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ATP synthase subunit c, sodium ion specific (ATP synthase F(0) sector subunit c) (F-type ATPase subunit c) (F-ATPase subunit c) (Lipid-binding protein)

 ATPL_CLOPD              Reviewed;          84 AA.
Q0ZS24;
03-MAR-2009, integrated into UniProtKB/Swiss-Prot.
22-AUG-2006, sequence version 1.
12-SEP-2018, entry version 57.
RecName: Full=ATP synthase subunit c, sodium ion specific;
AltName: Full=ATP synthase F(0) sector subunit c;
AltName: Full=F-type ATPase subunit c;
Short=F-ATPase subunit c;
AltName: Full=Lipid-binding protein;
Name=atpE;
Clostridium paradoxum.
Bacteria; Firmicutes; Clostridia; Clostridiales;
Peptostreptococcaceae.
NCBI_TaxID=29346;
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA], SUBSTRATE, FUNCTION, SUBUNIT,
INHIBITION, AND SUBCELLULAR LOCATION.
STRAIN=ATCC 51510 / DSM 7308 / CIP 105527 / JW-YL-7;
PubMed=16816177; DOI=10.1128/JB.00128-06;
Ferguson S.A., Keis S., Cook G.M.;
"Biochemical and molecular characterization of a Na+-translocating
F1Fo-ATPase from the thermoalkaliphilic bacterium Clostridium
paradoxum.";
J. Bacteriol. 188:5045-5054(2006).
[2]
MASS SPECTROMETRY, SUBUNIT, AND PRELIMINARY CRYSTALLIZATION.
STRAIN=ATCC 51510 / DSM 7308 / CIP 105527 / JW-YL-7;
PubMed=16980459; DOI=10.1128/JB.00934-06;
Meier T., Ferguson S.A., Cook G.M., Dimroth P., Vonck J.;
"Structural investigations of the membrane-embedded rotor ring of the
F-ATPase from Clostridium paradoxum.";
J. Bacteriol. 188:7759-7764(2006).
-!- FUNCTION: F(1)F(0) ATP synthase produces ATP from ADP in the
presence of a sodium gradient. F-type ATPases consist of two
structural domains, F(1) containing the extramembraneous catalytic
core and F(0) containing the membrane proton channel, linked
together by a central stalk and a peripheral stalk. During
catalysis, ATP synthesis in the catalytic domain of F(1) is
coupled via a rotary mechanism of the central stalk subunits to
proton translocation. {ECO:0000269|PubMed:16816177}.
-!- FUNCTION: Key component of the F(0) channel; it plays a direct
role in translocation across the membrane. A homomeric c-ring of
11 subunits forms the central stalk rotor element with the F(1)
delta and epsilon subunits. {ECO:0000269|PubMed:16816177}.
-!- FUNCTION: In this organism this enzyme may function as an ATP-
driven Na(+) ion pump to generate a Na(+) ion electrochemical
gradient rather than as an ATP synthase.
{ECO:0000269|PubMed:16816177}.
-!- ACTIVITY REGULATION: Inhibited by dicyclohexylcarbodiimide; the
enzyme is protected from inhibition by Na(+) in a pH-dependent
manner.
-!- SUBUNIT: F-type ATPases have 2 components, F(1) - the catalytic
core - and F(0) - the membrane sodium channel. F(1) has five
subunits: alpha(3), beta(3), gamma(1), delta(1), epsilon(1). F(0)
has three main subunits: a(1), b(2) and c(11). The alpha and beta
chains form an alternating ring which encloses part of the gamma
chain. F(1) is attached to F(0) by a central stalk formed by the
gamma and epsilon chains, while a peripheral stalk is formed by
the delta and b chains. {ECO:0000269|PubMed:16816177,
ECO:0000269|PubMed:16980459}.
-!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:16816177};
Multi-pass membrane protein {ECO:0000269|PubMed:16816177}.
-!- MASS SPECTROMETRY: Mass=8266; Method=MALDI; Range=1-84;
Evidence={ECO:0000269|PubMed:16980459};
-!- MISCELLANEOUS: The ATPase of C.paradoxum is of special interest
because it uses sodium ions instead of protons as the
physiological coupling ion.
-!- SIMILARITY: Belongs to the ATPase C chain family. {ECO:0000305}.
-----------------------------------------------------------------------
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EMBL; DQ193538; ABB13421.1; -; Genomic_DNA.
ProteinModelPortal; Q0ZS24; -.
SMR; Q0ZS24; -.
BRENDA; 3.6.3.14; 8815.
GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
GO; GO:0045263; C:proton-transporting ATP synthase complex, coupling factor F(o); IEA:UniProtKB-KW.
GO; GO:0008289; F:lipid binding; IEA:UniProtKB-KW.
GO; GO:0015078; F:proton transmembrane transporter activity; IEA:InterPro.
GO; GO:0015991; P:ATP hydrolysis coupled proton transport; IEA:InterPro.
GO; GO:0015986; P:ATP synthesis coupled proton transport; IEA:InterPro.
GO; GO:0006814; P:sodium ion transport; IEA:UniProtKB-KW.
Gene3D; 1.20.20.10; -; 1.
HAMAP; MF_01396; ATP_synth_c_bact; 1.
InterPro; IPR005953; ATP_synth_csu_bac/chlpt.
InterPro; IPR000454; ATP_synth_F0_csu.
InterPro; IPR038662; ATP_synth_F0_csu_sf.
InterPro; IPR002379; ATPase_proteolipid_c-like_dom.
InterPro; IPR035921; F/V-ATP_Csub_sf.
PANTHER; PTHR10031; PTHR10031; 1.
Pfam; PF00137; ATP-synt_C; 1.
PRINTS; PR00124; ATPASEC.
SUPFAM; SSF81333; SSF81333; 1.
TIGRFAMs; TIGR01260; ATP_synt_c; 1.
1: Evidence at protein level;
ATP synthesis; Cell membrane; CF(0); Hydrogen ion transport;
Ion transport; Lipid-binding; Membrane; Sodium; Sodium transport;
Transmembrane; Transmembrane helix; Transport.
CHAIN 1 84 ATP synthase subunit c, sodium ion
specific.
/FTId=PRO_0000365872.
TRANSMEM 6 26 Helical. {ECO:0000255}.
TRANSMEM 64 84 Helical. {ECO:0000255}.
SITE 65 65 Reversibly binds sodium during transport.
{ECO:0000305}.
SEQUENCE 84 AA; 8257 MW; 13DD93B439C433A1 CRC64;
MERALILAAS AIGAGLAMIA GIGPGIGQGF AAGKGAEAVG KQPEAQGDIL RTMLLGAAVA
ESTGIYALVV ALILLFANPL LNLL


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