HPPA_NITEU
ID HPPA_NITEU Reviewed; 685 AA.
AC Q82TF3;
DT 25-JUL-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2003, sequence version 1.
DT 03-AUG-2022, entry version 104.
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=NE1935;
OS Nitrosomonas europaea (strain ATCC 19718 / CIP 103999 / KCTC 2705 / NBRC
OS 14298).
OC Bacteria; Proteobacteria; Betaproteobacteria; Nitrosomonadales;
OC Nitrosomonadaceae; Nitrosomonas.
OX NCBI_TaxID=228410;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 19718 / CIP 103999 / KCTC 2705 / NBRC 14298;
RX PubMed=12700255; DOI=10.1128/jb.185.9.2759-2773.2003;
RA Chain P., Lamerdin J.E., Larimer F.W., Regala W., Lao V., Land M.L.,
RA Hauser L., Hooper A.B., Klotz M.G., Norton J., Sayavedra-Soto L.A.,
RA Arciero D.M., Hommes N.G., Whittaker M.M., Arp D.J.;
RT "Complete genome sequence of the ammonia-oxidizing bacterium and obligate
RT chemolithoautotroph Nitrosomonas europaea.";
RL J. Bacteriol. 185:2759-2773(2003).
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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AL954747; CAD85846.1; -; Genomic_DNA.
DR RefSeq; WP_011112471.1; NC_004757.1.
DR AlphaFoldDB; Q82TF3; -.
DR SMR; Q82TF3; -.
DR STRING; 228410.NE1935; -.
DR EnsemblBacteria; CAD85846; CAD85846; NE1935.
DR KEGG; neu:NE1935; -.
DR eggNOG; COG3808; Bacteria.
DR HOGENOM; CLU_008743_3_1_4; -.
DR OMA; MATTAMQ; -.
DR OrthoDB; 98036at2; -.
DR PhylomeDB; Q82TF3; -.
DR Proteomes; UP000001416; 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..685
FT /note="K(+)-insensitive pyrophosphate-energized proton
FT pump"
FT /id="PRO_0000217022"
FT TRANSMEM 3..23
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01129"
FT TRANSMEM 55..75
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 127..147
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01129"
FT TRANSMEM 157..177
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 260..280
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01129"
FT TRANSMEM 295..315
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01129"
FT TRANSMEM 333..353
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01129"
FT TRANSMEM 380..400
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01129"
FT TRANSMEM 402..422
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01129"
FT TRANSMEM 475..495
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01129"
FT TRANSMEM 510..530
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01129"
FT TRANSMEM 578..598
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01129"
FT TRANSMEM 600..620
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01129"
FT BINDING 187
FT /ligand="substrate"
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 194
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 217
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 220
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 439
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 627
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 657
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250"
FT BINDING 660
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT SITE 179
FT /note="Important for ion transport"
FT /evidence="ECO:0000250"
FT SITE 224
FT /note="Important for ion transport"
FT /evidence="ECO:0000250"
FT SITE 231
FT /note="Important for ion transport"
FT /evidence="ECO:0000250"
FT SITE 469
FT /note="Determinant of potassium independence"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01129"
FT SITE 661
FT /note="Important for ion transport"
FT /evidence="ECO:0000250"
FT SITE 672
FT /note="Important for ion transport"
FT /evidence="ECO:0000250"
SQ SEQUENCE 685 AA; 70050 MW; C196BDC99CF88507 CRC64;
MANGLTIAIC SAILALIFSG LWIRRIYAQS AGDSRMQEIA AAVQEGASAY LKRQYLTIGM
VGTVLFVIIG LALSWNTAIG FALGAILSGL AGFMGMNVSV QSNVRTAEAA RSGLNEALAI
AFRGGAVTGM LVVGLGLLGV AGYTALLVSG ADETSSISDL IHPLIGFAFG GSLISIFARL
GGGIFTKGAD VGADLVGKVE AGIPEDDPRN PAVIADNVGD NVGDCAGMAA DLFETYAVTI
IATMLLGALL FKTGTGDAAV YPLALGAASI VASIIGCYFV KMREGGKIMN ALYRGLAVAG
GIAFFAYLPI TVWFMGGATL TLDGTEVGGG ELIMRLFAST TIGLVLTGLM VVITEYYTST
EYPPVQHIAN ASTTGHATNI IAGLGVGMRA TAAPVLAVCA SIIVAYSLAG LYGIAIAATA
MLSMTGIIVA LDAYGPITDN AGGIAEMAGM PESVRAVTDP LDAVGNTTKA VTKGYAIGSA
GLAALVLFAD YTHGLEHANK LMTFDLSNHL VIIGLFIGGM VPFLFGAMSM EAVGRAAGSV
VLEVRRQFKE IPGIMDGSRK PDYSRAVDML TKAAIREMIV PSLLPVLIPV LVGVFLGPQA
LGGVLMGSIV TGLFIAISMT AGGGAWDNAK KYIEDGNYGG KGSDAHKAAV TGDTVGDPYK
DTAGPAINPL IKIINIVALL IIPLL
