HPPA_CLOTE
ID HPPA_CLOTE Reviewed; 673 AA.
AC Q898Q9;
DT 25-JUL-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2003, sequence version 1.
DT 03-AUG-2022, entry version 115.
DE RecName: Full=Putative K(+)-stimulated pyrophosphate-energized sodium pump {ECO:0000255|HAMAP-Rule:MF_01129};
DE EC=7.2.3.- {ECO:0000255|HAMAP-Rule:MF_01129};
DE AltName: Full=Membrane-bound sodium-translocating pyrophosphatase {ECO:0000255|HAMAP-Rule:MF_01129};
DE AltName: Full=Pyrophosphate-energized inorganic pyrophosphatase {ECO:0000255|HAMAP-Rule:MF_01129};
DE Short=Na(+)-PPase {ECO:0000255|HAMAP-Rule:MF_01129};
GN Name=hppA {ECO:0000255|HAMAP-Rule:MF_01129}; OrderedLocusNames=CTC_00383;
OS Clostridium tetani (strain Massachusetts / E88).
OC Bacteria; Firmicutes; Clostridia; Eubacteriales; Clostridiaceae;
OC Clostridium.
OX NCBI_TaxID=212717;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Massachusetts / E88;
RX PubMed=12552129; DOI=10.1073/pnas.0335853100;
RA Brueggemann H., Baeumer S., Fricke W.F., Wiezer A., Liesegang H.,
RA Decker I., Herzberg C., Martinez-Arias R., Merkl R., Henne A.,
RA Gottschalk G.;
RT "The genome sequence of Clostridium tetani, the causative agent of tetanus
RT disease.";
RL Proc. Natl. Acad. Sci. U.S.A. 100:1316-1321(2003).
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}.
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 -!- 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}.
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}.
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DR EMBL; AE015927; AAO35020.1; -; Genomic_DNA.
DR RefSeq; WP_011098691.1; NC_004557.1.
DR AlphaFoldDB; Q898Q9; -.
DR SMR; Q898Q9; -.
DR STRING; 212717.CTC_00383; -.
DR TCDB; 3.A.10.1.7; the h(+), na(+)-translocating pyrophosphatase (m(+)-ppase) family.
DR EnsemblBacteria; AAO35020; AAO35020; CTC_00383.
DR GeneID; 64180594; -.
DR KEGG; ctc:CTC_00383; -.
DR HOGENOM; CLU_008743_3_1_9; -.
DR OMA; MATTAMQ; -.
DR OrthoDB; 98036at2; -.
DR Proteomes; UP000001412; Chromosome.
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 3: Inferred from homology;
KW Calcium; Cell membrane; Ion transport; Magnesium; Membrane; Metal-binding;
KW Potassium; Reference proteome; Sodium; Sodium transport; Translocase;
KW Transmembrane; Transmembrane helix; Transport.
FT CHAIN 1..673
FT /note="Putative K(+)-stimulated pyrophosphate-energized
FT sodium pump"
FT /id="PRO_0000217002"
FT TRANSMEM 3..23
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01129"
FT TRANSMEM 62..82
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01129"
FT TRANSMEM 84..104
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01129"
FT TRANSMEM 127..147
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01129"
FT TRANSMEM 154..174
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01129"
FT TRANSMEM 222..242
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01129"
FT TRANSMEM 247..267
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01129"
FT TRANSMEM 279..299
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01129"
FT TRANSMEM 302..322
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01129"
FT TRANSMEM 364..384
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01129"
FT TRANSMEM 387..407
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01129"
FT TRANSMEM 449..469
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01129"
FT TRANSMEM 486..506
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01129"
FT TRANSMEM 553..573
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01129"
FT TRANSMEM 576..596
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01129"
FT TRANSMEM 652..672
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01129"
FT BINDING 177
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 180
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 184
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 207
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 210
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 419
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 603
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250"
FT BINDING 629
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250"
FT BINDING 633
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250"
FT BINDING 636
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT SITE 169
FT /note="Important for ion transport"
FT /evidence="ECO:0000250"
FT SITE 214
FT /note="Important for ion transport"
FT /evidence="ECO:0000250"
FT SITE 221
FT /note="Important for ion transport"
FT /evidence="ECO:0000250"
FT SITE 449
FT /note="Determinant of potassium dependence"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01129"
FT SITE 637
FT /note="Important for ion transport"
FT /evidence="ECO:0000250"
FT SITE 648
FT /note="Important for ion transport"
FT /evidence="ECO:0000250"
SQ SEQUENCE 673 AA; 69282 MW; E3505682EE10FF56 CRC64;
MESFIVYSVL AGVIALIFAF MLSSFISKES AGNERMQEIA GHIHDGAMAF LKTEYKYLTG
FIVIVTVILA IFVGWQTAAC FILGAIFSIF AGYFGMNVAT KANVRTAEAA RHSQGKALNI
AFSGGAVMGM SVVGLGVVGI GIMYYIFGGN MEFVTGFGLG ASSIALFARV GGGIYTKAAD
VGADLVGKVE AGIPEDDPRN PAVIADNVGD NVGDVAGMGA DLFESYVGSI ISALTLGTVV
YANKEGVMFP LILSSIGIVA SIIGILFSRK SKAKDPQKAL NTGTYIGGII VIVSAAILSN
TIFGNLKAFF AVASGLVVGM IIGKITEMYT SDAYSSVQKI ANQSETGPAT TIISGLAVGM
YSTLWPIVLI SIGVLVSFFV MGGGSNAMVG LYGISLAAVG MLSTTGLTVA VDAYGPIADN
AGGIAEMSEL PHEVREITDK LDSVGNTTAA IGKGFAIGSA ALTALSLFAS YAQATELESI
DILNTVTLVG LFIGAMLPFL FGALTMESVG KAANEMIEEV RRQFKTIPGI MEGKATPDYK
KCVDISTAAA IREMILPGVL AIVVPVAMGL LLGKEALGGL LAGALVSGVL VGILMSNAGG
AWDNAKKYIE GGAHGGKGSE AHKAAVVGDT VGDPFKDTSG PSMNILIKLM TIVSLVFAPV
VLQYGGILLN LIK
