HPPA_CARHZ
ID HPPA_CARHZ Reviewed; 686 AA.
AC Q3AFC6;
DT 02-NOV-2010, integrated into UniProtKB/Swiss-Prot.
DT 22-NOV-2005, sequence version 1.
DT 03-AUG-2022, entry version 77.
DE RecName: Full=K(+)-stimulated pyrophosphate-energized proton pump;
DE EC=7.1.3.1 {ECO:0000269|PubMed:12401795};
DE AltName: Full=Membrane-bound proton-translocating pyrophosphatase;
DE AltName: Full=Pyrophosphate-energized inorganic pyrophosphatase {ECO:0000255|HAMAP-Rule:MF_01129};
DE Short=H(+)-PPase;
GN Name=hppA {ECO:0000255|HAMAP-Rule:MF_01129}; OrderedLocusNames=CHY_0286;
OS Carboxydothermus hydrogenoformans (strain ATCC BAA-161 / DSM 6008 /
OS Z-2901).
OC Bacteria; Firmicutes; Clostridia; Thermoanaerobacterales;
OC Thermoanaerobacteraceae; Carboxydothermus.
OX NCBI_TaxID=246194;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-161 / DSM 6008 / Z-2901;
RX PubMed=16311624; DOI=10.1371/journal.pgen.0010065;
RA Wu M., Ren Q., Durkin A.S., Daugherty S.C., Brinkac L.M., Dodson R.J.,
RA Madupu R., Sullivan S.A., Kolonay J.F., Nelson W.C., Tallon L.J.,
RA Jones K.M., Ulrich L.E., Gonzalez J.M., Zhulin I.B., Robb F.T., Eisen J.A.;
RT "Life in hot carbon monoxide: the complete genome sequence of
RT Carboxydothermus hydrogenoformans Z-2901.";
RL PLoS Genet. 1:563-574(2005).
RN [2]
RP CATALYTIC ACTIVITY, ACTIVITY REGULATION, MUTAGENESIS OF ALA-460 AND
RP ALA-463, AND IDENTIFICATION OF SITE IMPORTANT FOR POTASSIUM DEPENDENCE.
RX PubMed=12401795; DOI=10.1074/jbc.m210341200;
RA Belogurov G.A., Lahti R.;
RT "A lysine substitute for K+. A460K mutation eliminates K+ dependence in H+-
RT pyrophosphatase of Carboxydothermus hydrogenoformans.";
RL J. Biol. Chem. 277:49651-49654(2002).
CC -!- FUNCTION: Proton 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 + 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:0000269|PubMed:12401795};
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, ECO:0000269|PubMed:12401795}.
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(+)-stimulated subfamily. {ECO:0000255|HAMAP-
CC Rule:MF_01129}.
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DR EMBL; CP000141; ABB14908.1; -; Genomic_DNA.
DR RefSeq; WP_011343234.1; NC_007503.1.
DR AlphaFoldDB; Q3AFC6; -.
DR SMR; Q3AFC6; -.
DR STRING; 246194.CHY_0286; -.
DR EnsemblBacteria; ABB14908; ABB14908; CHY_0286.
DR KEGG; chy:CHY_0286; -.
DR eggNOG; COG3808; Bacteria.
DR HOGENOM; CLU_008743_3_1_9; -.
DR OMA; MATTAMQ; -.
DR OrthoDB; 98036at2; -.
DR Proteomes; UP000002706; 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 1: Evidence at protein level;
KW Calcium; Cell membrane; Hydrogen ion transport; Ion transport; Magnesium;
KW Membrane; Metal-binding; Potassium; Reference proteome; Translocase;
KW Transmembrane; Transmembrane helix; Transport.
FT CHAIN 1..686
FT /note="K(+)-stimulated pyrophosphate-energized proton pump"
FT /id="PRO_0000401066"
FT TRANSMEM 6..26
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 89..109
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01129"
FT TRANSMEM 139..159
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01129"
FT TRANSMEM 165..185
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 264..284
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01129"
FT TRANSMEM 294..314
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01129"
FT TRANSMEM 327..347
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01129"
FT TRANSMEM 386..406
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01129"
FT TRANSMEM 408..428
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01129"
FT TRANSMEM 459..479
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01129"
FT TRANSMEM 509..529
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01129"
FT TRANSMEM 577..597
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 666..686
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01129"
FT BINDING 188
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 191
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 195
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 218
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 221
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 430
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 626
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250"
FT BINDING 652
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250"
FT BINDING 656
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250"
FT BINDING 659
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT SITE 180
FT /note="Important for ion transport"
FT /evidence="ECO:0000250"
FT SITE 225
FT /note="Important for ion transport"
FT /evidence="ECO:0000250"
FT SITE 232
FT /note="Important for ion transport"
FT /evidence="ECO:0000250"
FT SITE 460
FT /note="Important for potassium dependence"
FT SITE 660
FT /note="Important for ion transport"
FT /evidence="ECO:0000250"
FT SITE 671
FT /note="Important for ion transport"
FT /evidence="ECO:0000250"
FT MUTAGEN 460
FT /note="A->K: Confers K(+) independence to both
FT pyrophosphate hydrolysis and pyrophosphate-energized H(+)
FT translocation."
FT /evidence="ECO:0000269|PubMed:12401795"
FT MUTAGEN 463
FT /note="A->T: Does not affect the K(+) dependence of H(+)-
FT PPase. Decreased affinity for K(+)."
FT /evidence="ECO:0000269|PubMed:12401795"
SQ SEQUENCE 686 AA; 71063 MW; 39AAC4A0A6ECBD70 CRC64;
MENGMTLAYY GLGAGILAIL FALYLFSSVL KEDMGNEKMR EISQAIFEGA MAYLNRQYKT
LIPFALVVFV LLVVGFGYKE GDFGYGLKVG VSFLVGAIAS ALAGYAGMTS TTKANARTTQ
AARKSLNAAL NVAFRAGGVM GMSVAGLGLL GVSALYIIFK DVHVIDSFAF GASAIAFFAR
VGGGIYTKAA DVGADLVGKV EAGIPEDDPR NPAVIADNVG DNVGDTAGMG ADLFESYGAT
TMAAMLLGLT FAKNHGFSEV LGATFPLLLG AAGIVAAIIS TFFVRTSEDG NPQMALNIGL
WSTNFITAIF TYIIAQYVFG SEWAPKIFIA VVSGLVVNVA IGSLTEYYTS NLKPPAQKIA
EASTTGPATN IISGIAVGMR STYLPIIVIV AAIMVGYWAA GFYGIALAAM GMLATAAMVV
AVDSFGPVAD NAGGIAEMAE LGPEIRNKTD KLDAVGNTTA AVAKGFAIGS AALTALALFS
AYTDLAKTNP NLQKYLVNGK FDLNITDPWV LVGLFLGGTV AFLVAALTME SVGKAAFDMI
EEVRRQFREI PGLMEGKARP DYARCVSIST AAAIRQMIAP GLLAVGAPLA IGFILGFKAL
TGYLAGVTAT GVLLAIYMAN AGGAWDNAKK YIEAGNLGGK GSDTHKAAVV GDTVGDPFKD
TSGPAMNPLM KVAGTFALII VPLLLF
