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ATPD_AGRFC
ID   ATPD_AGRFC              Reviewed;         188 AA.
AC   Q7CWL8;
DT   05-MAY-2009, integrated into UniProtKB/Swiss-Prot.
DT   05-MAY-2009, sequence version 3.
DT   25-MAY-2022, entry version 88.
DE   RecName: Full=ATP synthase subunit delta {ECO:0000255|HAMAP-Rule:MF_01416};
DE   AltName: Full=ATP synthase F(1) sector subunit delta {ECO:0000255|HAMAP-Rule:MF_01416};
DE   AltName: Full=F-type ATPase subunit delta {ECO:0000255|HAMAP-Rule:MF_01416};
DE            Short=F-ATPase subunit delta {ECO:0000255|HAMAP-Rule:MF_01416};
GN   Name=atpH {ECO:0000255|HAMAP-Rule:MF_01416}; OrderedLocusNames=Atu2625;
GN   ORFNames=AGR_C_4759;
OS   Agrobacterium fabrum (strain C58 / ATCC 33970) (Agrobacterium tumefaciens
OS   (strain C58)).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Hyphomicrobiales;
OC   Rhizobiaceae; Rhizobium/Agrobacterium group; Agrobacterium;
OC   Agrobacterium tumefaciens complex.
OX   NCBI_TaxID=176299;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=C58 / ATCC 33970;
RX   PubMed=11743194; DOI=10.1126/science.1066803;
RA   Goodner B., Hinkle G., Gattung S., Miller N., Blanchard M., Qurollo B.,
RA   Goldman B.S., Cao Y., Askenazi M., Halling C., Mullin L., Houmiel K.,
RA   Gordon J., Vaudin M., Iartchouk O., Epp A., Liu F., Wollam C., Allinger M.,
RA   Doughty D., Scott C., Lappas C., Markelz B., Flanagan C., Crowell C.,
RA   Gurson J., Lomo C., Sear C., Strub G., Cielo C., Slater S.;
RT   "Genome sequence of the plant pathogen and biotechnology agent
RT   Agrobacterium tumefaciens C58.";
RL   Science 294:2323-2328(2001).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=C58 / ATCC 33970;
RX   PubMed=11743193; DOI=10.1126/science.1066804;
RA   Wood D.W., Setubal J.C., Kaul R., Monks D.E., Kitajima J.P., Okura V.K.,
RA   Zhou Y., Chen L., Wood G.E., Almeida N.F. Jr., Woo L., Chen Y.,
RA   Paulsen I.T., Eisen J.A., Karp P.D., Bovee D. Sr., Chapman P.,
RA   Clendenning J., Deatherage G., Gillet W., Grant C., Kutyavin T., Levy R.,
RA   Li M.-J., McClelland E., Palmieri A., Raymond C., Rouse G.,
RA   Saenphimmachak C., Wu Z., Romero P., Gordon D., Zhang S., Yoo H., Tao Y.,
RA   Biddle P., Jung M., Krespan W., Perry M., Gordon-Kamm B., Liao L., Kim S.,
RA   Hendrick C., Zhao Z.-Y., Dolan M., Chumley F., Tingey S.V., Tomb J.-F.,
RA   Gordon M.P., Olson M.V., Nester E.W.;
RT   "The genome of the natural genetic engineer Agrobacterium tumefaciens
RT   C58.";
RL   Science 294:2317-2323(2001).
CC   -!- FUNCTION: F(1)F(0) ATP synthase produces ATP from ADP in the presence
CC       of a proton or sodium gradient. F-type ATPases consist of two
CC       structural domains, F(1) containing the extramembraneous catalytic core
CC       and F(0) containing the membrane proton channel, linked together by a
CC       central stalk and a peripheral stalk. During catalysis, ATP synthesis
CC       in the catalytic domain of F(1) is coupled via a rotary mechanism of
CC       the central stalk subunits to proton translocation. {ECO:0000255|HAMAP-
CC       Rule:MF_01416}.
CC   -!- FUNCTION: This protein is part of the stalk that links CF(0) to CF(1).
CC       It either transmits conformational changes from CF(0) to CF(1) or is
CC       implicated in proton conduction. {ECO:0000255|HAMAP-Rule:MF_01416}.
CC   -!- SUBUNIT: F-type ATPases have 2 components, F(1) - the catalytic core
CC       - and F(0) - the membrane proton channel. F(1) has five subunits:
CC       alpha(3), beta(3), gamma(1), delta(1), epsilon(1). F(0) has three main
CC       subunits: a(1), b(2) and c(10-14). The alpha and beta chains form an
CC       alternating ring which encloses part of the gamma chain. F(1) is
CC       attached to F(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_01416}.
CC   -!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000255|HAMAP-
CC       Rule:MF_01416}; Peripheral membrane protein {ECO:0000255|HAMAP-
CC       Rule:MF_01416}.
CC   -!- SIMILARITY: Belongs to the ATPase delta chain family.
CC       {ECO:0000255|HAMAP-Rule:MF_01416}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAK88346.2; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR   EMBL; AE007869; AAK88346.2; ALT_INIT; Genomic_DNA.
DR   RefSeq; NP_355561.2; NC_003062.2.
DR   AlphaFoldDB; Q7CWL8; -.
DR   SMR; Q7CWL8; -.
DR   STRING; 176299.Atu2625; -.
DR   EnsemblBacteria; AAK88346; AAK88346; Atu2625.
DR   KEGG; atu:Atu2625; -.
DR   PATRIC; fig|176299.10.peg.2628; -.
DR   eggNOG; COG0712; Bacteria.
DR   HOGENOM; CLU_085114_0_1_5; -.
DR   OMA; MVDNIQD; -.
DR   Proteomes; UP000000813; Chromosome circular.
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   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;
KW   ATP synthesis; Cell inner membrane; Cell membrane; CF(1);
KW   Hydrogen ion transport; Ion transport; Membrane; Reference proteome;
KW   Transport.
FT   CHAIN           1..188
FT                   /note="ATP synthase subunit delta"
FT                   /id="PRO_0000370874"
SQ   SEQUENCE   188 AA;  19798 MW;  39F0EF40CBB5A373 CRC64;
     MPVAETSQGT SGVAERYASS LFELALEAGT VEAVQVELDK FGALLDESDD LKRLVASPVF
     SAEDQFKAIS AICEKAGIAG LAVNFLKVVA NNRRLFAVPG MIRAYRTIAA AHRGEITAEV
     TSAHALDEAQ ETELKAALKS VTGKDVAISV TVDPSILGGL IVKVGSRQID TSLRTKLSTL
     KLALKEVG
 
 
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