ATPL_BACP3
ID ATPL_BACP3 Reviewed; 72 AA.
AC P00845;
DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT 21-JUL-1986, sequence version 1.
DT 25-MAY-2022, entry version 116.
DE RecName: Full=ATP synthase subunit c;
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; Synonyms=uncE;
OS Bacillus sp. (strain PS3).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX NCBI_TaxID=2334;
RN [1]
RP PROTEIN SEQUENCE, AND FORMYLATION AT MET-1.
RX PubMed=6447066; DOI=10.1111/j.1432-1033.1980.tb04624.x;
RA Hoppe J., Sebald W.;
RT "Amino acid sequence of the proteolipid subunit of the proton-translocating
RT ATPase complex from the thermophilic bacterium PS-3.";
RL Eur. J. Biochem. 107:57-65(1980).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE, AND SUBUNIT.
RX PubMed=2894854; DOI=10.1016/0005-2728(88)90064-3;
RA Ohta S., Yohda M., Ishizuka M., Hirata H., Hamamoto T.,
RA Otawara-Hamamoto Y., Matsuda K., Kagawa Y.;
RT "Sequence and over-expression of subunits of adenosine triphosphate
RT synthase in thermophilic bacterium PS3.";
RL Biochim. Biophys. Acta 933:141-155(1988).
RN [3]
RP SUBUNIT, SUBUNIT C FUSIONS, AND MUTAGENESIS OF GLU-56.
RX PubMed=15302927; DOI=10.1073/pnas.0403545101;
RA Mitome N., Suzuki T., Hayashi S., Yoshida M.;
RT "Thermophilic ATP synthase has a decamer c-ring: indication of noninteger
RT 10:3 H+/ATP ratio and permissive elastic coupling.";
RL Proc. Natl. Acad. Sci. U.S.A. 101:12159-12164(2004).
RN [4]
RP STRUCTURE BY NMR.
RX PubMed=16497328; DOI=10.1016/j.jmb.2006.01.011;
RA Nakano T., Ikegami T., Suzuki T., Yoshida M., Akutsu H.;
RT "A new solution structure of ATP synthase subunit c from thermophilic
RT Bacillus PS3, suggesting a local conformational change for H+-
RT translocation.";
RL J. Mol. Biol. 358:132-144(2006).
CC -!- FUNCTION: F(1)F(0) ATP synthase produces ATP from ADP in the presence
CC of a proton or sodium gradient. F-type ATPases consist of two
CC structural domains, F(1) containing the extramembraneous catalytic core
CC and F(0) containing the membrane proton channel, linked together by a
CC central stalk and a peripheral stalk. During catalysis, ATP synthesis
CC in the catalytic domain of F(1) is coupled via a rotary mechanism of
CC the central stalk subunits to proton translocation.
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 10 subunits
CC forms the central stalk rotor element with the F(1) delta and epsilon
CC subunits.
CC -!- SUBUNIT: F-type ATPases have 2 components, F(1) - the catalytic core
CC - and F(0) - the membrane proton 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(10). 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:15302927, ECO:0000269|PubMed:2894854}.
CC -!- SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein.
CC -!- MISCELLANEOUS: Dicyclohexylcarbodiimide (DCDD) binding to the active
CC aspartate residue inhibits ATPase in vitro.
CC -!- MISCELLANEOUS: Fusion proteins corresponding to c(2), c(5) and c(10)
CC permit ATP synthesis in reconstitution experiments with F(1) and in the
CC absence of F(1) function as a proton channel; other fusions of c(3) to
CC c(14) do not.
CC -!- SIMILARITY: Belongs to the ATPase C chain family. {ECO:0000305}.
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DR EMBL; X07804; CAA30649.1; -; Genomic_DNA.
DR PDB; 1WU0; NMR; -; A=1-72.
DR PDB; 6N2D; EM; 3.30 A; c0/c1/c2/c3/c4/c5/c6/c7/c8/c9=1-72.
DR PDB; 6N2Y; EM; 3.00 A; c0/c1/c2/c3/c4/c5/c6/c7/c8/c9=1-72.
DR PDB; 6N2Z; EM; 3.00 A; c0/c1/c2/c3/c4/c5/c6/c7/c8/c9=1-72.
DR PDB; 6N30; EM; 3.20 A; c0/c1/c2/c3/c4/c5/c6/c7/c8/c9=1-72.
DR PDBsum; 1WU0; -.
DR PDBsum; 6N2D; -.
DR PDBsum; 6N2Y; -.
DR PDBsum; 6N2Z; -.
DR PDBsum; 6N30; -.
DR AlphaFoldDB; P00845; -.
DR BMRB; P00845; -.
DR SMR; P00845; -.
DR ChEMBL; CHEMBL3308989; -.
DR TCDB; 3.A.2.1.14; the h(+)- or na(+)-translocating f-type, v-type and a-type atpase (f-atpase) superfamily.
DR EvolutionaryTrace; P00845; -.
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 Gene3D; 1.20.20.10; -; 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; IPR020537; ATP_synth_F0_csu_DDCD_BS.
DR InterPro; IPR038662; ATP_synth_F0_csu_sf.
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.
DR PROSITE; PS00605; ATPASE_C; 1.
PE 1: Evidence at protein level;
KW 3D-structure; ATP synthesis; Cell membrane; CF(0);
KW Direct protein sequencing; Formylation; Hydrogen ion transport;
KW Ion transport; Lipid-binding; Membrane; Transmembrane; Transmembrane helix;
KW Transport.
FT CHAIN 1..72
FT /note="ATP synthase subunit c"
FT /id="PRO_0000112137"
FT TRANSMEM 1..21
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 48..68
FT /note="Helical"
FT /evidence="ECO:0000255"
FT SITE 56
FT /note="Reversibly protonated during proton transport"
FT MOD_RES 1
FT /note="N-formylmethionine"
FT /evidence="ECO:0000269|PubMed:6447066"
FT MUTAGEN 56
FT /note="E->Q: Abolishes proton transport in the c(10) fusion
FT protein."
FT /evidence="ECO:0000269|PubMed:15302927"
FT HELIX 4..35
FT /evidence="ECO:0007829|PDB:1WU0"
FT TURN 39..42
FT /evidence="ECO:0007829|PDB:1WU0"
FT HELIX 43..55
FT /evidence="ECO:0007829|PDB:1WU0"
FT HELIX 57..70
FT /evidence="ECO:0007829|PDB:1WU0"
SQ SEQUENCE 72 AA; 7334 MW; 211ED1F2BD740FE1 CRC64;
MSLGVLAAAI AVGLGALGAG IGNGLIVSRT IEGIARQPEL RPVLQTTMFI GVALVEALPI
IGVVFSFIYL GR
