ID   ATPD_TROWT              Reviewed;         262 AA.
AC   Q83G88;
DT   01-SEP-2009, integrated into UniProtKB/Swiss-Prot.
DT   01-SEP-2009, sequence version 2.
DT   25-MAY-2022, entry version 96.
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}; Synonyms=twt427;
GN   OrderedLocusNames=TWT_427;
OS   Tropheryma whipplei (strain Twist) (Whipple's bacillus).
OC   Bacteria; Actinobacteria; Micrococcales; Tropherymataceae; Tropheryma.
OX   NCBI_TaxID=203267;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Twist;
RX   PubMed=12902375; DOI=10.1101/gr.1474603;
RA   Raoult D., Ogata H., Audic S., Robert C., Suhre K., Drancourt M.,
RA   Claverie J.-M.;
RT   "Tropheryma whipplei twist: a human pathogenic Actinobacteria with a
RT   reduced genome.";
RL   Genome Res. 13:1800-1809(2003).
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 membrane {ECO:0000255|HAMAP-Rule:MF_01416};
CC       Peripheral membrane protein {ECO:0000255|HAMAP-Rule:MF_01416}.
CC   -!- SIMILARITY: Belongs to the ATPase delta chain family.
CC       {ECO:0000255|HAMAP-Rule:MF_01416}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAO44524.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR   EMBL; AE014184; AAO44524.1; ALT_INIT; Genomic_DNA.
DR   RefSeq; WP_011096293.1; NC_004572.3.
DR   AlphaFoldDB; Q83G88; -.
DR   SMR; Q83G88; -.
DR   STRING; 203267.TWT_427; -.
DR   EnsemblBacteria; AAO44524; AAO44524; TWT_427.
DR   GeneID; 67388114; -.
DR   KEGG; twh:TWT_427; -.
DR   eggNOG; COG0712; Bacteria.
DR   HOGENOM; CLU_1061480_0_0_11; -.
DR   OMA; FRFGRIV; -.
DR   OrthoDB; 1937493at2; -.
DR   Proteomes; UP000002200; 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   HAMAP; MF_01416; ATP_synth_delta_bact; 1.
DR   InterPro; IPR020781; ATPase_OSCP/d_CS.
DR   InterPro; IPR000711; ATPase_OSCP/dsu.
DR   Pfam; PF00213; OSCP; 1.
DR   PROSITE; PS00389; ATPASE_DELTA; 1.
PE   3: Inferred from homology;
KW   ATP synthesis; Cell membrane; CF(1); Hydrogen ion transport; Ion transport;
KW   Membrane; Reference proteome; Transport.
FT   CHAIN           1..262
FT                   /note="ATP synthase subunit delta"
FT                   /id="PRO_0000382166"
SQ   SEQUENCE   262 AA;  29652 MW;  FEDF86E934159642 CRC64;
     MPGSSSRSSL AHLRNRLSEC SDLQSLYEVA VLLAISRRLR SSLVSRSLSC VSKQKLIAEL
     TGKDPDAFIC MAVSLRWSEP IDLLYAFEEM FIRASCTRRF ADCRDFLDEL FWVSSIVDSH
     KILDKTLSAR FLPAYSKKQL ISGVFAGAHE GTLAVLEYFA CYMQKKRAFR ECVFFAEKIV
     ADELGAQIAD VTTERPLSRE QRDELVDVLS RRFKRRIILR EVINEKVFGG VRVQVNHSVI
     DDTVAVHLNN LALSFGALET FS