HPPA_CAUVC
ID HPPA_CAUVC Reviewed; 712 AA.
AC Q9A8J0;
DT 25-JUL-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2001, 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=CC_1363;
OS Caulobacter vibrioides (strain ATCC 19089 / CB15) (Caulobacter crescentus).
OC Bacteria; Proteobacteria; Alphaproteobacteria; Caulobacterales;
OC Caulobacteraceae; Caulobacter.
OX NCBI_TaxID=190650;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 19089 / CB15;
RX PubMed=11259647; DOI=10.1073/pnas.061029298;
RA Nierman W.C., Feldblyum T.V., Laub M.T., Paulsen I.T., Nelson K.E.,
RA Eisen J.A., Heidelberg J.F., Alley M.R.K., Ohta N., Maddock J.R.,
RA Potocka I., Nelson W.C., Newton A., Stephens C., Phadke N.D., Ely B.,
RA DeBoy R.T., Dodson R.J., Durkin A.S., Gwinn M.L., Haft D.H., Kolonay J.F.,
RA Smit J., Craven M.B., Khouri H.M., Shetty J., Berry K.J., Utterback T.R.,
RA Tran K., Wolf A.M., Vamathevan J.J., Ermolaeva M.D., White O.,
RA Salzberg S.L., Venter J.C., Shapiro L., Fraser C.M.;
RT "Complete genome sequence of Caulobacter crescentus.";
RL Proc. Natl. Acad. Sci. U.S.A. 98:4136-4141(2001).
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; AE005673; AAK23344.1; -; Genomic_DNA.
DR PIR; D87418; D87418.
DR RefSeq; NP_420176.1; NC_002696.2.
DR RefSeq; WP_010919240.1; NC_002696.2.
DR AlphaFoldDB; Q9A8J0; -.
DR SMR; Q9A8J0; -.
DR STRING; 190650.CC_1363; -.
DR EnsemblBacteria; AAK23344; AAK23344; CC_1363.
DR KEGG; ccr:CC_1363; -.
DR PATRIC; fig|190650.5.peg.1393; -.
DR eggNOG; COG3808; Bacteria.
DR HOGENOM; CLU_008743_3_1_5; -.
DR OMA; MATTAMQ; -.
DR BioCyc; CAULO:CC1363-MON; -.
DR Proteomes; UP000001816; 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..712
FT /note="K(+)-insensitive pyrophosphate-energized proton
FT pump"
FT /id="PRO_0000217013"
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 79..99
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 165..185
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 262..282
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01129"
FT TRANSMEM 293..313
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01129"
FT TRANSMEM 330..350
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01129"
FT TRANSMEM 393..413
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01129"
FT TRANSMEM 414..434
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01129"
FT TRANSMEM 467..487
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01129"
FT TRANSMEM 519..539
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01129"
FT TRANSMEM 588..608
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01129"
FT TRANSMEM 614..634
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 436
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 644
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250"
FT BINDING 676
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250"
FT BINDING 680
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250"
FT BINDING 683
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 466
FT /note="Determinant of potassium independence"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01129"
FT SITE 684
FT /note="Important for ion transport"
FT /evidence="ECO:0000250"
FT SITE 695
FT /note="Important for ion transport"
FT /evidence="ECO:0000250"
SQ SEQUENCE 712 AA; 72944 MW; 9092102AF55990C4 CRC64;
MSLWLYLAIG AGLLAVLYGA VQTASLMRAS AGNARMQEIA AAIQEGAQAY LKRQYTTISI
VGVVVIAALA FFFKSWEQPV GFALGAILSG AAGFAGMLIS VRANVRTAQA SSESLAKGLS
MAFTSGAVTG MLVAGFALLG VAGYYYVLLA TGHEATGRVV IDSLVALGFG ASLISIFARL
GGGIFTKGAD VGGDLVGKVE AGIPEDDPRN AATIADNVGD NVGDCAGMAA DLFETYAVTT
VATMVLAAIF FRGTEAVSAM MLLPLAICAV CIVTSIIGAF FVRLGKSQNI MGALYQGLIV
TGVLSIPAVW YVIHQLVPTA VEVDGRSYGA DALFYCGLAG LVVTAAIVMI TEYYTGTGFR
PVKSVAQASV SGHGTNVIQG LAMSLESTAL PALTIIVGIV VTYNLAGLFG IAIATTTMLS
LAGFIVALDA FGPVTDNAGG IAEMAGLPPE VRVTTDALDA VGNTTKAVTK GYAIGSAGLG
ALVLFAAYTE DLKFFSENAA PGSFFHGMGA VTFDLSNPYV VVGLLFGGLL PFLFGGLSMT
AVGRAAESVV AEVRRQFRDN PGIMTGEVKP EYGKAVDILT KAAIREMIVP SLLPVVSPVA
LFFVIQAIAG KVDAFAALGA MLMGVIVTGL FVAISMTSGG GAWDNAKKVI EEGFTDKNGV
LHKKGGETHK AAVTGDTVGD PYKDTSGPAV NPMIKITNIV ALLLLAVLAH GV
