HPPA_RHOPL
ID HPPA_RHOPL Reviewed; 725 AA.
AC Q8KY01;
DT 25-JUL-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2002, sequence version 1.
DT 03-AUG-2022, entry version 73.
DE RecName: Full=K(+)-insensitive pyrophosphate-energized proton pump {ECO:0000255|HAMAP-Rule:MF_01129};
DE EC=7.1.3.1 {ECO:0000255|HAMAP-Rule:MF_01129};
DE AltName: Full=Membrane-bound proton-translocating pyrophosphatase {ECO:0000255|HAMAP-Rule:MF_01129};
DE AltName: Full=Pyrophosphate-energized inorganic pyrophosphatase {ECO:0000255|HAMAP-Rule:MF_01129};
DE Short=H(+)-PPase {ECO:0000255|HAMAP-Rule:MF_01129};
GN Name=hppA {ECO:0000255|HAMAP-Rule:MF_01129};
OS Rhodopseudomonas palustris.
OC Bacteria; Proteobacteria; Alphaproteobacteria; Hyphomicrobiales;
OC Bradyrhizobiaceae; Rhodopseudomonas.
OX NCBI_TaxID=1076;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA Garcia-Contreras R., Celis H., Romero I.;
RT "H+-PPase from Rhodopseudomonas palustris: cloning, sequencing and
RT characterization.";
RL Submitted (NOV-2000) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Proton pump that utilizes the energy of pyrophosphate
CC hydrolysis as the driving force for proton movement across the
CC membrane. Generates a proton motive force. {ECO:0000255|HAMAP-
CC Rule:MF_01129}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=diphosphate + H(+)(in) + H2O = 2 H(+)(out) + 2 phosphate;
CC Xref=Rhea:RHEA:13973, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:33019, ChEBI:CHEBI:43474; EC=7.1.3.1;
CC 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 -!- 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(+)-insensitive 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; AF325217; AAM76681.1; -; Genomic_DNA.
DR AlphaFoldDB; Q8KY01; -.
DR SMR; Q8KY01; -.
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:0009678; F:pyrophosphate hydrolysis-driven proton transmembrane transporter activity; 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; Hydrogen ion transport; Ion transport; Magnesium;
KW Membrane; Metal-binding; Translocase; Transmembrane; Transmembrane helix;
KW Transport.
FT CHAIN 1..725
FT /note="K(+)-insensitive pyrophosphate-energized proton
FT pump"
FT /id="PRO_0000217029"
FT TRANSMEM 3..23
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01129"
FT TRANSMEM 60..80
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 129..149
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01129"
FT TRANSMEM 164..184
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01129"
FT TRANSMEM 236..256
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01129"
FT TRANSMEM 259..279
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01129"
FT TRANSMEM 290..310
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01129"
FT TRANSMEM 328..348
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01129"
FT TRANSMEM 388..408
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01129"
FT TRANSMEM 467..487
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01129"
FT TRANSMEM 503..523
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01129"
FT TRANSMEM 578..598
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01129"
FT TRANSMEM 599..619
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01129"
FT TRANSMEM 667..687
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01129"
FT BINDING 186
FT /ligand="substrate"
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 193
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 216
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 219
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 431
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 619
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250"
FT BINDING 651
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250"
FT BINDING 655
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250"
FT BINDING 658
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT SITE 178
FT /note="Important for ion transport"
FT /evidence="ECO:0000250"
FT SITE 223
FT /note="Important for ion transport"
FT /evidence="ECO:0000250"
FT SITE 230
FT /note="Important for ion transport"
FT /evidence="ECO:0000250"
FT SITE 461
FT /note="Determinant of potassium independence"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01129"
FT SITE 659
FT /note="Important for ion transport"
FT /evidence="ECO:0000250"
FT SITE 670
FT /note="Important for ion transport"
FT /evidence="ECO:0000250"
SQ SEQUENCE 725 AA; 73750 MW; 64C1C3D1C86AF4A4 CRC64;
MTTSLALYLA LGCGLAAVLY GFIQRGWILA QDAGNARMQE IAGAIQQGAA AYLARQYKTI
AIVGAVLAIL IFFFLGGLTA AGFVLGAVLS GACGFIGMNV SVRANVRTAQ AATKGIGPAL
DVAFKGGAIT GMLVVGLGLL GVSLFFWFLS GGIHADPATL KPLLGLAFGS SLISIFARLG
GGIFTKGADV GADLVGKVEA SIPEDDPRNP AVIADNVGDN VGDCAGMAAD LFETYAVTLI
AAMALGALLL PNAALAAAVY PLVLGGVSII ASIIGCAFVK ASPGMKNVMP ALYKGLIVAG
AISLVFFFFV TRMVMPDDAL GAGTQMRLFG ACVVGLVLTA AMVWVTEYYT GTQFKPVQHV
AQASTTGHGT NIIAGLGVSM KSTAWPVIFV CLAIYGAYAL AGLYGIAIAA TSMLSMAGIV
VARDAYGPIT DNAGGIAEMS GLPDSVRDIT DPLDAVGNTT KAVTKGYAIG SAGLAALVLF
ADYTHALEAR GMSLSFDLSD HRVIVGLFIG GLIPYLFASM AMEAVGRAAG SVVVEVRRQF
RDIKGIMEGT AKPEYGTAVD MLTTAAIKEM IVPSLLPVVA PILVGMLLGP AALGGLLMGT
IVTGIFVGIS MCTGGGAWDN AKKLIEEGFT DANGVLHKKG SEAHKAAVTG DTVGDPYKDT
AGPAVNPLIK IINIVALLIV PLLPLASNPV KASHAEPAPM VQPAETAPAM PAAPMAEPSA
PAASQ
