HPPA_PYRAE
ID HPPA_PYRAE Reviewed; 721 AA.
AC Q8ZWI8; Q9V2S8;
DT 25-JUL-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2002, sequence version 1.
DT 03-AUG-2022, entry version 116.
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, ECO:0000269|PubMed:10556526};
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=PAE1771;
OS Pyrobaculum aerophilum (strain ATCC 51768 / DSM 7523 / JCM 9630 / CIP
OS 104966 / NBRC 100827 / IM2).
OC Archaea; Crenarchaeota; Thermoprotei; Thermoproteales; Thermoproteaceae;
OC Pyrobaculum.
OX NCBI_TaxID=178306;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], CATALYTIC ACTIVITY, COFACTOR, AND
RP BIOPHYSICOCHEMICAL PROPERTIES.
RC STRAIN=ATCC 51768 / DSM 7523 / JCM 9630 / CIP 104966 / NBRC 100827 / IM2;
RX PubMed=10556526; DOI=10.1016/s0014-5793(99)01404-0;
RA Drozdowicz Y.M., Lu Y.-P., Patel V., Fitz-Gibbon S., Miller J.H., Rea P.A.;
RT "A thermostable vacuolar-type membrane pyrophosphatase from the archaeon
RT Pyrobaculum aerophilum: implications for the origins of pyrophosphate-
RT energized pumps.";
RL FEBS Lett. 460:505-512(1999).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 51768 / DSM 7523 / JCM 9630 / CIP 104966 / NBRC 100827 / IM2;
RX PubMed=11792869; DOI=10.1073/pnas.241636498;
RA Fitz-Gibbon S.T., Ladner H., Kim U.-J., Stetter K.O., Simon M.I.,
RA Miller J.H.;
RT "Genome sequence of the hyperthermophilic crenarchaeon Pyrobaculum
RT aerophilum.";
RL Proc. Natl. Acad. Sci. U.S.A. 99:984-989(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 ECO:0000269|PubMed:10556526};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_01129,
CC ECO:0000269|PubMed:10556526};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Temperature dependence:
CC Optimum temperature is 80 degrees Celsius.
CC {ECO:0000269|PubMed:10556526};
CC -!- SUBUNIT: Homodimer. {ECO:0000255|HAMAP-Rule:MF_01129}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000255|HAMAP-Rule:MF_01129};
CC Multi-pass membrane protein {ECO:0000255|HAMAP-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; AF182812; AAF01029.1; -; Genomic_DNA.
DR EMBL; AE009441; AAL63714.1; -; Genomic_DNA.
DR AlphaFoldDB; Q8ZWI8; -.
DR SMR; Q8ZWI8; -.
DR STRING; 178306.PAE1771; -.
DR TCDB; 3.A.10.3.1; the h(+), na(+)-translocating pyrophosphatase (m(+)-ppase) family.
DR EnsemblBacteria; AAL63714; AAL63714; PAE1771.
DR KEGG; pai:PAE1771; -.
DR PATRIC; fig|178306.9.peg.1304; -.
DR eggNOG; arCOG04949; Archaea.
DR HOGENOM; CLU_008743_3_1_2; -.
DR InParanoid; Q8ZWI8; -.
DR OMA; MATTAMQ; -.
DR BRENDA; 7.1.3.1; 5239.
DR Proteomes; UP000002439; 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 membrane; Hydrogen ion transport; Ion transport; Magnesium;
KW Membrane; Metal-binding; Reference proteome; Translocase; Transmembrane;
KW Transmembrane helix; Transport.
FT CHAIN 1..721
FT /note="K(+)-insensitive pyrophosphate-energized proton
FT pump"
FT /id="PRO_0000217038"
FT TRANSMEM 8..28
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01129"
FT TRANSMEM 57..77
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01129"
FT TRANSMEM 82..102
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01129"
FT TRANSMEM 136..156
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 247..267
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 323..343
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01129"
FT TRANSMEM 374..394
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01129"
FT TRANSMEM 416..436
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01129"
FT TRANSMEM 483..503
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01129"
FT TRANSMEM 527..547
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01129"
FT TRANSMEM 599..619
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01129"
FT TRANSMEM 621..641
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01129"
FT TRANSMEM 698..718
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01129"
FT BINDING 191
FT /ligand="substrate"
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 198
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 221
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 224
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 446
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 648
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 676
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250"
FT BINDING 679
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT SITE 183
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 235
FT /note="Important for ion transport"
FT /evidence="ECO:0000250"
FT SITE 476
FT /note="Important for potassium independence"
FT /evidence="ECO:0000250"
FT SITE 680
FT /note="Important for ion transport"
FT /evidence="ECO:0000250"
FT SITE 691
FT /note="Important for ion transport"
FT /evidence="ECO:0000250"
FT CONFLICT 305
FT /note="S -> T (in Ref. 1; AAF01029)"
FT /evidence="ECO:0000305"
FT CONFLICT 553
FT /note="A -> P (in Ref. 1; AAF01029)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 721 AA; 75394 MW; 56D9A64A998C7829 CRC64;
MNMISYALLG VILGISGVIY AVYLAVWVLR QDPGNEKMRF ISQAIATGAR AYLFRQYRTL
AVLLVILAVL ILVAIDMPRR TFGLTALAFI VGALGSMLAG YLGMYVTTRS ASRVAQAAAT
GGMGKALLVS WRAGAVMGLS LASIALLLIS GFYLVFRSVL PDDWAVPLVA LGFGASLVTL
FMRVGGGIYT KAADLGADLV GKVEAGIPED DPRNPGVIAD NVGDNVGDVA GMAADVYESY
IVTVTAAIFL AAILGLPTQF IEAIILFAAL ALVATFAGVN LLKTTGVKHP LSSISLAIYA
TIGLSVVLFF IGAFTLGLDS TKALALAATT SLGAVIAPLI VKITDYYTSY NYGPVRKIAE
QAKISPATVI ITGYGVGLMS AIPVIAVIVA VLGISYMIGY YTVPVSGFGE LSKYLAGIFG
TAMASVGLLV VAGIIITADS YGPVSDNAGG VVEMAGLPDE VREITDVLDS VGNTTKATTK
GYAIASAALA ALVLFIALIF EIVYSASKIL GKGIVDMISE SLSGLQLINA NVLIGAFLGV
ALVYFFSSRT LEAVGRTAME IVEEIRRQFR EKPGILEWKE QPDYARVVDI ATRRALGEFL
IPGLAAIVLP LITGLLLGWN ALAGLIMGAI VAGVPRALLM ANAGGAWDNA KKYIEIQGLK
KTEMHKAAVI GDTVGDPMKD TVGPSLNPLI KVLNTLSVVF TYVIVSTNIA LGIWPSGLLP
F
