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ATP synthase subunit c (ATP synthase F(0) sector subunit c) (F-type ATPase subunit c) (F-ATPase subunit c) (Lipid-binding protein)

 ATPL_BACP3              Reviewed;          72 AA.
P00845;
21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
21-JUL-1986, sequence version 1.
28-MAR-2018, entry version 105.
RecName: Full=ATP synthase subunit c;
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;
Bacillus sp. (strain PS3).
Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus.
NCBI_TaxID=2334;
[1]
PROTEIN SEQUENCE, AND FORMYLATION AT MET-1.
PubMed=6447066; DOI=10.1111/j.1432-1033.1980.tb04624.x;
Hoppe J., Sebald W.;
"Amino acid sequence of the proteolipid subunit of the proton-
translocating ATPase complex from the thermophilic bacterium PS-3.";
Eur. J. Biochem. 107:57-65(1980).
[2]
NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE, AND SUBUNIT.
PubMed=2894854; DOI=10.1016/0005-2728(88)90064-3;
Ohta S., Yohda M., Ishizuka M., Hirata H., Hamamoto T.,
Otawara-Hamamoto Y., Matsuda K., Kagawa Y.;
"Sequence and over-expression of subunits of adenosine triphosphate
synthase in thermophilic bacterium PS3.";
Biochim. Biophys. Acta 933:141-155(1988).
[3]
SUBUNIT, SUBUNIT C FUSIONS, AND MUTAGENESIS OF GLU-56.
PubMed=15302927; DOI=10.1073/pnas.0403545101;
Mitome N., Suzuki T., Hayashi S., Yoshida M.;
"Thermophilic ATP synthase has a decamer c-ring: indication of
noninteger 10:3 H+/ATP ratio and permissive elastic coupling.";
Proc. Natl. Acad. Sci. U.S.A. 101:12159-12164(2004).
[4]
STRUCTURE BY NMR.
PubMed=16497328; DOI=10.1016/j.jmb.2006.01.011;
Nakano T., Ikegami T., Suzuki T., Yoshida M., Akutsu H.;
"A new solution structure of ATP synthase subunit c from thermophilic
Bacillus PS3, suggesting a local conformational change for H+-
translocation.";
J. Mol. Biol. 358:132-144(2006).
-!- 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 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.
-!- FUNCTION: Key component of the F(0) channel; it plays a direct
role in translocation across the membrane. A homomeric c-ring of
10 subunits forms the central stalk rotor element with the F(1)
delta and epsilon subunits.
-!- SUBUNIT: F-type ATPases have 2 components, F(1) - the catalytic
core - and F(0) - the membrane proton 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). 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:15302927,
ECO:0000269|PubMed:2894854}.
-!- SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein.
-!- MISCELLANEOUS: Dicyclohexylcarbodiimide (DCDD) binding to the
active aspartate residue inhibits ATPase in vitro.
-!- MISCELLANEOUS: Fusion proteins corresponding to c(2), c(5) and
c(10) permit ATP synthesis in reconstitution experiments with F(1)
and in the absence of F(1) function as a proton channel; other
fusions of c(3) to c(14) do not.
-!- SIMILARITY: Belongs to the ATPase C chain family. {ECO:0000305}.
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EMBL; X07804; CAA30649.1; -; Genomic_DNA.
PDB; 1WU0; NMR; -; A=1-72.
PDBsum; 1WU0; -.
ProteinModelPortal; P00845; -.
SMR; P00845; -.
EvolutionaryTrace; P00845; -.
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:0015078; F:hydrogen ion transmembrane transporter activity; IEA:InterPro.
GO; GO:0008289; F:lipid binding; IEA:UniProtKB-KW.
GO; GO:0015991; P:ATP hydrolysis coupled proton transport; IEA:InterPro.
GO; GO:0015986; P:ATP synthesis coupled proton transport; IEA:InterPro.
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; 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;
3D-structure; ATP synthesis; Cell membrane; CF(0);
Direct protein sequencing; Formylation; Hydrogen ion transport;
Ion transport; Lipid-binding; Membrane; Transmembrane;
Transmembrane helix; Transport.
CHAIN 1 72 ATP synthase subunit c.
/FTId=PRO_0000112137.
TRANSMEM 1 21 Helical. {ECO:0000255}.
TRANSMEM 48 68 Helical. {ECO:0000255}.
SITE 56 56 Reversibly protonated during proton
transport.
MOD_RES 1 1 N-formylmethionine.
{ECO:0000269|PubMed:6447066}.
MUTAGEN 56 56 E->Q: Abolishes proton transport in the
c(10) fusion protein.
{ECO:0000269|PubMed:15302927}.
HELIX 4 35 {ECO:0000244|PDB:1WU0}.
TURN 39 42 {ECO:0000244|PDB:1WU0}.
HELIX 43 55 {ECO:0000244|PDB:1WU0}.
HELIX 57 70 {ECO:0000244|PDB:1WU0}.
SEQUENCE 72 AA; 7334 MW; 211ED1F2BD740FE1 CRC64;
MSLGVLAAAI AVGLGALGAG IGNGLIVSRT IEGIARQPEL RPVLQTTMFI GVALVEALPI
IGVVFSFIYL GR


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