HPPA_RHORT
ID HPPA_RHORT Reviewed; 702 AA.
AC O68460; Q2RTC7;
DT 25-JUL-2003, integrated into UniProtKB/Swiss-Prot.
DT 21-MAR-2006, sequence version 3.
DT 03-AUG-2022, entry version 123.
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}; Synonyms=rrpP, vppA;
GN OrderedLocusNames=Rru_A1818;
OS Rhodospirillum rubrum (strain ATCC 11170 / ATH 1.1.1 / DSM 467 / LMG 4362 /
OS NCIMB 8255 / S1).
OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhodospirillales;
OC Rhodospirillaceae; Rhodospirillum.
OX NCBI_TaxID=269796;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=9630689; DOI=10.1016/s0005-2728(98)00062-0;
RA Baltscheffsky M., Nadanaciva S., Schultz A.;
RT "A pyrophosphate synthase gene: molecular cloning and sequencing of the
RT cDNA encoding the inorganic pyrophosphate synthase from Rhodospirillum
RT rubrum.";
RL Biochim. Biophys. Acta 1364:301-306(1998).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 11170 / ATH 1.1.1 / DSM 467 / LMG 4362 / NCIMB 8255 / S1;
RX PubMed=21886856; DOI=10.4056/sigs.1804360;
RA Munk A.C., Copeland A., Lucas S., Lapidus A., Del Rio T.G., Barry K.,
RA Detter J.C., Hammon N., Israni S., Pitluck S., Brettin T., Bruce D.,
RA Han C., Tapia R., Gilna P., Schmutz J., Larimer F., Land M., Kyrpides N.C.,
RA Mavromatis K., Richardson P., Rohde M., Goeker M., Klenk H.P., Zhang Y.,
RA Roberts G.P., Reslewic S., Schwartz D.C.;
RT "Complete genome sequence of Rhodospirillum rubrum type strain (S1).";
RL Stand. Genomic Sci. 4:293-302(2011).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-81.
RX PubMed=15292143; DOI=10.1128/jb.186.16.5418-5426.2004;
RA Lopez-Marques R.L., Perez-Castineira J.R., Losada M., Serrano A.;
RT "Differential regulation of soluble and membrane-bound inorganic
RT pyrophosphatases in the photosynthetic bacterium Rhodospirillum rubrum
RT provides insights into pyrophosphate-based stress bioenergetics.";
RL J. Bacteriol. 186:5418-5426(2004).
RN [4]
RP CHARACTERIZATION, AND MUTAGENESIS OF GLY-185; CYS-222 AND CYS-573.
RX PubMed=11956221; DOI=10.1074/jbc.m202951200;
RA Belogurov G.A., Turkina M.V., Penttinen A., Huopalahti S., Baykov A.A.,
RA Lahti R.;
RT "H+-pyrophosphatase of Rhodospirillum rubrum. High yield expression in
RT Escherichia coli and identification of the Cys residues responsible for
RT inactivation my mersalyl.";
RL J. Biol. Chem. 277:22209-22214(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; AF044912; AAC38615.2; -; mRNA.
DR EMBL; CP000230; ABC22618.1; -; Genomic_DNA.
DR EMBL; AJ549291; CAD70568.1; -; Genomic_DNA.
DR RefSeq; WP_011389571.1; NC_007643.1.
DR RefSeq; YP_426905.1; NC_007643.1.
DR AlphaFoldDB; O68460; -.
DR SMR; O68460; -.
DR STRING; 269796.Rru_A1818; -.
DR TCDB; 3.A.10.2.1; the h(+), na(+)-translocating pyrophosphatase (m(+)-ppase) family.
DR EnsemblBacteria; ABC22618; ABC22618; Rru_A1818.
DR KEGG; rru:Rru_A1818; -.
DR PATRIC; fig|269796.9.peg.1896; -.
DR eggNOG; COG3808; Bacteria.
DR HOGENOM; CLU_008743_3_1_5; -.
DR OMA; MATTAMQ; -.
DR OrthoDB; 98036at2; -.
DR PhylomeDB; O68460; -.
DR BRENDA; 7.1.3.1; 5420.
DR Proteomes; UP000001929; 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 1: Evidence at protein level;
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..702
FT /note="K(+)-insensitive pyrophosphate-energized proton
FT pump"
FT /id="PRO_0000217030"
FT TRANSMEM 3..23
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01129"
FT TRANSMEM 63..83
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 162..182
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01129"
FT TRANSMEM 234..254
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01129"
FT TRANSMEM 255..275
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01129"
FT TRANSMEM 294..314
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01129"
FT TRANSMEM 329..349
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01129"
FT TRANSMEM 379..399
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01129"
FT TRANSMEM 407..427
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01129"
FT TRANSMEM 466..486
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01129"
FT TRANSMEM 517..537
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01129"
FT TRANSMEM 586..606
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01129"
FT TRANSMEM 612..632
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01129"
FT BINDING 184
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 187
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 191
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 214
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
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 435
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 642
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250"
FT BINDING 668
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250"
FT BINDING 672
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250"
FT BINDING 675
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT SITE 176
FT /note="Important for ion transport"
FT /evidence="ECO:0000250"
FT SITE 221
FT /note="Important for ion transport"
FT /evidence="ECO:0000250"
FT SITE 228
FT /note="Important for ion transport"
FT /evidence="ECO:0000250"
FT SITE 465
FT /note="Determinant of potassium independence"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01129"
FT SITE 676
FT /note="Important for ion transport"
FT /evidence="ECO:0000250"
FT SITE 687
FT /note="Important for ion transport"
FT /evidence="ECO:0000250"
FT MUTAGEN 185
FT /note="G->A: No effect on activity; decreased sensitivity
FT to the sulfhydryl modifying reagent mersalyl."
FT /evidence="ECO:0000269|PubMed:11956221"
FT MUTAGEN 222
FT /note="C->V: No effect on activity; decreased sensitivity
FT to the sulfhydryl modifying reagent mersalyl."
FT /evidence="ECO:0000269|PubMed:11956221"
FT MUTAGEN 573
FT /note="C->A: No effect on activity; decreased sensitivity
FT to the sulfhydryl modifying reagent mersalyl."
FT /evidence="ECO:0000269|PubMed:11956221"
FT CONFLICT 72
FT /note="L -> V (in Ref. 3; CAD70568)"
FT /evidence="ECO:0000305"
FT CONFLICT 78
FT /note="G -> V (in Ref. 3; CAD70568)"
FT /evidence="ECO:0000305"
FT CONFLICT 185
FT /note="G -> C (in Ref. 1; AAC38615)"
FT /evidence="ECO:0000305"
FT CONFLICT 476
FT /note="A -> S (in Ref. 1; AAC38615)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 702 AA; 71547 MW; 6F0D50BEA919F0F2 CRC64;
MAGIYLFVVA AALAALGYGA LTIKTIMAAD AGTARMQEIS GAVQEGASAF LNRQYKTIAV
VGAVVFVILT ALLGISVGFG FLIGAVCSGI AGYVGMYISV RANVRVAAGA QQGLARGLEL
AFQSGAVTGM LVAGLALLSV AFYYILLVGI GATGRALIDP LVALGFGASL ISIFARLGGG
IFTKGADVGA DLVGKVEAGI PEDDPRNPAV IADNVGDNVG DCAGMAADLF ETYAVTVVAT
MVLASIFFAG VPAMTSMMAY PLAIGGVCIL ASILGTKFVK LGPKNNIMGA LYRGFLVSAG
ASFVGIILAT AIVPGFGDIQ GANGVLYSGF DLFLCAVIGL LVTGLLIWVT EYYTGTNFRP
VRSVAKASTT GHGTNVIQGL AISMEATALP ALIICAAIIT TYQLSGLFGI AITVTSMLAL
AGMVVALDAY GPVTDNAGGI AEMANLPEDV RKTTDALDAV GNTTKAVTKG YAIGSAGLGA
LVLFAAYTED LAFFKANVDA YPAFAGVDVN FSLSSPYVVV GLFIGGLLPY LFGSMGMTAV
GRAAGSVVEE VRRQFREIPG IMEGTAKPEY GRCVDMLTKA AIKEMIIPSL LPVLAPIVLY
FVILGIADKS AAFSALGAML LGVIVTGLFV AISMTAGGGA WDNAKKYIED GHYGGKGSEA
HKAAVTGDTV GDPYKDTAGP AVNPMIKITN IVALLLLAVL AH
