HPPA_BACTN
ID HPPA_BACTN Reviewed; 734 AA.
AC Q8A294;
DT 25-JUL-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2003, sequence version 1.
DT 03-AUG-2022, entry version 117.
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=BT_3411;
OS Bacteroides thetaiotaomicron (strain ATCC 29148 / DSM 2079 / JCM 5827 /
OS CCUG 10774 / NCTC 10582 / VPI-5482 / E50).
OC Bacteria; Bacteroidetes; Bacteroidia; Bacteroidales; Bacteroidaceae;
OC Bacteroides.
OX NCBI_TaxID=226186;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 29148 / DSM 2079 / JCM 5827 / CCUG 10774 / NCTC 10582 /
RC VPI-5482 / E50;
RX PubMed=12663928; DOI=10.1126/science.1080029;
RA Xu J., Bjursell M.K., Himrod J., Deng S., Carmichael L.K., Chiang H.C.,
RA Hooper L.V., Gordon J.I.;
RT "A genomic view of the human-Bacteroides thetaiotaomicron symbiosis.";
RL Science 299:2074-2076(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}.
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DR EMBL; AE015928; AAO78517.1; -; Genomic_DNA.
DR RefSeq; NP_812323.1; NC_004663.1.
DR RefSeq; WP_008767612.1; NC_004663.1.
DR AlphaFoldDB; Q8A294; -.
DR SMR; Q8A294; -.
DR PaxDb; Q8A294; -.
DR PRIDE; Q8A294; -.
DR EnsemblBacteria; AAO78517; AAO78517; BT_3411.
DR GeneID; 60924591; -.
DR KEGG; bth:BT_3411; -.
DR PATRIC; fig|226186.12.peg.3480; -.
DR eggNOG; COG3808; Bacteria.
DR HOGENOM; CLU_008743_3_1_10; -.
DR InParanoid; Q8A294; -.
DR OMA; MATTAMQ; -.
DR Proteomes; UP000001414; 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 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..734
FT /note="Putative K(+)-stimulated pyrophosphate-energized
FT sodium pump"
FT /id="PRO_0000217001"
FT TRANSMEM 3..23
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01129"
FT TRANSMEM 58..78
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 134..154
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01129"
FT TRANSMEM 169..189
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01129"
FT TRANSMEM 244..264
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01129"
FT TRANSMEM 275..295
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01129"
FT TRANSMEM 314..334
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01129"
FT TRANSMEM 336..356
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01129"
FT TRANSMEM 377..397
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01129"
FT TRANSMEM 398..418
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01129"
FT TRANSMEM 423..443
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01129"
FT TRANSMEM 491..511
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01129"
FT TRANSMEM 557..577
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01129"
FT TRANSMEM 629..649
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 TRANSMEM 712..732
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01129"
FT BINDING 199
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 202
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
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 229
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 232
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 455
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 670
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250"
FT BINDING 696
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250"
FT BINDING 700
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250"
FT BINDING 703
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT SITE 191
FT /note="Important for ion transport"
FT /evidence="ECO:0000250"
FT SITE 236
FT /note="Important for ion transport"
FT /evidence="ECO:0000250"
FT SITE 243
FT /note="Important for ion transport"
FT /evidence="ECO:0000250"
FT SITE 485
FT /note="Determinant of potassium dependence"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01129"
FT SITE 704
FT /note="Important for ion transport"
FT /evidence="ECO:0000250"
FT SITE 715
FT /note="Important for ion transport"
FT /evidence="ECO:0000250"
SQ SEQUENCE 734 AA; 76538 MW; 59DA2F60FEC56F46 CRC64;
MDSILFWLVP VASVLALCFA YYFHKQMMKE SEGTPQMIKI AAAVRKGAMS YLKQQYKIVG
CVFLGLVILF SIMAYGFHVQ NVWVPIAFLT GGFFSGLSGF LGMKTATYAS ARTANAARNS
LNSGLRIAFR SGAVMGLVVV GLGLLDISFW YLLLNAVIPA DALTPTHKLC VITTTMLTFG
MGASTQALFA RVGGGIYTKA ADVGADLVGK VEAGIPEDDP RNPATIADNV GDNVGDVAGM
GADLYESYCG SILATAALGA AAFIHSADTV MQFKAVIAPM LIAAVGILLS IIGIFSVRTK
ENATVKDLLG SLAFGTNLSS VLIVAATFLI LWLLQLDNWI WISCAVVVGL LVGIVIGRST
EYYTSQSYRP TQKLSESGKT GPATVIISGI GLGMLSTAIP VIAVVVGIIA SFLLASGFDF
SNVGMGLYGI GIAAVGMLST LGITLATDAY GPIADNAGGN AEMAGLGAEV RKRTDALDSL
GNTTAATGKG FAIGSAALTG LALLASYIEE IRIGLTRLGT VDLSMPNGDV VSTANATFVD
FMNYYDVTLM NPKVLSGMFL GSMMAFLFCG LTMNAVGRAA GHMVDEVRRQ FREIKGILTG
EAEPDYERCV AISTKGAQRE MVIPSLIAIL APIATGLIFG VTGVLGLLIG GLSTGFVLAI
FMANAGGAWD NAKKYVEEGN FGGKGGEVHK ATVVGDTVGD PFKDTSGPSL NILIKLMSMV
AIVMAGLTVA WSLF
