HPPA_XANAC
ID HPPA_XANAC Reviewed; 675 AA.
AC Q8PH20;
DT 25-JUL-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2002, sequence version 1.
DT 03-AUG-2022, entry version 114.
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=XAC3440;
OS Xanthomonas axonopodis pv. citri (strain 306).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Xanthomonadales;
OC Xanthomonadaceae; Xanthomonas.
OX NCBI_TaxID=190486;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=306;
RX PubMed=12024217; DOI=10.1038/417459a;
RA da Silva A.C.R., Ferro J.A., Reinach F.C., Farah C.S., Furlan L.R.,
RA Quaggio R.B., Monteiro-Vitorello C.B., Van Sluys M.A., Almeida N.F. Jr.,
RA Alves L.M.C., do Amaral A.M., Bertolini M.C., Camargo L.E.A., Camarotte G.,
RA Cannavan F., Cardozo J., Chambergo F., Ciapina L.P., Cicarelli R.M.B.,
RA Coutinho L.L., Cursino-Santos J.R., El-Dorry H., Faria J.B.,
RA Ferreira A.J.S., Ferreira R.C.C., Ferro M.I.T., Formighieri E.F.,
RA Franco M.C., Greggio C.C., Gruber A., Katsuyama A.M., Kishi L.T.,
RA Leite R.P., Lemos E.G.M., Lemos M.V.F., Locali E.C., Machado M.A.,
RA Madeira A.M.B.N., Martinez-Rossi N.M., Martins E.C., Meidanis J.,
RA Menck C.F.M., Miyaki C.Y., Moon D.H., Moreira L.M., Novo M.T.M.,
RA Okura V.K., Oliveira M.C., Oliveira V.R., Pereira H.A., Rossi A.,
RA Sena J.A.D., Silva C., de Souza R.F., Spinola L.A.F., Takita M.A.,
RA Tamura R.E., Teixeira E.C., Tezza R.I.D., Trindade dos Santos M.,
RA Truffi D., Tsai S.M., White F.F., Setubal J.C., Kitajima J.P.;
RT "Comparison of the genomes of two Xanthomonas pathogens with differing host
RT specificities.";
RL Nature 417:459-463(2002).
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; AE008923; AAM38283.1; -; Genomic_DNA.
DR RefSeq; WP_011052280.1; NC_003919.1.
DR AlphaFoldDB; Q8PH20; -.
DR SMR; Q8PH20; -.
DR STRING; 190486.XAC3440; -.
DR PRIDE; Q8PH20; -.
DR EnsemblBacteria; AAM38283; AAM38283; XAC3440.
DR GeneID; 66912483; -.
DR KEGG; xac:XAC3440; -.
DR eggNOG; COG3808; Bacteria.
DR HOGENOM; CLU_008743_3_1_6; -.
DR OMA; MATTAMQ; -.
DR Proteomes; UP000000576; 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; Translocase;
KW Transmembrane; Transmembrane helix; Transport.
FT CHAIN 1..675
FT /note="K(+)-insensitive pyrophosphate-energized proton
FT pump"
FT /id="PRO_0000217034"
FT TRANSMEM 5..25
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01129"
FT TRANSMEM 65..85
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 164..184
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 258..278
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01129"
FT TRANSMEM 287..307
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01129"
FT TRANSMEM 321..341
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01129"
FT TRANSMEM 384..404
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01129"
FT TRANSMEM 405..425
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01129"
FT TRANSMEM 458..478
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01129"
FT TRANSMEM 500..520
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01129"
FT TRANSMEM 568..588
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01129"
FT TRANSMEM 590..610
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01129"
FT TRANSMEM 655..675
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 427
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 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 457
FT /note="Determinant of potassium independence"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01129"
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 675 AA; 69285 MW; 05C28DAEDFA8106B CRC64;
MLEHYGLWLA LGCAVLAIVY GIVSARWVVA QPSGNARMQE IAAAIQEGAR AYLNRQYLTI
SVAGAVLFVL VGLFLSWYTA IGFALGAVLS GLAGYIGMNV SVRANVRTAE AARHGIGKAM
DVAFRGGAIT GMLVVGLGLL GVAGYFAVLQ GMGLPLEQNL HALVGLAFGS SLISIFARLG
GGIFTKGADV GADLVGKVEA GIPEDDPRNP AVIADNVGDN VGDCAGMAAD LFETYAVTVI
ATMLLGSLTL ADTGSHAVLY PLVLGGVSII ASIVGAAFVK VKDGGSIMGA LYKGVIVSGV
LAALAYWPIT QSLMRDNIHG ATALYACALI GLVLTGLIVW ITEYYTGTQY TPVQHVASAS
TTGHGTNIIA GLGISMKSTA LPVIAVCAAI WGAFHFGGLY GIAIAATAML SMAGMIVALD
AYGPITDNAG GIAEMAELPP EVRNITDPLD AVGNTTKAVT KGYAIGSAAL AALVLFADYT
HNLQAANPDQ VYAFDLSDHT VIIGLLIGGL IPYLFGAMAM EAVGRAAGAV VEEVRRQFRE
LPGIMAGTAK PQYDRAVDML TRSAIGEMIV PSLLPVVVPI IVGLLLGPRA LGGLLIGTIV
TGLFLAISMT TGGGAWDNAK KYIEDGHFGG KGSEAHKAAI TGDTVGDPYK DTAGPAINPL
IKIINIVALL LVPLL
