ATPA_PROMO
ID ATPA_PROMO Reviewed; 500 AA.
AC P29706;
DT 01-APR-1993, integrated into UniProtKB/Swiss-Prot.
DT 07-DEC-2004, sequence version 2.
DT 03-AUG-2022, entry version 135.
DE RecName: Full=ATP synthase subunit alpha, sodium ion specific;
DE EC=7.2.2.1;
DE AltName: Full=Na(+)-translocating ATPase subunit alpha;
GN Name=atpA {ECO:0000255|HAMAP-Rule:MF_01346}; Synonyms=uncA;
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;
RA Krumholz L.R., Esser U., Simoni R.D.;
RL Submitted (MAR-1991) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 140-269.
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 SEQUENCE REVISION TO 466-500.
RX PubMed=7556212; DOI=10.1111/j.1432-1033.1995.tb20849.x;
RA Gerike U., Kaim G.W., Dimroth P.;
RT "In vivo synthesis of ATPase complexes of Propionigenium modestum and
RT Escherichia coli and analysis of their function.";
RL Eur. J. Biochem. 232:596-602(1995).
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).
CC -!- FUNCTION: Produces ATP from ADP in the presence of a sodium ion
CC gradient across the membrane. The alpha chain is a regulatory subunit.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + H2O + 4 Na(+)(in) = ADP + H(+) + 4 Na(+)(out) +
CC phosphate; Xref=Rhea:RHEA:58156, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:29101, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:43474, ChEBI:CHEBI:456216; EC=7.2.2.1;
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, b and c.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000255|HAMAP-Rule:MF_01346};
CC Peripheral membrane protein {ECO:0000255|HAMAP-Rule:MF_01346}.
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 alpha/beta chains family.
CC {ECO:0000255|HAMAP-Rule:MF_01346}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAA41372.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; X58461; CAA41372.1; ALT_FRAME; Genomic_DNA.
DR EMBL; X66103; CAA46898.1; ALT_SEQ; Genomic_DNA.
DR PIR; S29039; S29039.
DR AlphaFoldDB; P29706; -.
DR SMR; P29706; -.
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: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:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0046933; F:proton-transporting ATP synthase activity, rotational mechanism; IEA:UniProtKB-UniRule.
DR GO; GO:0046932; F:sodium-transporting ATP synthase activity, rotational mechanism; IEA:UniProtKB-EC.
DR GO; GO:0046962; F:sodium-transporting ATPase activity, rotational mechanism; IEA:UniProtKB-EC.
DR CDD; cd18113; ATP-synt_F1_alpha_C; 1.
DR CDD; cd01132; F1_ATPase_alpha; 1.
DR Gene3D; 1.20.150.20; -; 1.
DR Gene3D; 2.40.30.20; -; 1.
DR Gene3D; 3.40.50.300; -; 1.
DR HAMAP; MF_01346; ATP_synth_alpha_bact; 1.
DR InterPro; IPR023366; ATP_synth_asu-like_sf.
DR InterPro; IPR000793; ATP_synth_asu_C.
DR InterPro; IPR038376; ATP_synth_asu_C_sf.
DR InterPro; IPR033732; ATP_synth_F1_a.
DR InterPro; IPR005294; ATP_synth_F1_asu.
DR InterPro; IPR020003; ATPase_a/bsu_AS.
DR InterPro; IPR004100; ATPase_F1/V1/A1_a/bsu_N.
DR InterPro; IPR036121; ATPase_F1/V1/A1_a/bsu_N_sf.
DR InterPro; IPR000194; ATPase_F1/V1/A1_a/bsu_nucl-bd.
DR InterPro; IPR027417; P-loop_NTPase.
DR Pfam; PF00006; ATP-synt_ab; 1.
DR Pfam; PF00306; ATP-synt_ab_C; 1.
DR Pfam; PF02874; ATP-synt_ab_N; 1.
DR PIRSF; PIRSF039088; F_ATPase_subunit_alpha; 1.
DR SUPFAM; SSF50615; SSF50615; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
DR TIGRFAMs; TIGR00962; atpA; 1.
DR PROSITE; PS00152; ATPASE_ALPHA_BETA; 1.
PE 1: Evidence at protein level;
KW ATP synthesis; ATP-binding; Cell membrane; CF(1);
KW Direct protein sequencing; Ion transport; Membrane; Nucleotide-binding;
KW Sodium; Sodium transport; Translocase; Transport.
FT CHAIN 1..500
FT /note="ATP synthase subunit alpha, sodium ion specific"
FT /id="PRO_0000144343"
FT BINDING 169..176
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01346"
FT SITE 362
FT /note="Required for activity"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01346"
FT CONFLICT 150
FT /note="I -> Y (in Ref. 2; CAA46898)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 500 AA; 54472 MW; 0DA1BF1C0D4D3CA4 CRC64;
MKIRPEEISG IIKTEIENYK KSLDVKTSGS VVQVGDGIAR IYGLSNAKAG ELLEFPNGIT
GMALNLEENN VGAVILGDPT GVKEGDEVRA TGQIAAVGAG EALLGRVVNS LGEPIDGKGE
LKTEKMMPLD RKAYGIISRK PVHEPLQTGI KSIDGMVPIG RGQRELIIGD RQTGKTAVAL
DAIINQKDTG VKCIYVAIGQ KRSTVAQIVK RLEDAGALEY TIVVAATASE SAPLQYMAPY
TGVSMGEYFM DKGEHVLIVY DDLSKHAVAY REMSLLLKRP PGREAFPGDV FYLHSRLLER
AAKLSDEIGA GSITALPIIE TQAGDVSAYI PTNVISITDG QIFLDSQLFN SGFRPAINAG
ISVSRVGGAA QIKAMKQVAA QVKLELAQYN ELLTFAQFGS DLDKATLAQL ERGHRIMEIL
KQEQYKPFVV EEQVVSFFTV INGYLDDIAI DQVRRFEKEL LEELKDNTTI LAEIVEKKAI
KEDLDAKLRK AIEDFKKKFS
