HPPA_RHIME
ID HPPA_RHIME Reviewed; 711 AA.
AC Q8VRZ3; Q92QT7;
DT 25-JUL-2003, integrated into UniProtKB/Swiss-Prot.
DT 25-JUL-2003, sequence version 2.
DT 03-AUG-2022, entry version 112.
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}; OrderedLocusNames=R01218;
GN ORFNames=SMc01780;
OS Rhizobium meliloti (strain 1021) (Ensifer meliloti) (Sinorhizobium
OS meliloti).
OC Bacteria; Proteobacteria; Alphaproteobacteria; Hyphomicrobiales;
OC Rhizobiaceae; Sinorhizobium/Ensifer group; Sinorhizobium.
OX NCBI_TaxID=266834;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=1021;
RX PubMed=11481430; DOI=10.1073/pnas.161294398;
RA Capela D., Barloy-Hubler F., Gouzy J., Bothe G., Ampe F., Batut J.,
RA Boistard P., Becker A., Boutry M., Cadieu E., Dreano S., Gloux S.,
RA Godrie T., Goffeau A., Kahn D., Kiss E., Lelaure V., Masuy D., Pohl T.,
RA Portetelle D., Puehler A., Purnelle B., Ramsperger U., Renard C.,
RA Thebault P., Vandenbol M., Weidner S., Galibert F.;
RT "Analysis of the chromosome sequence of the legume symbiont Sinorhizobium
RT meliloti strain 1021.";
RL Proc. Natl. Acad. Sci. U.S.A. 98:9877-9882(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=1021;
RX PubMed=11474104; DOI=10.1126/science.1060966;
RA Galibert F., Finan T.M., Long S.R., Puehler A., Abola P., Ampe F.,
RA Barloy-Hubler F., Barnett M.J., Becker A., Boistard P., Bothe G.,
RA Boutry M., Bowser L., Buhrmester J., Cadieu E., Capela D., Chain P.,
RA Cowie A., Davis R.W., Dreano S., Federspiel N.A., Fisher R.F., Gloux S.,
RA Godrie T., Goffeau A., Golding B., Gouzy J., Gurjal M., Hernandez-Lucas I.,
RA Hong A., Huizar L., Hyman R.W., Jones T., Kahn D., Kahn M.L., Kalman S.,
RA Keating D.H., Kiss E., Komp C., Lelaure V., Masuy D., Palm C., Peck M.C.,
RA Pohl T.M., Portetelle D., Purnelle B., Ramsperger U., Surzycki R.,
RA Thebault P., Vandenbol M., Vorhoelter F.J., Weidner S., Wells D.H.,
RA Wong K., Yeh K.-C., Batut J.;
RT "The composite genome of the legume symbiont Sinorhizobium meliloti.";
RL Science 293:668-672(2001).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 35-698.
RC STRAIN=RCR2011 / SU47;
RA Jumas-Bilak E., Michaux-Charachon S., Teyssier C.;
RT "High prevalence of the H+ proton-pumping inorganic pyrophosphatase gene in
RT alpha proteobacteria and evidence of lateral transfer in its phylogeny.";
RL Submitted (SEP-2001) 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 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(+)-insensitive subfamily. {ECO:0000255|HAMAP-
CC Rule:MF_01129}.
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DR EMBL; AL591688; CAC45797.1; -; Genomic_DNA.
DR EMBL; AF417513; AAL69329.1; -; Genomic_DNA.
DR RefSeq; NP_385324.1; NC_003047.1.
DR RefSeq; WP_010969115.1; NC_003047.1.
DR AlphaFoldDB; Q8VRZ3; -.
DR SMR; Q8VRZ3; -.
DR STRING; 266834.SMc01780; -.
DR EnsemblBacteria; CAC45797; CAC45797; SMc01780.
DR GeneID; 61602676; -.
DR KEGG; sme:SMc01780; -.
DR PATRIC; fig|266834.11.peg.2630; -.
DR eggNOG; COG3808; Bacteria.
DR HOGENOM; CLU_008743_3_1_5; -.
DR OMA; MATTAMQ; -.
DR Proteomes; UP000001976; 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: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 inner membrane; Cell membrane; Hydrogen ion transport;
KW Ion transport; Magnesium; Membrane; Metal-binding; Reference proteome;
KW Translocase; Transmembrane; Transmembrane helix; Transport.
FT CHAIN 1..711
FT /note="K(+)-insensitive pyrophosphate-energized proton
FT pump"
FT /id="PRO_0000217027"
FT TRANSMEM 1..21
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01129"
FT TRANSMEM 48..70
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 126..146
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 239..259
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01129"
FT TRANSMEM 261..281
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01129"
FT TRANSMEM 296..316
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01129"
FT TRANSMEM 331..351
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01129"
FT TRANSMEM 382..402
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01129"
FT TRANSMEM 409..429
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01129"
FT TRANSMEM 468..488
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01129"
FT TRANSMEM 520..540
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01129"
FT TRANSMEM 589..609
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 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 437
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 678
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250"
FT BINDING 682
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250"
FT BINDING 685
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 467
FT /note="Determinant of potassium independence"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01129"
FT SITE 686
FT /note="Important for ion transport"
FT /evidence="ECO:0000250"
FT SITE 697
FT /note="Important for ion transport"
FT /evidence="ECO:0000250"
FT CONFLICT 38
FT /note="I -> V (in Ref. 3; AAL69329)"
FT /evidence="ECO:0000305"
FT CONFLICT 116..117
FT /note="GL -> DI (in Ref. 3; AAL69329)"
FT /evidence="ECO:0000305"
FT CONFLICT 144..158
FT /note="LILTAGLGHEPAARE -> FVLIVWLGYAPADRA (in Ref. 3;
FT AAL69329)"
FT /evidence="ECO:0000305"
FT CONFLICT 162
FT /note="A -> S (in Ref. 3; AAL69329)"
FT /evidence="ECO:0000305"
FT CONFLICT 174
FT /note="S -> A (in Ref. 3; AAL69329)"
FT /evidence="ECO:0000305"
FT CONFLICT 177
FT /note="A -> V (in Ref. 3; AAL69329)"
FT /evidence="ECO:0000305"
FT CONFLICT 201..203
FT /note="GIP -> CIR (in Ref. 3; AAL69329)"
FT /evidence="ECO:0000305"
FT CONFLICT 208..209
FT /note="RN -> CI (in Ref. 3; AAL69329)"
FT /evidence="ECO:0000305"
FT CONFLICT 215
FT /note="D -> N (in Ref. 3; AAL69329)"
FT /evidence="ECO:0000305"
FT CONFLICT 219
FT /note="D -> H (in Ref. 3; AAL69329)"
FT /evidence="ECO:0000305"
FT CONFLICT 222..223
FT /note="GD -> CG (in Ref. 3; AAL69329)"
FT /evidence="ECO:0000305"
FT CONFLICT 226
FT /note="G -> A (in Ref. 3; AAL69329)"
FT /evidence="ECO:0000305"
FT CONFLICT 238
FT /note="S -> T (in Ref. 3; AAL69329)"
FT /evidence="ECO:0000305"
FT CONFLICT 456
FT /note="T -> N (in Ref. 3; AAL69329)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 711 AA; 72257 MW; 55AAD7CF3242A681 CRC64;
MTILLGVIAC GLLSVVYAIW ATKSVLAADQ GNARMQEIAG FIREGAQAYL TRQYTTIAIV
GVVVFIAAWL LLSGAAAIGF LIGAVLSGAA GFIGMHVSVR ANVRTAQAAS VSLASGLDIA
FKSGAITGML VAGLALLGVS VYYLILTAGL GHEPAAREVI DALVALGFGA SLISIFARLG
GGIFTKGADV GGDLVGKVEA GIPEDDPRNP ATIADNVGDN VGDCAGMAAD LFETYAVSVV
ATMVLASIFF AGAPVLATVM TYPLAICAAC IITSIIGTFF VKLGANASIM GALYRGLIVT
GALSILGLGA ATSLTIGWGS IGTVAGMDIT GWNLFLCGII GLIVTALIVV ITEYYTGTNK
RPVNSIAQAS VTGHGTNVIQ GLAVSLESTA LPAIVIVGGI IATYQFAGLF GTAIAVTAML
GLAGMIVALD AFGPVTDNAG GIAEMSHLPP EVRKSTDALD AVGNTTKAVT KGYAIGSAGL
GALVLFAAYS NDLAYFAANG DKHPYFADVG TISFDLSNPY VVAGLIFGGL IPYLFGGIAM
TAVGRAGSAV VEEVRRQFKE KPGIMEGKDR PDYGRAVDML TKAAIREMII PSLLPVLAPI
VVYFGVLLIS GSKASAFAAL GASLLGVIVN GLFVAISMTS GGGAWDNAKK SFEDGFVDRN
GTRHMKGSEA HKASVTGDTV GDPYKDTAGP AVNPAIKITN IVALLLLAVL A
