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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)

 H6LFT2_ACEWD            Unreviewed;        82 AA.
H6LFT2;
18-APR-2012, integrated into UniProtKB/TrEMBL.
18-APR-2012, sequence version 1.
10-OCT-2018, entry version 54.
RecName: Full=ATP synthase subunit c {ECO:0000256|HAMAP-Rule:MF_01396};
AltName: Full=ATP synthase F(0) sector subunit c {ECO:0000256|HAMAP-Rule:MF_01396};
AltName: Full=F-type ATPase subunit c {ECO:0000256|HAMAP-Rule:MF_01396};
Short=F-ATPase subunit c {ECO:0000256|HAMAP-Rule:MF_01396};
AltName: Full=Lipid-binding protein {ECO:0000256|HAMAP-Rule:MF_01396};
Name=atpE3 {ECO:0000313|EMBL:AFA47027.1};
Synonyms=atpE {ECO:0000256|HAMAP-Rule:MF_01396},
atpE2 {ECO:0000313|EMBL:AFA47026.1};
OrderedLocusNames=Awo_c02170 {ECO:0000313|EMBL:AFA47026.1},
Awo_c02180 {ECO:0000313|EMBL:AFA47027.1};
Acetobacterium woodii (strain ATCC 29683 / DSM 1030 / JCM 2381 / KCTC
1655 / WB1).
Bacteria; Firmicutes; Clostridia; Clostridiales; Eubacteriaceae;
Acetobacterium.
NCBI_TaxID=931626 {ECO:0000313|EMBL:AFA47027.1, ECO:0000313|Proteomes:UP000007177};
[1] {ECO:0000313|Proteomes:UP000007177}
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=ATCC 29683 / DSM 1030 / JCM 2381 / KCTC 1655 / WB1
{ECO:0000313|Proteomes:UP000007177};
Poehlein A., Schmidt S., Kaster A.-K., Goenrich M., Vollmers J.,
Thuermer A., Gottschalk G., Thauer R.K., Daniel R., Mueller V.;
"Complete genome sequence of Acetobacterium woodii.";
Submitted (JUL-2011) to the EMBL/GenBank/DDBJ databases.
[2] {ECO:0000313|EMBL:AFA47027.1}
NUCLEOTIDE SEQUENCE.
STRAIN=DSM 1030 {ECO:0000313|EMBL:AFA47027.1};
PubMed=22479398; DOI=10.1371/journal.pone.0033439;
Poehlein A., Schmidt S., Kaster A.K., Goenrich M., Vollmers J.,
Thurmer A., Bertsch J., Schuchmann K., Voigt B., Hecker M., Daniel R.,
Thauer R.K., Gottschalk G., Muller V.;
"An ancient pathway combining carbon dioxide fixation with the
generation and utilization of a sodium ion gradient for ATP
synthesis.";
PLoS ONE 7:E33439-E33439(2012).
[3] {ECO:0000213|PDB:4BEM}
X-RAY CRYSTALLOGRAPHY (2.10 ANGSTROMS).
PubMed=25381992; DOI=10.1038/NCOMMS6286;
Matthies D., Zhou W., Klyszejko A.L., Anselmi C., Yildiz O.,
Brandt K., Muller V., Faraldo-Gomez J.D., Meier T.;
"High-resolution structure and mechanism of an F/V-hybrid rotor ring
in a Na-coupled ATP synthase.";
Nat. Commun. 5:5286-5286(2014).
-!- 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. {ECO:0000256|HAMAP-Rule:MF_01396}.
-!- 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. {ECO:0000256|HAMAP-
Rule:MF_01396}.
-!- 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(10-14). 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. {ECO:0000256|HAMAP-Rule:MF_01396}.
-!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000256|HAMAP-
Rule:MF_01396}; Multi-pass membrane protein {ECO:0000256|HAMAP-
Rule:MF_01396}.
-!- SIMILARITY: Belongs to the ATPase C chain family.
{ECO:0000256|HAMAP-Rule:MF_01396}.
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EMBL; CP002987; AFA47026.1; -; Genomic_DNA.
EMBL; CP002987; AFA47027.1; -; Genomic_DNA.
RefSeq; WP_014354630.1; NC_016894.1.
PDB; 4BEM; X-ray; 2.10 A; A/B/C/D/E/F/G/H/I=1-82.
PDBsum; 4BEM; -.
SMR; H6LFT2; -.
STRING; 931626.Awo_c02180; -.
EnsemblBacteria; AFA47026; AFA47026; Awo_c02170.
EnsemblBacteria; AFA47027; AFA47027; Awo_c02180.
KEGG; awo:Awo_c02170; -.
KEGG; awo:Awo_c02180; -.
eggNOG; ENOG4105VH4; Bacteria.
eggNOG; COG0636; LUCA.
KO; K02110; -.
OMA; ESIAIYC; -.
OrthoDB; POG091H043Z; -.
BioCyc; AWOO931626:G1H37-227-MONOMER; -.
BioCyc; AWOO931626:G1H37-228-MONOMER; -.
Proteomes; UP000007177; Chromosome.
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:0015991; P:ATP hydrolysis coupled proton transport; IEA:InterPro.
GO; GO:0015986; P:ATP synthesis coupled proton transport; IEA:UniProtKB-UniRule.
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;
3D-structure {ECO:0000213|PDB:4BEM};
ATP synthesis {ECO:0000256|HAMAP-Rule:MF_01396};
Cell membrane {ECO:0000256|HAMAP-Rule:MF_01396};
CF(0) {ECO:0000256|HAMAP-Rule:MF_01396};
Complete proteome {ECO:0000313|Proteomes:UP000007177};
Hydrogen ion transport {ECO:0000256|HAMAP-Rule:MF_01396};
Hydrolase {ECO:0000313|EMBL:AFA47027.1};
Ion transport {ECO:0000256|HAMAP-Rule:MF_01396};
Lipid-binding {ECO:0000256|HAMAP-Rule:MF_01396};
Membrane {ECO:0000256|HAMAP-Rule:MF_01396};
Reference proteome {ECO:0000313|Proteomes:UP000007177};
Transmembrane {ECO:0000256|HAMAP-Rule:MF_01396};
Transmembrane helix {ECO:0000256|HAMAP-Rule:MF_01396};
Transport {ECO:0000256|HAMAP-Rule:MF_01396}.
TRANSMEM 6 33 Helical. {ECO:0000256|HAMAP-
Rule:MF_01396}.
TRANSMEM 54 78 Helical. {ECO:0000256|HAMAP-
Rule:MF_01396}.
DOMAIN 13 75 ATP-synt_C. {ECO:0000259|Pfam:PF00137}.
SITE 62 62 Reversibly protonated during proton
transport. {ECO:0000256|HAMAP-
Rule:MF_01396}.
SEQUENCE 82 AA; 8182 MW; 1B103E6B5640A840 CRC64;
MEGLDFIKAC SAIGAGIAMI AGVGPGIGQG FAAGKGAEAV GRQPEAQSDI IRTMLLGAAV
AETTGIYGLI VALILLFANP FF


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