ID   ATPD_CLOPD              Reviewed;         180 AA.
AC   Q0ZS22;
DT   05-MAY-2009, integrated into UniProtKB/Swiss-Prot.
DT   22-AUG-2006, sequence version 1.
DT   25-MAY-2022, entry version 61.
DE   RecName: Full=ATP synthase subunit delta, sodium ion specific {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};
OS   Clostridium paradoxum.
OC   Bacteria; Firmicutes; Clostridia; Eubacteriales; Peptostreptococcaceae.
OX   NCBI_TaxID=29346;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], SUBSTRATE, FUNCTION, SUBUNIT,
RP   INHIBITION, AND SUBCELLULAR LOCATION.
RC   STRAIN=ATCC 51510 / DSM 7308 / CIP 105527 / JW-YL-7;
RX   PubMed=16816177; DOI=10.1128/jb.00128-06;
RA   Ferguson S.A., Keis S., Cook G.M.;
RT   "Biochemical and molecular characterization of a Na+-translocating F1Fo-
RT   ATPase from the thermoalkaliphilic bacterium Clostridium paradoxum.";
RL   J. Bacteriol. 188:5045-5054(2006).
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   -!- FUNCTION: In this organism this enzyme may function as an ATP-driven
CC       Na(+) ion pump to generate a Na(+) ion electrochemical gradient rather
CC       than as an ATP synthase. {ECO:0000269|PubMed:16816177}.
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, ECO:0000269|PubMed:16816177}.
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000255|HAMAP-Rule:MF_01416,
CC       ECO:0000269|PubMed:16816177}; Peripheral membrane protein
CC       {ECO:0000255|HAMAP-Rule:MF_01416, ECO:0000269|PubMed:16816177}.
CC   -!- MISCELLANEOUS: The ATPase of C.paradoxum is of special interest because
CC       it uses sodium ions instead of protons as the physiological coupling
CC       ion.
CC   -!- SIMILARITY: Belongs to the ATPase delta chain family.
CC       {ECO:0000255|HAMAP-Rule:MF_01416}.
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DR   EMBL; DQ193538; ABB13423.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q0ZS22; -.
DR   SMR; Q0ZS22; -.
DR   BRENDA; 7.1.2.2; 8815.
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:0006814; P:sodium ion transport; IEA:UniProtKB-KW.
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   1: Evidence at protein level;
KW   ATP synthesis; Cell membrane; CF(1); Hydrogen ion transport; Ion transport;
KW   Membrane; Sodium; Sodium transport; Transport.
FT   CHAIN           1..180
FT                   /note="ATP synthase subunit delta, sodium ion specific"
FT                   /id="PRO_0000370948"
SQ   SEQUENCE   180 AA;  20764 MW;  3D518D3E8748984F CRC64;
     MAKLVATRYA SAIFEVGVEL NKEEMFYEEL KIISSNFEEN EKFFKMLKTP ILSKQEKKEL
     IENIYKDKAS LEIVNFLKVL IDKDRISIIR EIVDIYKQLL NENKNEIQAI AITAVPMSEE
     SLKELTYKLC EKTKKNVKVK NQVDPTVLGG VLVKMGNEEI DGTVKTKLEK LKKQLHQIIA