ATPL_PROMO
ID ATPL_PROMO Reviewed; 89 AA.
AC P21905;
DT 01-MAY-1991, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-1991, sequence version 1.
DT 25-MAY-2022, entry version 115.
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; Synonyms=uncE;
OS Propionigenium modestum.
OC Bacteria; Fusobacteria; Fusobacteriales; Fusobacteriaceae; Propionigenium.
OX NCBI_TaxID=2333;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND PROTEIN SEQUENCE OF 1-34.
RC STRAIN=DSM 2376 / Gra Succ2;
RX PubMed=2146118; DOI=10.1111/j.1432-1033.1990.tb19352.x;
RA Ludwig W., Kaim G., Laubinger W., Dimroth P., Hoppe J., Schleifer K.H.;
RT "Sequence of subunit c of the sodium ion translocating adenosine
RT triphosphate synthase of Propionigenium modestum.";
RL Eur. J. Biochem. 193:395-399(1990).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=DSM 2376 / Gra Succ2;
RX PubMed=1386022; DOI=10.1111/j.1432-1033.1992.tb17072.x;
RA Kaim G.W., Ludwig W., Dimroth P., Schleifer K.H.;
RT "Cloning, sequencing and in vivo expression of genes encoding the F0 part
RT of the sodium-ion-dependent ATP synthase of Propionigenium modestum in
RT Escherichia coli.";
RL Eur. J. Biochem. 207:463-470(1992).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=DSM 2376 / Gra Succ2;
RX PubMed=2170948; DOI=10.1093/nar/18.19.5887;
RA Esser U., Krumholz L.R., Simoni R.D.;
RT "Nucleotide sequence of the F0 subunits of the sodium dependent F1F0 ATPase
RT of Propionigenium modestum.";
RL Nucleic Acids Res. 18:5887-5888(1990).
RN [4]
RP PROTEIN SEQUENCE OF 1-7.
RX PubMed=8422943; DOI=10.1016/0014-5793(93)81742-i;
RA Gerike U., Dimroth P.;
RT "N-terminal amino acid sequences of the subunits of the Na(+)-translocating
RT F1F0 ATPase from Propionigenium modestum.";
RL FEBS Lett. 316:89-92(1993).
RN [5]
RP DISCUSSION OF SEQUENCE.
RX PubMed=1533602; DOI=10.1016/0378-1097(92)90559-7;
RA Krumholz L.R., Esser U., Simoni R.D.;
RT "Characterization of the genes coding for the F1F0 subunits of the sodium
RT dependent ATPase of Propionigenium modestum.";
RL FEMS Microbiol. Lett. 70:37-41(1992).
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 between 10-14
CC subunits forms the central stalk rotor element with the F(1) delta and
CC epsilon subunits (Probable). {ECO:0000305}.
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(10-14). 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 (By similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Multi-pass membrane
CC protein {ECO:0000305}.
CC -!- MISCELLANEOUS: The ATPase of P.modestum is of special interest because
CC it uses sodium ions instead of protons as the physiological coupling
CC ion.
CC -!- SIMILARITY: Belongs to the ATPase C chain family. {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; X53845; CAA37840.1; -; Genomic_DNA.
DR EMBL; X66102; CAA46895.1; -; Genomic_DNA.
DR EMBL; X53960; CAA37912.1; -; Genomic_DNA.
DR EMBL; X58461; CAA41369.1; -; Genomic_DNA.
DR PIR; S23322; S23322.
DR AlphaFoldDB; P21905; -.
DR BMRB; P21905; -.
DR SMR; P21905; -.
DR DrugBank; DB03143; Nonan-1-Ol.
DR TCDB; 3.A.2.1.2; the h(+)- or na(+)-translocating f-type, v-type and a-type atpase (f-atpase) superfamily.
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 ATP synthesis; Cell membrane; CF(0); Direct protein sequencing;
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_0000112158"
FT TRANSMEM 9..29
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 68..88
FT /note="Helical"
FT /evidence="ECO:0000255"
FT SITE 65
FT /note="Reversibly binds sodium during transport"
FT /evidence="ECO:0000250"
SQ SEQUENCE 89 AA; 8731 MW; B78210162391DD62 CRC64;
MDMVLAKTVV LAASAVGAGA AMIAGIGPGV GQGYAAGKAV ESVARQPEAK GDIISTMVLG
QAIAESTGIY SLVIALILLY ANPFVGLLG
