ATPD_PROMO
ID ATPD_PROMO Reviewed; 174 AA.
AC P29708;
DT 01-APR-1993, integrated into UniProtKB/Swiss-Prot.
DT 01-APR-1993, sequence version 1.
DT 25-MAY-2022, entry version 96.
DE RecName: Full=ATP synthase subunit delta, sodium ion specific {ECO:0000255|HAMAP-Rule:MF_01416};
DE AltName: Full=ATP synthase F(1) sector subunit delta {ECO:0000255|HAMAP-Rule:MF_01416};
DE AltName: Full=F-type ATPase subunit delta {ECO:0000255|HAMAP-Rule:MF_01416};
DE Short=F-ATPase subunit delta {ECO:0000255|HAMAP-Rule:MF_01416};
GN Name=atpH {ECO:0000255|HAMAP-Rule:MF_01416}; Synonyms=uncH;
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=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).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-118.
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 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).
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. {ECO:0000255|HAMAP-
CC Rule:MF_01416}.
CC -!- FUNCTION: This protein is part of the stalk that links CF(0) to CF(1).
CC It either transmits conformational changes from CF(0) to CF(1) or is
CC implicated in proton conduction. {ECO:0000255|HAMAP-Rule:MF_01416}.
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(10-14). 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 {ECO:0000255|HAMAP-Rule:MF_01416}.
CC -!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000255|HAMAP-
CC Rule:MF_01416}; Peripheral membrane protein {ECO:0000255|HAMAP-
CC Rule:MF_01416}.
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 delta chain family.
CC {ECO:0000255|HAMAP-Rule:MF_01416}.
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DR EMBL; X58461; CAA41371.1; -; Genomic_DNA.
DR EMBL; X66102; CAA46897.1; -; Genomic_DNA.
DR PIR; S29038; S29038.
DR AlphaFoldDB; P29708; -.
DR SMR; P29708; -.
DR TCDB; 3.A.2.1.2; the h(+)- or na(+)-translocating f-type, v-type and a-type atpase (f-atpase) superfamily.
DR PRIDE; P29708; -.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0045261; C:proton-transporting ATP synthase complex, catalytic core F(1); 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; 1.10.520.20; -; 1.
DR HAMAP; MF_01416; ATP_synth_delta_bact; 1.
DR InterPro; IPR026015; ATP_synth_OSCP/delta_N_sf.
DR InterPro; IPR020781; ATPase_OSCP/d_CS.
DR InterPro; IPR000711; ATPase_OSCP/dsu.
DR PANTHER; PTHR11910; PTHR11910; 1.
DR Pfam; PF00213; OSCP; 1.
DR PRINTS; PR00125; ATPASEDELTA.
DR SUPFAM; SSF47928; SSF47928; 1.
DR TIGRFAMs; TIGR01145; ATP_synt_delta; 1.
DR PROSITE; PS00389; ATPASE_DELTA; 1.
PE 1: Evidence at protein level;
KW ATP synthesis; Cell inner membrane; Cell membrane; CF(1);
KW Direct protein sequencing; Hydrogen ion transport; Ion transport; Membrane;
KW Sodium; Sodium transport; Transport.
FT CHAIN 1..174
FT /note="ATP synthase subunit delta, sodium ion specific"
FT /id="PRO_0000193474"
FT CONFLICT 58..59
FT /note="KK -> FF (in Ref. 2; CAA46897)"
FT /evidence="ECO:0000305"
FT CONFLICT 113..117
FT /note="FAIEP -> LRMNL (in Ref. 2; CAA46897)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 174 AA; 19945 MW; 94C1E8A60A311295 CRC64;
MIEAQVGRRY AEAIYEIAES NDNVKELYET LNGVMELYNT DKEFKTLVDH PLIKREDKKE
FAKKIFGELE ESSLNIIFYL IEKDRLSSIR GIVAEYLKIY YAKNQILDVE AIFAIEPTKD
QKAKLIEQLE KKTGKKVNLE VSIDKSIIAG GIIKIGDEII DGSVRRQLDT IARS
