HPPA_BRUSU
ID HPPA_BRUSU Reviewed; 718 AA.
AC Q8G1E6; G0K8J0; Q8VRZ4;
DT 25-JUL-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2003, sequence version 1.
DT 03-AUG-2022, entry version 107.
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};
GN OrderedLocusNames=BR0771, BS1330_I0767;
OS Brucella suis biovar 1 (strain 1330).
OC Bacteria; Proteobacteria; Alphaproteobacteria; Hyphomicrobiales;
OC Brucellaceae; Brucella/Ochrobactrum group; Brucella.
OX NCBI_TaxID=204722;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=1330;
RX PubMed=12271122; DOI=10.1073/pnas.192319099;
RA Paulsen I.T., Seshadri R., Nelson K.E., Eisen J.A., Heidelberg J.F.,
RA Read T.D., Dodson R.J., Umayam L.A., Brinkac L.M., Beanan M.J.,
RA Daugherty S.C., DeBoy R.T., Durkin A.S., Kolonay J.F., Madupu R.,
RA Nelson W.C., Ayodeji B., Kraul M., Shetty J., Malek J.A., Van Aken S.E.,
RA Riedmuller S., Tettelin H., Gill S.R., White O., Salzberg S.L.,
RA Hoover D.L., Lindler L.E., Halling S.M., Boyle S.M., Fraser C.M.;
RT "The Brucella suis genome reveals fundamental similarities between animal
RT and plant pathogens and symbionts.";
RL Proc. Natl. Acad. Sci. U.S.A. 99:13148-13153(2002).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=1330;
RX PubMed=22038969; DOI=10.1128/jb.06181-11;
RA Tae H., Shallom S., Settlage R., Preston D., Adams L.G., Garner H.R.;
RT "Revised genome sequence of Brucella suis 1330.";
RL J. Bacteriol. 193:6410-6410(2011).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 39-718.
RA Jumas-Bilak E., Michaux-Charachon S., Teyssier C.;
RT "High prevalence of the H+ proton-pumping inorganic pyrophosphatase gene in
RT alpha proteobacteria and evidence of lateral transfer in its phylogeny.";
RL Submitted (SEP-2001) to the EMBL/GenBank/DDBJ databases.
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; AE014291; AAN29700.1; -; Genomic_DNA.
DR EMBL; CP002997; AEM18117.1; -; Genomic_DNA.
DR EMBL; AF417512; AAL69328.1; -; Genomic_DNA.
DR RefSeq; WP_006190074.1; NZ_KN046804.1.
DR AlphaFoldDB; Q8G1E6; -.
DR SMR; Q8G1E6; -.
DR EnsemblBacteria; AEM18117; AEM18117; BS1330_I0767.
DR GeneID; 45051843; -.
DR KEGG; bms:BR0771; -.
DR KEGG; bsi:BS1330_I0767; -.
DR PATRIC; fig|204722.21.peg.2649; -.
DR HOGENOM; CLU_008743_3_1_5; -.
DR OMA; MATTAMQ; -.
DR Proteomes; UP000007104; Chromosome I.
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..718
FT /note="K(+)-insensitive pyrophosphate-energized proton
FT pump"
FT /id="PRO_0000217012"
FT TRANSMEM 6..26
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01129"
FT TRANSMEM 61..81
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 112..132
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01129"
FT TRANSMEM 133..153
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01129"
FT TRANSMEM 168..188
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01129"
FT TRANSMEM 235..255
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 300..320
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01129"
FT TRANSMEM 335..355
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01129"
FT TRANSMEM 385..405
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01129"
FT TRANSMEM 413..433
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01129"
FT TRANSMEM 472..492
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01129"
FT TRANSMEM 524..544
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 620..640
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01129"
FT TRANSMEM 695..715
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01129"
FT BINDING 190
FT /ligand="substrate"
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 197
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
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 223
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 441
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 650
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250"
FT BINDING 682
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250"
FT BINDING 686
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250"
FT BINDING 689
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT SITE 182
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 234
FT /note="Important for ion transport"
FT /evidence="ECO:0000250"
FT SITE 471
FT /note="Determinant of potassium independence"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01129"
FT SITE 690
FT /note="Important for ion transport"
FT /evidence="ECO:0000250"
FT SITE 701
FT /note="Important for ion transport"
FT /evidence="ECO:0000250"
FT CONFLICT 98
FT /note="G -> E (in Ref. 3; AAL69328)"
FT /evidence="ECO:0000305"
FT CONFLICT 113
FT /note="A -> V (in Ref. 3; AAL69328)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 718 AA; 73369 MW; B31744D1D5A046FC CRC64;
MQMGMAVLVL VIACGVLSVL FAIWAIRSVL AADQGTQRMQ EIAEAIREGA SAYLTRQYST
IAIVGIVVFL LAWYLLSLNA AMGFLIGAVL SGVTGFIGMH VSVRANVRTA QAASLSLAGG
LELAFKSGAI TGLLVAGLAL LGVSVYYFVL TVWLGYAPAD RTVIDSLVSL GFGASLISIF
ARLGGGIFTK GADVGGDLVG KVEAGIPEDD PRNPATIADN VGDNVGDCAG MAADLFETYA
VTVVATMVLG AIFFHGSDAL TNVMLYPLMI CGACVITSIV GTFFVKLGVN GSIMGALYKG
LIATGLLSIV GLGVANTLTV GWGEIGTVAG KSITGTNLFV CGLIGLIVTG LIVVITEYYT
GTNKRPVNSI AQASVTGHGT NVIQGLAVSL ESTALPAIVI VGGIISTYQL AGLFGTAIAV
TAMLGIAGMI VALDAFGPVT DNAGGIAEMA GLDPEVRKAT DALDAVGNTT KAVTKGYAIG
SAGLGALVLF AAYSNDLAYF AANGQIYPYF ADMGPVSFDL SNPYVVAGLI FGGLIPYLFG
GMAMTAVGRA GGAVVQEVRR QFREKPGIMT GKERPDYARA VDLLTKAAIR EMIIPSLLPV
LAPIVVYFGV LLISGSKAAA FAALGASLLG VIINGLFVAI SMTSGGGAWD NAKKSFEDGF
TDADGVKHMK GSEAHKASVT GDTVGDPYKD TAGPAVNPAI KITNIVALLL LAVLAHMA
