HPPA1_MOOTA
ID HPPA1_MOOTA Reviewed; 672 AA.
AC Q2RIS7;
DT 30-NOV-2010, integrated into UniProtKB/Swiss-Prot.
DT 24-JAN-2006, sequence version 1.
DT 03-AUG-2022, entry version 86.
DE RecName: Full=Putative K(+)-stimulated pyrophosphate-energized sodium pump 1 {ECO:0000255|HAMAP-Rule:MF_01129};
DE EC=7.2.3.- {ECO:0000255|HAMAP-Rule:MF_01129, ECO:0000269|PubMed:17605473};
DE AltName: Full=Membrane-bound sodium-translocating pyrophosphatase 1 {ECO:0000255|HAMAP-Rule:MF_01129};
DE AltName: Full=Pyrophosphate-energized inorganic pyrophosphatase 1 {ECO:0000255|HAMAP-Rule:MF_01129};
DE Short=Na(+)-PPase 1 {ECO:0000255|HAMAP-Rule:MF_01129};
GN Name=hppA1 {ECO:0000255|HAMAP-Rule:MF_01129}; OrderedLocusNames=Moth_1349;
OS Moorella thermoacetica (strain ATCC 39073 / JCM 9320).
OC Bacteria; Firmicutes; Clostridia; Thermoanaerobacterales;
OC Thermoanaerobacteraceae; Moorella group; Moorella.
OX NCBI_TaxID=264732;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 39073 / JCM 9320;
RX PubMed=18631365; DOI=10.1111/j.1462-2920.2008.01679.x;
RA Pierce E., Xie G., Barabote R.D., Saunders E., Han C.S., Detter J.C.,
RA Richardson P., Brettin T.S., Das A., Ljungdahl L.G., Ragsdale S.W.;
RT "The complete genome sequence of Moorella thermoacetica (f. Clostridium
RT thermoaceticum).";
RL Environ. Microbiol. 10:2550-2573(2008).
RN [2]
RP FUNCTION, CATALYTIC ACTIVITY, AND ACTIVITY REGULATION.
RX PubMed=17605473; DOI=10.1021/bi700564b;
RA Malinen A.M., Belogurov G.A., Baykov A.A., Lahti R.;
RT "Na+-pyrophosphatase: a novel primary sodium pump.";
RL Biochemistry 46:8872-8878(2007).
CC -!- FUNCTION: Sodium pump that utilizes the energy of pyrophosphate
CC hydrolysis as the driving force for Na(+) movement across the membrane.
CC {ECO:0000255|HAMAP-Rule:MF_01129, ECO:0000269|PubMed:17605473}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=diphosphate + H2O + Na(+)(in) = H(+) + Na(+)(out) + 2
CC phosphate; Xref=Rhea:RHEA:57884, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:29101, ChEBI:CHEBI:33019,
CC ChEBI:CHEBI:43474; Evidence={ECO:0000255|HAMAP-Rule:MF_01129,
CC ECO:0000269|PubMed:17605473};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_01129};
CC -!- ACTIVITY REGULATION: Requires K(+) for maximal activity.
CC {ECO:0000255|HAMAP-Rule:MF_01129, ECO:0000269|PubMed:17605473}.
CC -!- SUBUNIT: Homodimer. {ECO:0000255|HAMAP-Rule:MF_01129}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000255|HAMAP-Rule:MF_01129};
CC Multi-pass membrane protein {ECO:0000255|HAMAP-Rule:MF_01129}.
CC -!- SIMILARITY: Belongs to the H(+)-translocating pyrophosphatase (TC
CC 3.A.10) family. K(+)-stimulated subfamily. {ECO:0000255|HAMAP-
CC Rule:MF_01129}.
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; CP000232; ABC19662.1; -; Genomic_DNA.
DR RefSeq; WP_011392862.1; NC_007644.1.
DR RefSeq; YP_430205.1; NC_007644.1.
DR AlphaFoldDB; Q2RIS7; -.
DR SMR; Q2RIS7; -.
DR STRING; 264732.Moth_1349; -.
DR TCDB; 3.A.10.1.3; the h(+), na(+)-translocating pyrophosphatase (m(+)-ppase) family.
DR PRIDE; Q2RIS7; -.
DR EnsemblBacteria; ABC19662; ABC19662; Moth_1349.
DR KEGG; mta:Moth_1349; -.
DR PATRIC; fig|264732.11.peg.1448; -.
DR eggNOG; COG3808; Bacteria.
DR HOGENOM; CLU_008743_3_1_9; -.
DR OMA; MATTAMQ; -.
DR BRENDA; 7.1.3.2; 1528.
DR GO; GO:0005887; C:integral component of plasma membrane; IEA:UniProtKB-UniRule.
DR GO; GO:0004427; F:inorganic diphosphatase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-UniRule.
DR GO; GO:0030955; F:potassium ion binding; IEA:UniProtKB-UniRule.
DR GO; GO:0009678; F:pyrophosphate hydrolysis-driven proton transmembrane transporter activity; IEA:UniProtKB-UniRule.
DR GO; GO:0006814; P:sodium ion transport; IEA:UniProtKB-UniRule.
DR HAMAP; MF_01129; PPase_energized_pump; 1.
DR InterPro; IPR004131; PPase-energised_H-pump.
DR PANTHER; PTHR31998; PTHR31998; 1.
DR Pfam; PF03030; H_PPase; 1.
DR PIRSF; PIRSF001265; H+-PPase; 1.
DR TIGRFAMs; TIGR01104; V_PPase; 1.
PE 1: Evidence at protein level;
KW Calcium; Cell membrane; Ion transport; Magnesium; Membrane; Metal-binding;
KW Potassium; Sodium; Sodium transport; Translocase; Transmembrane;
KW Transmembrane helix; Transport.
FT CHAIN 1..672
FT /note="Putative K(+)-stimulated pyrophosphate-energized
FT sodium pump 1"
FT /id="PRO_0000401182"
FT TRANSMEM 1..21
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01129"
FT TRANSMEM 55..75
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01129"
FT TRANSMEM 82..102
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01129"
FT TRANSMEM 133..153
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01129"
FT TRANSMEM 158..178
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01129"
FT TRANSMEM 227..247
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01129"
FT TRANSMEM 252..272
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01129"
FT TRANSMEM 283..303
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01129"
FT TRANSMEM 317..337
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01129"
FT TRANSMEM 370..390
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01129"
FT TRANSMEM 397..417
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01129"
FT TRANSMEM 461..481
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01129"
FT TRANSMEM 492..512
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01129"
FT TRANSMEM 560..580
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01129"
FT TRANSMEM 584..604
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01129"
FT TRANSMEM 650..670
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01129"
FT BINDING 182
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 185
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 189
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 212
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 215
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 425
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 611
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250"
FT BINDING 637
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250"
FT BINDING 641
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250"
FT BINDING 644
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT SITE 174
FT /note="Important for ion transport"
FT /evidence="ECO:0000250"
FT SITE 219
FT /note="Important for ion transport"
FT /evidence="ECO:0000250"
FT SITE 226
FT /note="Important for ion transport"
FT /evidence="ECO:0000250"
FT SITE 455
FT /note="Determinant of potassium dependence"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01129"
FT SITE 645
FT /note="Important for ion transport"
FT /evidence="ECO:0000250"
FT SITE 656
FT /note="Important for ion transport"
FT /evidence="ECO:0000250"
SQ SEQUENCE 672 AA; 68449 MW; 23BA53EA9C76900B CRC64;
MELLAPLTGI VALLFAFYLT NKINRSDPGN PRMQEIAVAI HEGAMAFLMR EYRTLIFFVL
GMTALIVVAG FMTRGAESMQ PATAIAYVAG TLCSIGAGYI GMQVATRANV RTANAARHSS
NAALDIAFSG GSVMGMAVVG LGLLGLGIIN YVFKNPSIVN GFALGASSIA LFARVGGGIY
TKAADVGADL VGKVEAGIPE DDPRNPAVIA DNVGDNVGDV AGMGADLFES YVGSIISGIA
LAAALNIPNG TLVPLMIAAI GIVSSILGAF FVKTGEGANA QKALNTGTMV ASILAIVGTF
LATRLLPAHF TAGSMSYTST GVFAATIAGL IAGVLIGRIT EYYTSGDYEP VKEIAKASQT
GTATNIIEGL STGMLSTVLP ILVIVIAIIA SYRFAGLYGI AMAAVGMLST TGTTVAVDAY
GPIADNAGGI AEMAELDPKV RKITDALDSV GNTTAAIGKG FAIGSAALTA LALFSAYTAA
ARITAIDLTD PKVVGGLFIG GMLPFLFAAL TMKAVGRAAF QMIEEVRRQF KSIPGLMEGK
ARPDYARCVA ISTGAAIKEM IVPGLLAVLV PLAVGLIPGL GKEALGGLLA GATVTGFLMA
VMMANAGGAW DNAKKYIEGG QYGGKGSPAH AAAVNGDTVG DPFKDTSGPA MNILIKLMTI
VSLVFAPLFM QL
