HPPA1_METMA
ID HPPA1_METMA Reviewed; 676 AA.
AC Q8PYZ8;
DT 25-JUL-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2002, sequence version 1.
DT 03-AUG-2022, entry version 131.
DE RecName: Full=K(+)-stimulated pyrophosphate-energized sodium pump;
DE EC=7.2.3.- {ECO:0000255|HAMAP-Rule:MF_01129, ECO:0000269|PubMed:17605473};
DE AltName: Full=Membrane-bound sodium-translocating pyrophosphatase {ECO:0000255|HAMAP-Rule:MF_01129};
DE AltName: Full=Mm-PPase;
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=hppA1 {ECO:0000255|HAMAP-Rule:MF_01129}; OrderedLocusNames=MM_0700;
OS Methanosarcina mazei (strain ATCC BAA-159 / DSM 3647 / Goe1 / Go1 / JCM
OS 11833 / OCM 88) (Methanosarcina frisia).
OC Archaea; Euryarchaeota; Stenosarchaea group; Methanomicrobia;
OC Methanosarcinales; Methanosarcinaceae; Methanosarcina.
OX NCBI_TaxID=192952;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC BAA-159 / DSM 3647 / Goe1 / Go1 / JCM 11833 / OCM 88;
RA Baeumer S., Lentes S., Gottschalk G., Deppenmeier U.;
RT "Identification and analysis of proton-translocating pyrophosphatases in
RT the methanogenic archaeon Methanosarcina mazei.";
RL Submitted (MAY-2002) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-159 / DSM 3647 / Goe1 / Go1 / JCM 11833 / OCM 88;
RX PubMed=12125824;
RA Deppenmeier U., Johann A., Hartsch T., Merkl R., Schmitz R.A.,
RA Martinez-Arias R., Henne A., Wiezer A., Baeumer S., Jacobi C.,
RA Brueggemann H., Lienard T., Christmann A., Boemecke M., Steckel S.,
RA Bhattacharyya A., Lykidis A., Overbeek R., Klenk H.-P., Gunsalus R.P.,
RA Fritz H.-J., Gottschalk G.;
RT "The genome of Methanosarcina mazei: evidence for lateral gene transfer
RT between Bacteria and Archaea.";
RL J. Mol. Microbiol. Biotechnol. 4:453-461(2002).
RN [3]
RP FUNCTION, CATALYTIC ACTIVITY, COFACTOR, ACTIVITY REGULATION,
RP BIOPHYSICOCHEMICAL PROPERTIES, AND SUBCELLULAR LOCATION.
RX PubMed=17605473; DOI=10.1021/bi700564b;
RA Malinen A.M., Belogurov G.A., Baykov A.A., Lahti R.;
RT "Na+-pyrophosphatase: a novel primary sodium pump.";
RL Biochemistry 46:8872-8878(2007).
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, ECO:0000269|PubMed:17605473}.
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 ECO:0000269|PubMed:17605473};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_01129,
CC ECO:0000269|PubMed:17605473};
CC -!- ACTIVITY REGULATION: Requires K(+) for maximal activity. Inhibited by
CC the Na(+) ionophore monensin, activated by the K(+) ionophore
CC valinomycin and unaffected by the protonophore CCCP.
CC {ECO:0000255|HAMAP-Rule:MF_01129, ECO:0000269|PubMed:17605473}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC pH dependence:
CC Optimum pH is 7.5. {ECO:0000269|PubMed:17605473};
CC -!- SUBUNIT: Homodimer. {ECO:0000255|HAMAP-Rule:MF_01129}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000255|HAMAP-Rule:MF_01129,
CC ECO:0000269|PubMed:17605473}; Multi-pass membrane protein
CC {ECO:0000255|HAMAP-Rule:MF_01129, ECO:0000269|PubMed:17605473}.
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; AF312701; AAM22543.1; -; Genomic_DNA.
DR EMBL; AE008384; AAM30396.1; -; Genomic_DNA.
DR RefSeq; WP_011032651.1; NC_003901.1.
DR AlphaFoldDB; Q8PYZ8; -.
DR SMR; Q8PYZ8; -.
DR TCDB; 3.A.10.1.14; the h(+), na(+)-translocating pyrophosphatase (m(+)-ppase) family.
DR EnsemblBacteria; AAM30396; AAM30396; MM_0700.
DR GeneID; 44086082; -.
DR KEGG; mma:MM_0700; -.
DR PATRIC; fig|192952.21.peg.833; -.
DR eggNOG; arCOG04949; Archaea.
DR HOGENOM; CLU_008743_3_1_2; -.
DR OMA; GWKGILF; -.
DR BRENDA; 7.1.3.2; 3270.
DR Proteomes; UP000000595; 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; Ion transport; Magnesium; Membrane; Metal-binding;
KW Potassium; Reference proteome; Sodium; Sodium transport; Translocase;
KW Transmembrane; Transmembrane helix; Transport.
FT CHAIN 1..676
FT /note="K(+)-stimulated pyrophosphate-energized sodium pump"
FT /id="PRO_0000217007"
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 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 158..178
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01129"
FT TRANSMEM 241..261
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01129"
FT TRANSMEM 265..285
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01129"
FT TRANSMEM 298..318
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01129"
FT TRANSMEM 324..344
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01129"
FT TRANSMEM 390..410
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01129"
FT TRANSMEM 411..431
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01129"
FT TRANSMEM 469..489
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01129"
FT TRANSMEM 501..521
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01129"
FT TRANSMEM 572..592
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01129"
FT TRANSMEM 593..613
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01129"
FT TRANSMEM 656..676
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 433
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 617
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250"
FT BINDING 643
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250"
FT BINDING 647
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250"
FT BINDING 650
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 463
FT /note="Important for potassium dependence"
FT /evidence="ECO:0000250"
FT SITE 651
FT /note="Important for ion transport"
FT /evidence="ECO:0000250"
FT SITE 662
FT /note="Important for ion transport"
FT /evidence="ECO:0000250"
SQ SEQUENCE 676 AA; 69221 MW; 36DFDBDA732A9AD8 CRC64;
MDMLIYLTPI CALIGLIFAG ISYKNVRNEG EGNELIKKIT AAIHGGAMVY LNRQYRAIAV
FVVFIAIVLA LVLPNGVLTA ACFVFGAVLS ATAGYAGMLT ATIANGRTTN AATRGIGPAF
KVSFASGTVM GMSVVGLGLF GLSLSFIILG NIYTDMDLFT LLNIIAGFSF GASSIALFAR
VGGGIFTKAA DVGADLVGKV EAGIPEDDPR NPAVIADNVG DNVGDIAGMG ADLYESYVGS
IIATMLLAAS TAAATFPGIP VMNVVMVPLV IAAVGILASV IGTFFVRTNK TESSAIHMAF
NMGLIAAIVL TVIASYVVTG HLLGGYGLNV FFSTVAGLVA GFLIGQITEH YTSYDKKPTL
TVAHSCQTGS ATNVITGFAK GMESTLWPAV IISIAIYIAF QLAGLYGIAI AAVGMLATLG
ISLSVDAYGP VADNAGGIAE MSHQKKEVRQ ITDTLDAVGN TTAAMGKGFA IGSAALTALS
LFASYAIAVG LTSIDVMNPN VFIGLIIGAM LPFLFSSMTI LAVGNAAGEV VVEVRRQFKE
IKGLMEGKAD PDYSKCITIS THSALKEMIP PGILAVIAPI LVGLVLGAGA LGGLLAGSVV
SGFMLAITMS NAGGSWDNAK KFIELGNFGG KGSDAHKAGV TGDTVGDPFK DTAGPAINIL
IKLMSIVALV FAPLFI
