HPPA_LEPIN
ID HPPA_LEPIN Reviewed; 704 AA.
AC Q8F641;
DT 25-JUL-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2003, sequence version 1.
DT 03-AUG-2022, entry version 124.
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=LA_1471;
OS Leptospira interrogans serogroup Icterohaemorrhagiae serovar Lai (strain
OS 56601).
OC Bacteria; Spirochaetes; Leptospirales; Leptospiraceae; Leptospira.
OX NCBI_TaxID=189518;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=56601;
RX PubMed=12712204; DOI=10.1038/nature01597;
RA Ren S.-X., Fu G., Jiang X.-G., Zeng R., Miao Y.-G., Xu H., Zhang Y.-X.,
RA Xiong H., Lu G., Lu L.-F., Jiang H.-Q., Jia J., Tu Y.-F., Jiang J.-X.,
RA Gu W.-Y., Zhang Y.-Q., Cai Z., Sheng H.-H., Yin H.-F., Zhang Y., Zhu G.-F.,
RA Wan M., Huang H.-L., Qian Z., Wang S.-Y., Ma W., Yao Z.-J., Shen Y.,
RA Qiang B.-Q., Xia Q.-C., Guo X.-K., Danchin A., Saint Girons I.,
RA Somerville R.L., Wen Y.-M., Shi M.-H., Chen Z., Xu J.-G., Zhao G.-P.;
RT "Unique physiological and pathogenic features of Leptospira interrogans
RT revealed by whole-genome sequencing.";
RL Nature 422:888-893(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 inner membrane {ECO:0000255|HAMAP-
CC Rule:MF_01129}; Multi-pass membrane protein {ECO:0000255|HAMAP-
CC 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 -!- SEQUENCE CAUTION:
CC Sequence=AAN48670.2; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AE010300; AAN48670.2; ALT_INIT; Genomic_DNA.
DR RefSeq; NP_711652.2; NC_004342.2.
DR RefSeq; WP_001089694.1; NC_004342.2.
DR AlphaFoldDB; Q8F641; -.
DR SMR; Q8F641; -.
DR STRING; 189518.LA_1471; -.
DR EnsemblBacteria; AAN48670; AAN48670; LA_1471.
DR GeneID; 61142169; -.
DR KEGG; lil:LA_1471; -.
DR PATRIC; fig|189518.3.peg.1472; -.
DR HOGENOM; CLU_008743_3_1_12; -.
DR InParanoid; Q8F641; -.
DR OMA; MATTAMQ; -.
DR Proteomes; UP000001408; Chromosome I.
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 inner membrane; Cell membrane; Ion transport; Magnesium;
KW Membrane; Metal-binding; Potassium; Reference proteome; Sodium;
KW Sodium transport; Translocase; Transmembrane; Transmembrane helix;
KW Transport.
FT CHAIN 1..704
FT /note="Putative K(+)-stimulated pyrophosphate-energized
FT sodium pump"
FT /id="PRO_0000217018"
FT TRANSMEM 3..23
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01129"
FT TRANSMEM 64..84
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01129"
FT TRANSMEM 91..111
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01129"
FT TRANSMEM 144..164
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01129"
FT TRANSMEM 174..194
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01129"
FT TRANSMEM 276..296
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01129"
FT TRANSMEM 313..333
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01129"
FT TRANSMEM 346..366
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 429..449
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01129"
FT TRANSMEM 483..503
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01129"
FT TRANSMEM 514..534
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01129"
FT TRANSMEM 586..606
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01129"
FT TRANSMEM 608..628
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01129"
FT TRANSMEM 680..700
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01129"
FT BINDING 203
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 206
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 210
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 233
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 236
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 451
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 635
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250"
FT BINDING 660
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250"
FT BINDING 664
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250"
FT BINDING 667
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT SITE 195
FT /note="Important for ion transport"
FT /evidence="ECO:0000250"
FT SITE 240
FT /note="Important for ion transport"
FT /evidence="ECO:0000250"
FT SITE 247
FT /note="Important for ion transport"
FT /evidence="ECO:0000250"
FT SITE 481
FT /note="Important for potassium dependence"
FT /evidence="ECO:0000250"
FT SITE 668
FT /note="Important for ion transport"
FT /evidence="ECO:0000250"
FT SITE 679
FT /note="Important for ion transport"
FT /evidence="ECO:0000250"
SQ SEQUENCE 704 AA; 73106 MW; 9369E135382D96BC CRC64;
MNSVTIIIAM SILAIVTAVV YTLKVTSIKV GTLGGNEKET KKLLEISSAI SEGAMAFLVR
EYKVISLFIA FMAVLIVLLL DNPGSEGFND GIYTAIAFVS GALISCISGF IGMKIATAGN
VRTAEAAKSS MAKAFRVAFD SGAVMGFGLV GLAILGMIVL FLVFTGMYPG VEKHFLMESL
AGFGLGGSAV ALFGRVGGGI YTKAADVGAD LVGKVEKGIP EDDPRNPATI ADNVGDNVGD
VAGMGADLFG SCAEATCAAL VIGATASALS GSVDALLYPL LISAFGIPAS ILTSFLARVK
EDGNVESALK VQLWVSTLLV AGIMYFVTKT FMVDSFEIAG KTITKWDVYI SMVVGLFSGM
FIGIVTEYYT SHSYKPVREV AEASNTGAAT NIIYGLSLGY HSSVIPVILL VITIVTANLL
AGMYGIAIAA LGMISTIAIG LTIDAYGPVS DNAGGIAEMA ELGKEVRDRT DTLDAAGNTT
AAIGKGFAIG SAALTSLALF AAFITRTHTT SLEVLNAEVF GGLMFGAMLP FLFTAMTMKS
VGKAAVDMVE EVRKQFKEIP GIMEGKNKPD YKRCVDISTS AALREMILPG LLVLLTPILV
GYLFGVKTLA GVLAGALVAG VVLAISAANS GGGWDNAKKY IEKKAGGKGS DQHKAAVVGD
TVGDPFKDTS GPSINILIKL MAITSLVFAE FFVQQGGLIF KIFH
