ID   HPPA_RHOPA              Reviewed;         706 AA.
AC   P60363;
DT   16-FEB-2004, integrated into UniProtKB/Swiss-Prot.
DT   16-FEB-2004, sequence version 1.
DT   18-JUN-2025, entry version 117.
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};
GN   OrderedLocusNames=RPA2731;
OS   Rhodopseudomonas palustris (strain ATCC BAA-98 / CGA009).
OC   Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
OC   Hyphomicrobiales; Nitrobacteraceae; Rhodopseudomonas.
OX   NCBI_TaxID=258594;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-98 / CGA009;
RX   PubMed=14704707; DOI=10.1038/nbt923;
RA   Larimer F.W., Chain P., Hauser L., Lamerdin J.E., Malfatti S., Do L.,
RA   Land M.L., Pelletier D.A., Beatty J.T., Lang A.S., Tabita F.R.,
RA   Gibson J.L., Hanson T.E., Bobst C., Torres y Torres J.L., Peres C.,
RA   Harrison F.H., Gibson J., Harwood C.S.;
RT   "Complete genome sequence of the metabolically versatile photosynthetic
RT   bacterium Rhodopseudomonas palustris.";
RL   Nat. Biotechnol. 22:55-61(2004).
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 + H2O + H(+)(in) = 2 phosphate + 2 H(+)(out);
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; Evidence={ECO:0000255|HAMAP-
CC         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
CC       (TC 3.A.10) family. K(+)-insensitive subfamily. {ECO:0000255|HAMAP-
CC       Rule:MF_01129}.
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DR   EMBL; BX572601; CAE28173.1; -; Genomic_DNA.
DR   RefSeq; WP_011158282.1; NZ_CP116810.1.
DR   AlphaFoldDB; P60363; -.
DR   SMR; P60363; -.
DR   STRING; 258594.RPA2731; -.
DR   GeneID; 66893807; -.
DR   eggNOG; COG3808; Bacteria.
DR   HOGENOM; CLU_008743_3_1_5; -.
DR   PhylomeDB; P60363; -.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0009678; F:diphosphate hydrolysis-driven proton transmembrane transporter activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0004427; F:inorganic diphosphate phosphatase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-UniRule.
DR   HAMAP; MF_01129; PPase_energized_pump; 1.
DR   InterPro; IPR004131; PPase-energised_H-pump.
DR   NCBIfam; NF001951; PRK00733.1-2; 1.
DR   NCBIfam; NF001960; PRK00733.3-5; 1.
DR   NCBIfam; TIGR01104; V_PPase; 1.
DR   PANTHER; PTHR31998; K(+)-INSENSITIVE PYROPHOSPHATE-ENERGIZED PROTON PUMP; 1.
DR   Pfam; PF03030; H_PPase; 1.
DR   PIRSF; PIRSF001265; H+-PPase; 1.
PE   3: Inferred from homology;
KW   Calcium; Cell inner membrane; Cell membrane; Hydrogen ion transport;
KW   Ion transport; Magnesium; Membrane; Metal-binding; Translocase;
KW   Transmembrane; Transmembrane helix; Transport.
FT   CHAIN           1..706
FT                   /note="K(+)-insensitive pyrophosphate-energized proton
FT                   pump"
FT                   /id="PRO_0000217028"
FT   TRANSMEM        1..21
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        83..103
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        231..251
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01129"
FT   TRANSMEM        263..283
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01129"
FT   TRANSMEM        300..320
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01129"
FT   TRANSMEM        330..350
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01129"
FT   TRANSMEM        393..413
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01129"
FT   TRANSMEM        414..434
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        516..536
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01129"
FT   TRANSMEM        585..605
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01129"
FT   TRANSMEM        616..636
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01129"
FT   TRANSMEM        685..705
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         436
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250"
FT   BINDING         646
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /evidence="ECO:0000250"
FT   BINDING         672
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /evidence="ECO:0000250"
FT   BINDING         676
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /evidence="ECO:0000250"
FT   BINDING         679
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            466
FT                   /note="Determinant of potassium independence"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01129"
FT   SITE            680
FT                   /note="Important for ion transport"
FT                   /evidence="ECO:0000250"
FT   SITE            691
FT                   /note="Important for ion transport"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   706 AA;  71952 MW;  FB4332D4F65F668E CRC64;
     MTALWVIVLC GALSIVYAIW ATSSVLAADQ GNARMQEIAG AVREGAQAYL KRQYMTIAIV
     GVVIFALLAY FLGILVAIGF AIGAILSGAA GFIGMNVSVR ANVRTAQAAT TSLAGGLELA
     FKAGAITGLL VAGLALLGVT LYFIYLIHFA GLQANSRTVV DALVALGFGA SLISIFARLG
     GGIFTKGADV GGDLVGKVEA GIPEDDPRNP ATIADNVGDN VGDCAGMAAD LFETYAVTAV
     ATMVLAAIFF GSATPDQLQS VMTLPLAIGG ICILTSIAGT FFVKLGASQS IMGALYKGLI
     ATGVLSLVGV GVVIHQLIGF GPLPGVSYTG LALFECGIVG LAVTGLIIWI TEYYTGTDFR
     PVKSIAQASV TGHGTNVIQG LAISMESTAL PAIVIIAGIL ITYSLAGLFG IAIATTTMLA
     LAGMIVALDA FGPVTDNAGG IAEMAGLPKE VRKSTDALDA VGNTTKAVTK GYAIGSAGLG
     ALVLFAAYNE DLKFFIAQKS PYFVGVAPDF SLNNPYVVVG LLFGGLLPYL FGAMGMTAVG
     RAAGAIVEEV RRQFREKPGI MKGTDKPDYG KAVDLLTKAA IKEMIIPSLL PVLSPIFVYF
     AIYAIAGGGA AGKSAAFSAV GAMLLGVIVT GLFVAISMTS GGGAWDNAKK YIEDGHHGGK
     GSDAHKAAVT GDTVGDPYKD TAGPAVNPMI KITNIVALLL LAILAH
//