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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_PROMO              Reviewed;          89 AA.
P21905;
01-MAY-1991, integrated into UniProtKB/Swiss-Prot.
01-MAY-1991, sequence version 1.
07-OCT-2020, entry version 112.
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; Synonyms=uncE;
Propionigenium modestum.
Bacteria; Fusobacteria; Fusobacteriales; Fusobacteriaceae; Propionigenium.
NCBI_TaxID=2333;
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND PROTEIN SEQUENCE OF 1-34.
STRAIN=DSM 2376 / Gra Succ2;
PubMed=2146118; DOI=10.1111/j.1432-1033.1990.tb19352.x;
Ludwig W., Kaim G., Laubinger W., Dimroth P., Hoppe J., Schleifer K.H.;
"Sequence of subunit c of the sodium ion translocating adenosine
triphosphate synthase of Propionigenium modestum.";
Eur. J. Biochem. 193:395-399(1990).
[2]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
STRAIN=DSM 2376 / Gra Succ2;
PubMed=1386022; DOI=10.1111/j.1432-1033.1992.tb17072.x;
Kaim G.W., Ludwig W., Dimroth P., Schleifer K.H.;
"Cloning, sequencing and in vivo expression of genes encoding the F0 part
of the sodium-ion-dependent ATP synthase of Propionigenium modestum in
Escherichia coli.";
Eur. J. Biochem. 207:463-470(1992).
[3]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
STRAIN=DSM 2376 / Gra Succ2;
PubMed=2170948; DOI=10.1093/nar/18.19.5887;
Esser U., Krumholz L.R., Simoni R.D.;
"Nucleotide sequence of the F0 subunits of the sodium dependent F1F0 ATPase
of Propionigenium modestum.";
Nucleic Acids Res. 18:5887-5888(1990).
[4]
PROTEIN SEQUENCE OF 1-7.
PubMed=8422943; DOI=10.1016/0014-5793(93)81742-i;
Gerike U., Dimroth P.;
"N-terminal amino acid sequences of the subunits of the Na(+)-translocating
F1F0 ATPase from Propionigenium modestum.";
FEBS Lett. 316:89-92(1993).
[5]
DISCUSSION OF SEQUENCE.
PubMed=1533602; DOI=10.1016/0378-1097(92)90559-7;
Krumholz L.R., Esser U., Simoni R.D.;
"Characterization of the genes coding for the F1F0 subunits of the sodium
dependent ATPase of Propionigenium modestum.";
FEMS Microbiol. Lett. 70:37-41(1992).
-!- FUNCTION: F(1)F(0) ATP synthase produces ATP from ADP in the presence
of a proton or sodium gradient. F-type ATPases consist of two
structural domains, F(1) containing the extramembraneous catalytic core
and F(0) containing the membrane sodium 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 sodium translocation.
-!- FUNCTION: Key component of the F(0) channel; it plays a direct role in
translocation across the membrane. A homomeric c-ring of between 10-14
subunits forms the central stalk rotor element with the F(1) delta and
epsilon subunits (Probable). {ECO:0000305}.
-!- 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(10-14). 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
(By similarity). {ECO:0000250}.
-!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Multi-pass membrane
protein {ECO:0000305}.
-!- MISCELLANEOUS: The ATPase of P.modestum 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; X53845; CAA37840.1; -; Genomic_DNA.
EMBL; X66102; CAA46895.1; -; Genomic_DNA.
EMBL; X53960; CAA37912.1; -; Genomic_DNA.
EMBL; X58461; CAA41369.1; -; Genomic_DNA.
PIR; S23322; S23322.
BMRB; P21905; -.
SMR; P21905; -.
DrugBank; DB03143; Nonan-1-Ol.
TCDB; 3.A.2.1.2; the h(+)- or na(+)-translocating f-type, v-type and a-type atpase (f-atpase) superfamily.
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:0046933; F:proton-transporting ATP synthase activity, rotational mechanism; IEA:UniProtKB-UniRule.
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; IPR020537; ATP_synth_F0_csu_DDCD_BS.
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.
PROSITE; PS00605; ATPASE_C; 1.
1: Evidence at protein level;
ATP synthesis; Cell membrane; CF(0); Direct protein sequencing;
Hydrogen ion transport; Ion transport; Lipid-binding; Membrane; Sodium;
Sodium transport; Transmembrane; Transmembrane helix; Transport.
CHAIN 1..89
/note="ATP synthase subunit c, sodium ion specific"
/id="PRO_0000112158"
TRANSMEM 9..29
/note="Helical"
/evidence="ECO:0000255"
TRANSMEM 68..88
/note="Helical"
/evidence="ECO:0000255"
SITE 65
/note="Reversibly binds sodium during transport"
/evidence="ECO:0000250"
SEQUENCE 89 AA; 8731 MW; B78210162391DD62 CRC64;
MDMVLAKTVV LAASAVGAGA AMIAGIGPGV GQGYAAGKAV ESVARQPEAK GDIISTMVLG
QAIAESTGIY SLVIALILLY ANPFVGLLG


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[atpE atpH tlr0431] ATP synthase subunit c (ATP synthase F(0) sector subunit c) (F-type ATPase subunit c) (F-ATPase subunit c) (Lipid-binding protein)
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[ATP5MC2 ATP5G2] ATP synthase F(0) complex subunit C2, mitochondrial (ATP synthase lipid-binding protein) (ATP synthase membrane subunit c locus 2) (ATP synthase proteolipid P2) (ATPase protein 9) (ATPase subunit c)
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