ATPL_ILYTA
ID ATPL_ILYTA Reviewed; 89 AA.
AC Q8KRV3;
DT 03-MAR-2009, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2002, sequence version 1.
DT 25-MAY-2022, entry version 87.
DE RecName: Full=ATP synthase subunit c, sodium ion specific;
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;
OS Ilyobacter tartaricus.
OC Bacteria; Fusobacteria; Fusobacteriales; Fusobacteriaceae; Ilyobacter.
OX NCBI_TaxID=167644;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 35898 / DSM 2382;
RX PubMed=12531483; DOI=10.1016/s0167-4781(02)00625-5;
RA Meier T., von Ballmoos C., Neumann S., Kaim G.;
RT "Complete DNA sequence of the atp operon of the sodium-dependent F1Fo ATP
RT synthase from Ilyobacter tartaricus and identification of the encoded
RT subunits.";
RL Biochim. Biophys. Acta 1625:221-226(2003).
RN [2]
RP X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS), AND SUBUNIT.
RX PubMed=15860619; DOI=10.1126/science.1111199;
RA Meier T., Polzer P., Diederichs K., Welte W., Dimroth P.;
RT "Structure of the rotor ring of F-Type Na+-ATPase from Ilyobacter
RT tartaricus.";
RL Science 308:659-662(2005).
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 sodium 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 sodium 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 11 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 sodium 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(11). 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:15860619}.
CC -!- SUBCELLULAR LOCATION: Cell inner membrane; Multi-pass membrane protein.
CC -!- MISCELLANEOUS: The ATPase of I.tartaricus is of special interest
CC because it uses sodium ions instead of protons as the physiological
CC coupling ion.
CC -!- SIMILARITY: Belongs to the ATPase C chain family. {ECO:0000305}.
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DR EMBL; AF522463; AAM94908.1; -; Genomic_DNA.
DR PDB; 1YCE; X-ray; 2.40 A; A/B/C/D/E/F/G/H/I/J/K/L/M/N/O/P/Q/R/S/T/U/V/a/b/c/d/e/f/g/h/i/j/k/l/m/n/o/p/q/r/s/t/u/v=1-89.
DR PDB; 2WGM; X-ray; 2.35 A; A/B/C/D/E/F/G/H/I/J/K/L/M/N/O/P/Q/R/S/T/U/V/a/b/c/d/e/f/g/h/i/j/k/l/m/n/o/p/q/r/s/t/u/v=1-89.
DR PDBsum; 1YCE; -.
DR PDBsum; 2WGM; -.
DR AlphaFoldDB; Q8KRV3; -.
DR SMR; Q8KRV3; -.
DR EvolutionaryTrace; Q8KRV3; -.
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 GO; GO:0006814; P:sodium ion transport; IEA:UniProtKB-KW.
DR Gene3D; 1.20.120.610; -; 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; 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 inner membrane; Cell membrane; CF(0);
KW Hydrogen ion transport; Ion transport; Lipid-binding; Membrane; Sodium;
KW Sodium transport; Transmembrane; Transmembrane helix; Transport.
FT CHAIN 1..89
FT /note="ATP synthase subunit c, sodium ion specific"
FT /id="PRO_0000365891"
FT TOPO_DOM 1..8
FT /note="Periplasmic"
FT TRANSMEM 9..29
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 30..67
FT /note="Cytoplasmic"
FT TRANSMEM 68..88
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 89
FT /note="Periplasmic"
FT SITE 65
FT /note="Reversibly binds sodium during transport"
FT HELIX 3..21
FT /evidence="ECO:0007829|PDB:2WGM"
FT HELIX 22..25
FT /evidence="ECO:0007829|PDB:2WGM"
FT HELIX 26..45
FT /evidence="ECO:0007829|PDB:2WGM"
FT HELIX 47..49
FT /evidence="ECO:0007829|PDB:2WGM"
FT HELIX 50..80
FT /evidence="ECO:0007829|PDB:2WGM"
FT TURN 85..87
FT /evidence="ECO:0007829|PDB:2WGM"
SQ SEQUENCE 89 AA; 8795 MW; BC23BE5DC1FD76C5 CRC64;
MDMLFAKTVV LAASAVGAGT AMIAGIGPGV GQGYAAGKAV ESVARQPEAK GDIISTMVLG
QAVAESTGIY SLVIALILLY ANPFVGLLG
