ID   ATPD_MYCGA              Reviewed;         181 AA.
AC   P33254;
DT   01-FEB-1994, integrated into UniProtKB/Swiss-Prot.
DT   15-AUG-2003, sequence version 2.
DT   03-AUG-2022, entry version 127.
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=MYCGA3030;
GN   ORFNames=MGA_1170;
OS   Mycoplasma gallisepticum (strain R(low / passage 15 / clone 2))
OS   (Mycoplasmoides gallisepticum).
OC   Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mycoplasma.
OX   NCBI_TaxID=710127;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=A5969Var.B;
RX   PubMed=1386735; DOI=10.1042/bj2850881;
RA   Rasmussen O.F., Shirvan M.H., Margalit H., Christiansen C., Rottem S.;
RT   "Nucleotide sequence, organization and characterization of the atp genes
RT   and the encoded subunits of Mycoplasma gallisepticum ATPase.";
RL   Biochem. J. 285:881-888(1992).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=R(low / passage 15 / clone 2);
RX   PubMed=12949158; DOI=10.1099/mic.0.26427-0;
RA   Papazisi L., Gorton T.S., Kutish G., Markham P.F., Browning G.F.,
RA   Nguyen D.K., Swartzell S., Madan A., Mahairas G., Geary S.J.;
RT   "The complete genome sequence of the avian pathogen Mycoplasma
RT   gallisepticum strain R(low).";
RL   Microbiology 149:2307-2316(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}.
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DR   EMBL; X64256; CAA45548.1; -; Genomic_DNA.
DR   EMBL; AE015450; AAP56653.1; -; Genomic_DNA.
DR   PIR; S24336; S24336.
DR   RefSeq; WP_011113544.1; NC_004829.2.
DR   AlphaFoldDB; P33254; -.
DR   SMR; P33254; -.
DR   GeneID; 57203606; -.
DR   KEGG; mga:MGA_1170; -.
DR   HOGENOM; CLU_085114_4_2_14; -.
DR   OMA; EYDTYRM; -.
DR   OrthoDB; 1937493at2; -.
DR   Proteomes; UP000001418; 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   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 membrane; CF(1); Hydrogen ion transport; Ion transport;
KW   Membrane; Reference proteome; Transport.
FT   CHAIN           1..181
FT                   /note="ATP synthase subunit delta"
FT                   /id="PRO_0000193467"
FT   CONFLICT        101
FT                   /note="E -> K (in Ref. 1; CAA45548)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        123
FT                   /note="Q -> E (in Ref. 1; CAA45548)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        129
FT                   /note="H -> Y (in Ref. 1; CAA45548)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   181 AA;  21175 MW;  C2D9A0FD77C79F50 CRC64;
     MDTNIMGFAR ALVDLAHEED KVHLFYDNLK VVFDLVKENQ DLMSLMNSQV LSKNQKHEII
     DVVFKDHLTQ TIVDFLKVVI DNREFFHIKS IIKKFFRMIE EEEHTIFINV VSAHELNDDQ
     KAQLVEKLHK KFASQVKILY QTDPSLIAGI RIQSNDLLID NSIDGKLKLL KHQLRTFSKE
     N