(data stored in SCRATCH zone)

SWISSPROT: D3VG31_XENNA

ID   D3VG31_XENNA            Unreviewed;       177 AA.
AC   D3VG31;
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 delta {ECO:0000256|HAMAP-Rule:MF_01416};
DE   AltName: Full=ATP synthase F(1) sector subunit delta {ECO:0000256|HAMAP-Rule:MF_01416};
DE   AltName: Full=F-type ATPase subunit delta {ECO:0000256|HAMAP-Rule:MF_01416};
DE            Short=F-ATPase subunit delta {ECO:0000256|HAMAP-Rule:MF_01416};
GN   Name=atpH {ECO:0000256|HAMAP-Rule:MF_01416,
GN   ECO:0000313|EMBL:CBJ88121.1};
GN   OrderedLocusNames=XNC1_0028 {ECO:0000313|EMBL:CBJ88121.1};
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:CBJ88121.1, 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:CBJ88121.1, 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: F(1)F(0) ATP synthase produces ATP from ADP in the
CC       presence of a proton or sodium gradient. F-type ATPases consist of
CC       two structural domains, F(1) containing the extramembraneous
CC       catalytic core and F(0) containing the membrane proton channel,
CC       linked together by a central stalk and a peripheral stalk. During
CC       catalysis, ATP synthesis in the catalytic domain of F(1) is
CC       coupled via a rotary mechanism of the central stalk subunits to
CC       proton translocation. {ECO:0000256|HAMAP-Rule:MF_01416}.
CC   -!- FUNCTION: This protein is part of the stalk that links CF(0) to
CC       CF(1). It either transmits conformational changes from CF(0) to
CC       CF(1) or is implicated in proton conduction. {ECO:0000256|HAMAP-
CC       Rule:MF_01416}.
CC   -!- SUBUNIT: F-type ATPases have 2 components, F(1) - the catalytic
CC       core - and F(0) - the membrane proton channel. F(1) has five
CC       subunits: alpha(3), beta(3), gamma(1), delta(1), epsilon(1). F(0)
CC       has three main subunits: a(1), b(2) and c(10-14). The alpha and
CC       beta chains form an alternating ring which encloses part of the
CC       gamma chain. F(1) is attached to F(0) by a central stalk formed by
CC       the gamma and epsilon chains, while a peripheral stalk is formed
CC       by the delta and b chains. {ECO:0000256|HAMAP-Rule:MF_01416}.
CC   -!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000256|HAMAP-
CC       Rule:MF_01416}; Peripheral membrane protein {ECO:0000256|HAMAP-
CC       Rule:MF_01416}.
CC   -!- SIMILARITY: Belongs to the ATPase delta chain family.
CC       {ECO:0000256|HAMAP-Rule:MF_01416, ECO:0000256|SAAS:SAAS01082575}.
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DR   EMBL; FN667742; CBJ88121.1; -; Genomic_DNA.
DR   RefSeq; WP_013183044.1; NC_014228.1.
DR   STRING; 406817.XNC1_0028; -.
DR   EnsemblBacteria; CBJ88121; CBJ88121; XNC1_0028.
DR   KEGG; xne:XNC1_0028; -.
DR   eggNOG; ENOG4107S15; Bacteria.
DR   eggNOG; COG0712; LUCA.
DR   HOGENOM; HOG000075824; -.
DR   KO; K02113; -.
DR   OMA; MVDNIQD; -.
DR   Proteomes; UP000008075; Chromosome.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0045261; C:proton-transporting ATP synthase complex, catalytic core F(1); 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; 1.10.520.20; -; 1.
DR   HAMAP; MF_01416; ATP_synth_delta_bact; 1.
DR   InterPro; IPR026015; ATP_synth_OSCP/delta_N_sf.
DR   InterPro; IPR020781; ATPase_OSCP/d_CS.
DR   InterPro; IPR000711; ATPase_OSCP/dsu.
DR   PANTHER; PTHR11910; PTHR11910; 1.
DR   Pfam; PF00213; OSCP; 1.
DR   PRINTS; PR00125; ATPASEDELTA.
DR   SUPFAM; SSF47928; SSF47928; 1.
DR   TIGRFAMs; TIGR01145; ATP_synt_delta; 1.
DR   PROSITE; PS00389; ATPASE_DELTA; 1.
PE   3: Inferred from homology;
DR   PRODOM; D3VG31.
DR   SWISS-2DPAGE; D3VG31.
KW   ATP synthesis {ECO:0000256|HAMAP-Rule:MF_01416,
KW   ECO:0000256|SAAS:SAAS00673570};
KW   Cell inner membrane {ECO:0000256|HAMAP-Rule:MF_01416};
KW   Cell membrane {ECO:0000256|HAMAP-Rule:MF_01416};
KW   CF(1) {ECO:0000256|HAMAP-Rule:MF_01416};
KW   Complete proteome {ECO:0000313|Proteomes:UP000008075};
KW   Hydrogen ion transport {ECO:0000256|HAMAP-Rule:MF_01416,
KW   ECO:0000256|SAAS:SAAS00673590};
KW   Hydrolase {ECO:0000313|EMBL:CBJ88121.1};
KW   Ion transport {ECO:0000256|HAMAP-Rule:MF_01416,
KW   ECO:0000256|SAAS:SAAS00673577};
KW   Membrane {ECO:0000256|HAMAP-Rule:MF_01416,
KW   ECO:0000256|SAAS:SAAS00673593};
KW   Reference proteome {ECO:0000313|Proteomes:UP000008075};
KW   Transport {ECO:0000256|HAMAP-Rule:MF_01416,
KW   ECO:0000256|SAAS:SAAS00673594}.
SQ   SEQUENCE   177 AA;  19676 MW;  56E0AD140E165049 CRC64;
     MSEFATVARP YAKAAFDFAV EHQSIEHWQN MLAFIAEVTR NEQVGELLSG SLAPETLAKT
     FITLCGEQVD AHAQNFIRVM AENGRLLVLP EVFQQFIQLR ASLESTIDVE VISVSELNEQ
     QQAKISAAME KRLSRKVKLN CKIDKSVIAG VVIRAGDMVI DGSIRGRLDR LTDDLQS
//

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