1.
DR   STRING; 406817.XNC1_0031; -.
DR   EnsemblBacteria; CBJ88124; CBJ88124; XNC1_0031.
DR   KEGG; xne:XNC1_0031; -.
DR   eggNOG; ENOG4105EE4; Bacteria.
DR   eggNOG; COG0356; LUCA.
DR   HOGENOM; HOG000253872; -.
DR   KO; K02108; -.
DR   OMA; QVFLTSW; -.
DR   Proteomes; UP000008075; 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; D3VG34.
DR   SWISS-2DPAGE; D3VG34.
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:UP000008075};
KW   Hydrogen ion transport {ECO:0000256|HAMAP-Rule:MF_01393,
KW   ECO:0000256|RuleBase:RU000483};
KW   Hydrolase {ECO:0000313|EMBL:CBJ88124.1};
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:UP000008075};
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     39     63       Helical. {ECO:0000256|HAMAP-Rule:
FT                                MF_01393}.
FT   TRANSMEM    103    121       Helical. {ECO:0000256|HAMAP-Rule:
FT                                MF_01393}.
FT   TRANSMEM    150    169       Helical. {ECO:0000256|HAMAP-Rule:
FT                                MF_01393}.
FT   TRANSMEM    214    236       Helical. {ECO:0000256|HAMAP-Rule:
FT                                MF_01393}.
FT   TRANSMEM    242    267       Helical. {ECO:0000256|HAMAP-Rule:
FT                                MF_01393}.
SQ   SEQUENCE   274 AA;  30587 MW;  D522A26507EA6AF4 CRC64;
     MSASGEVSTS EYISHHLRHL QLDLRTFELV NPHASGYEAT FWTLNIDSLF FSIVLGMLFL
     FVFRRVAVCA TDGVPGKFQT AVEMIIGFVD NTVRDMYHGK SKVIAPLALT VFVWVLLMNA
     LDLLPVDFIP YIGEHVFGLP ALRIVPTADV SVTLSMALGV FVLILFYSIK MKGIGGFAKE
     LTLQPFNHPL FIPINLILEG VSLLSKPISL GLRLFGNMYA GELIFILIAA LLPVWSQWLL
     SLPWAIFHIL IITLQAFIFM VLTIVYLSMA SEEH
//

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