ATP6_PROMO
ID ATP6_PROMO Reviewed; 289 AA.
AC P21903;
DT 01-MAY-1991, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-1991, sequence version 1.
DT 25-MAY-2022, entry version 120.
DE RecName: Full=ATP synthase subunit a, sodium ion specific {ECO:0000255|HAMAP-Rule:MF_01393};
DE AltName: Full=ATP synthase F0 sector subunit a {ECO:0000255|HAMAP-Rule:MF_01393};
DE AltName: Full=F-ATPase subunit 6 {ECO:0000255|HAMAP-Rule:MF_01393};
GN Name=atpB {ECO:0000255|HAMAP-Rule:MF_01393}; Synonyms=uncB;
OS Propionigenium modestum.
OC Bacteria; Fusobacteria; Fusobacteriales; Fusobacteriaceae; Propionigenium.
OX NCBI_TaxID=2333;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=DSM 2376 / Gra Succ2;
RX PubMed=2174545; DOI=10.1093/nar/18.22.6697;
RA Kaim G.W., Ludwig W., Dimroth P., Schleifer K.H.;
RT "Sequence of subunits a and b of the sodium ion translocating adenosine
RT triphosphate synthase of Propionigenium modestum.";
RL Nucleic Acids Res. 18:6697-6697(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 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: Key component of the proton channel; it plays a direct role
CC in the translocation of protons across the membrane.
CC -!- SUBUNIT: F-type ATPases have 2 components, CF(1) - the catalytic core
CC - and CF(0) - the membrane proton channel. CF(1) has five subunits:
CC alpha(3), beta(3), gamma(1), delta(1), epsilon(1). CF(0) has three main
CC subunits: a(1), b(2) and c(9-12). The alpha and beta chains form an
CC alternating ring which encloses part of the gamma chain. CF(1) is
CC attached to CF(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 -!- SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein.
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 A chain family. {ECO:0000255|HAMAP-
CC Rule:MF_01393}.
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DR EMBL; X54809; CAA38579.1; -; Genomic_DNA.
DR EMBL; X66102; CAA46894.1; -; Genomic_DNA.
DR EMBL; X53960; CAA37911.1; -; Genomic_DNA.
DR EMBL; X58461; CAA41368.1; -; Genomic_DNA.
DR PIR; S12619; S12619.
DR AlphaFoldDB; P21903; -.
DR SMR; P21903; -.
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: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; 1.20.120.220; -; 1.
DR HAMAP; MF_01393; ATP_synth_a_bact; 1.
DR InterPro; IPR045082; ATP_syn_F0_a_bact/chloroplast.
DR InterPro; IPR000568; ATP_synth_F0_asu.
DR InterPro; IPR023011; ATP_synth_F0_asu_AS.
DR InterPro; IPR035908; F0_ATP_A_sf.
DR PANTHER; PTHR42823; PTHR42823; 1.
DR Pfam; PF00119; ATP-synt_A; 1.
DR PRINTS; PR00123; ATPASEA.
DR SUPFAM; SSF81336; SSF81336; 1.
DR TIGRFAMs; TIGR01131; ATP_synt_6_or_A; 1.
DR PROSITE; PS00449; ATPASE_A; 1.
PE 3: Inferred from homology;
KW ATP synthesis; Cell membrane; CF(0); Hydrogen ion transport; Ion transport;
KW Membrane; Sodium; Sodium transport; Transmembrane; Transmembrane helix;
KW Transport.
FT CHAIN 1..289
FT /note="ATP synthase subunit a, sodium ion specific"
FT /id="PRO_0000082065"
FT TRANSMEM 7..27
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01393"
FT TRANSMEM 65..85
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01393"
FT TRANSMEM 129..149
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01393"
FT TRANSMEM 169..189
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01393"
FT TRANSMEM 231..251
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01393"
FT TRANSMEM 257..277
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01393"
FT CONFLICT 114
FT /note="Y -> I (in Ref. 3; CAA37911/CAA41368)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 289 AA; 32224 MW; 6EF6A9BE97A9129E CRC64;
MKKMGPIILA VVIAIGTFAL KMMGVIGFKT PPLVEGPKIM FYVPLPEAMH DFPFAMEMAS
GVYGFPVTIT VISTWFVMLF LIMVFRWSSK NLEVVPERKQ AFFETIYGFL DDLYGQLLGN
WKKKYFTYIG TLFLFLLISN IVSFFPIPGF SSENGVFSIA PALRTPTADL NTTVGLALLT
TYSFIAASFR TSGFFGFFKG LFEPMPLMFP INLAGEFAKP TNISIRLFGN MFAGMVILGL
LYKAAPVLIP APLHLYFDLF SGVVQSFVFI MLTMVYIQGS IGDAEYLED
