HPPA2_MOOTA
ID HPPA2_MOOTA Reviewed; 682 AA.
AC Q2RLE0;
DT 30-NOV-2010, integrated into UniProtKB/Swiss-Prot.
DT 24-JAN-2006, sequence version 1.
DT 03-AUG-2022, entry version 87.
DE RecName: Full=K(+)-insensitive pyrophosphate-energized proton pump 2 {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 2 {ECO:0000255|HAMAP-Rule:MF_01129};
DE AltName: Full=Pyrophosphate-energized inorganic pyrophosphatase 2 {ECO:0000255|HAMAP-Rule:MF_01129};
DE Short=H(+)-PPase 2 {ECO:0000255|HAMAP-Rule:MF_01129};
GN Name=hppA2 {ECO:0000255|HAMAP-Rule:MF_01129}; OrderedLocusNames=Moth_0418;
OS Moorella thermoacetica (strain ATCC 39073 / JCM 9320).
OC Bacteria; Firmicutes; Clostridia; Thermoanaerobacterales;
OC Thermoanaerobacteraceae; Moorella group; Moorella.
OX NCBI_TaxID=264732;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 39073 / JCM 9320;
RX PubMed=18631365; DOI=10.1111/j.1462-2920.2008.01679.x;
RA Pierce E., Xie G., Barabote R.D., Saunders E., Han C.S., Detter J.C.,
RA Richardson P., Brettin T.S., Das A., Ljungdahl L.G., Ragsdale S.W.;
RT "The complete genome sequence of Moorella thermoacetica (f. Clostridium
RT thermoaceticum).";
RL Environ. Microbiol. 10:2550-2573(2008).
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}.
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DR EMBL; CP000232; ABC18749.1; -; Genomic_DNA.
DR RefSeq; WP_011391956.1; NC_007644.1.
DR RefSeq; YP_429292.1; NC_007644.1.
DR AlphaFoldDB; Q2RLE0; -.
DR SMR; Q2RLE0; -.
DR STRING; 264732.Moth_0418; -.
DR EnsemblBacteria; ABC18749; ABC18749; Moth_0418.
DR KEGG; mta:Moth_0418; -.
DR PATRIC; fig|264732.11.peg.452; -.
DR eggNOG; COG3808; Bacteria.
DR HOGENOM; CLU_008743_3_1_9; -.
DR OMA; GWKGILF; -.
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..682
FT /note="K(+)-insensitive pyrophosphate-energized proton pump
FT 2"
FT /id="PRO_0000401183"
FT TRANSMEM 1..21
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01129"
FT TRANSMEM 56..76
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01129"
FT TRANSMEM 78..98
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01129"
FT TRANSMEM 130..150
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01129"
FT TRANSMEM 160..180
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01129"
FT TRANSMEM 237..257
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01129"
FT TRANSMEM 258..278
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01129"
FT TRANSMEM 291..311
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01129"
FT TRANSMEM 318..338
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01129"
FT TRANSMEM 353..373
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01129"
FT TRANSMEM 375..395
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01129"
FT TRANSMEM 404..424
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 506..526
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01129"
FT TRANSMEM 574..594
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01129"
FT TRANSMEM 595..615
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01129"
FT TRANSMEM 662..682
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01129"
FT BINDING 183
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 186
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 190
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 432
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 623
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250"
FT BINDING 649
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250"
FT BINDING 653
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250"
FT BINDING 656
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT SITE 220
FT /note="Important for ion transport"
FT /evidence="ECO:0000250"
FT SITE 227
FT /note="Important for ion transport"
FT /evidence="ECO:0000250"
FT SITE 462
FT /note="Determinant of potassium independence"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01129"
FT SITE 657
FT /note="Important for ion transport"
FT /evidence="ECO:0000250"
FT SITE 668
FT /note="Important for ion transport"
FT /evidence="ECO:0000250"
SQ SEQUENCE 682 AA; 70892 MW; EB2C42189831A9AF CRC64;
MELFPIIPAG GILALLVALY MTSSVLKEDT GPKEMQTIAA AIREGAMAFL NRQYRTIAGL
ALIVAVLLAL LTRQYHTAVA FITGAFASAL SGYIGMYVAV NANLRVAAGA RNSLNKALTV
AFRGGAVTGL AVTALSLLGV TSLFYAFGGA TNPTRAPLDI VGFGFGASFV ALFAQLSGGI
YTKAADVGAD LVGKVEAGIP EDDPRNPAVI ADLVGDNVGD CAGRGADLFE STAAENIGAM
ILGIALVPFF GVKGIVFPLV ARAAGIIASI IGMFFVRAEE NQDPMAALNR GYIVTSILAI
IFLYPISRYM LSGPGVNFIY FYGAGIIGIV LSFIFVLITQ YYTSYDYRPV KEIARASITG
PATNIISGVA VGFESTALPV VFISLAILGA YWLGLKSGLP GGGLYGTAVA TMGMLSTAAY
ILAMDTYGPI TDNAGGIVEM SGAPEEVRRR TDRLDASGNT TKALTKGYAI GSAALATFLL
FSAYIDEVKI ALNIKGNFPV DIGKPEVFVG AFIAAMMVLL FSSTAIRAVG NAAQYVILEV
RRQFKEIPGI MEGTAKPEYG ACVDIVTRGA LKEMVLPGLI VVITPIIVGL VLKAEAAAAF
LMVGTITGVI VALFLNNGGG AWDNAKKYIE LGNFGGKGSE AHKAGVVGDT VGDPFKDTAG
PSLHVLVKLI STITLVLAGL FI
