ATPL_CLOPD
ID ATPL_CLOPD Reviewed; 84 AA.
AC Q0ZS24;
DT 03-MAR-2009, integrated into UniProtKB/Swiss-Prot.
DT 22-AUG-2006, sequence version 1.
DT 25-MAY-2022, entry version 67.
DE RecName: Full=ATP synthase subunit c, sodium ion specific;
DE AltName: Full=ATP synthase F(0) sector subunit c;
DE AltName: Full=F-type ATPase subunit c;
DE Short=F-ATPase subunit c;
DE AltName: Full=Lipid-binding protein;
GN Name=atpE;
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).
RN [2]
RP MASS SPECTROMETRY, SUBUNIT, AND PRELIMINARY CRYSTALLIZATION.
RC STRAIN=ATCC 51510 / DSM 7308 / CIP 105527 / JW-YL-7;
RX PubMed=16980459; DOI=10.1128/jb.00934-06;
RA Meier T., Ferguson S.A., Cook G.M., Dimroth P., Vonck J.;
RT "Structural investigations of the membrane-embedded rotor ring of the F-
RT ATPase from Clostridium paradoxum.";
RL J. Bacteriol. 188:7759-7764(2006).
CC -!- FUNCTION: F(1)F(0) ATP synthase produces ATP from ADP in the presence
CC of a sodium gradient. F-type ATPases consist of two structural domains,
CC F(1) containing the extramembraneous catalytic core and F(0) containing
CC the membrane proton channel, linked together by a central stalk and a
CC peripheral stalk. During catalysis, ATP synthesis in the catalytic
CC domain of F(1) is coupled via a rotary mechanism of the central stalk
CC subunits to proton translocation. {ECO:0000269|PubMed:16816177}.
CC -!- FUNCTION: Key component of the F(0) channel; it plays a direct role in
CC translocation across the membrane. A homomeric c-ring of 11 subunits
CC forms the central stalk rotor element with the F(1) delta and epsilon
CC subunits. {ECO:0000269|PubMed:16816177}.
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 -!- ACTIVITY REGULATION: Inhibited by dicyclohexylcarbodiimide; the enzyme
CC is protected from inhibition by Na(+) in a pH-dependent manner.
CC -!- SUBUNIT: F-type ATPases have 2 components, F(1) - the catalytic core
CC - and F(0) - the membrane sodium 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(11). 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:0000269|PubMed:16816177, ECO:0000269|PubMed:16980459}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:16816177};
CC Multi-pass membrane protein {ECO:0000269|PubMed:16816177}.
CC -!- MASS SPECTROMETRY: Mass=8266; Method=MALDI;
CC Evidence={ECO:0000269|PubMed:16980459};
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 C chain family. {ECO:0000305}.
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DR EMBL; DQ193538; ABB13421.1; -; Genomic_DNA.
DR AlphaFoldDB; Q0ZS24; -.
DR SMR; Q0ZS24; -.
DR BRENDA; 7.1.2.2; 8815.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0045263; C:proton-transporting ATP synthase complex, coupling factor F(o); IEA:UniProtKB-KW.
DR GO; GO:0008289; F:lipid binding; 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; 1.20.120.610; -; 1.
DR HAMAP; MF_01396; ATP_synth_c_bact; 1.
DR InterPro; IPR005953; ATP_synth_csu_bac/chlpt.
DR InterPro; IPR000454; ATP_synth_F0_csu.
DR InterPro; IPR002379; ATPase_proteolipid_c-like_dom.
DR InterPro; IPR035921; F/V-ATP_Csub_sf.
DR PANTHER; PTHR10031; PTHR10031; 1.
DR Pfam; PF00137; ATP-synt_C; 1.
DR PRINTS; PR00124; ATPASEC.
DR SUPFAM; SSF81333; SSF81333; 1.
DR TIGRFAMs; TIGR01260; ATP_synt_c; 1.
PE 1: Evidence at protein level;
KW ATP synthesis; Cell membrane; CF(0); Hydrogen ion transport; Ion transport;
KW Lipid-binding; Membrane; Sodium; Sodium transport; Transmembrane;
KW Transmembrane helix; Transport.
FT CHAIN 1..84
FT /note="ATP synthase subunit c, sodium ion specific"
FT /id="PRO_0000365872"
FT TRANSMEM 6..26
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 64..84
FT /note="Helical"
FT /evidence="ECO:0000255"
FT SITE 65
FT /note="Reversibly binds sodium during transport"
FT /evidence="ECO:0000305"
SQ SEQUENCE 84 AA; 8257 MW; 13DD93B439C433A1 CRC64;
MERALILAAS AIGAGLAMIA GIGPGIGQGF AAGKGAEAVG KQPEAQGDIL RTMLLGAAVA
ESTGIYALVV ALILLFANPL LNLL
