(data stored in SCRATCH zone)

SWISSPROT: Q47TP2_THEFY

ID   Q47TP2_THEFY            Unreviewed;       812 AA.
AC   Q47TP2;
DT   13-SEP-2005, integrated into UniProtKB/TrEMBL.
DT   13-SEP-2005, sequence version 1.
DT   08-MAY-2019, entry version 86.
DE   RecName: Full=K(+)-insensitive pyrophosphate-energized proton pump {ECO:0000256|HAMAP-Rule:MF_01129};
DE            EC=7.1.3.1 {ECO:0000256|HAMAP-Rule:MF_01129};
DE   AltName: Full=Membrane-bound proton-translocating pyrophosphatase {ECO:0000256|HAMAP-Rule:MF_01129};
DE   AltName: Full=Pyrophosphate-energized inorganic pyrophosphatase {ECO:0000256|HAMAP-Rule:MF_01129};
DE            Short=H(+)-PPase {ECO:0000256|HAMAP-Rule:MF_01129};
GN   Name=hppA {ECO:0000256|HAMAP-Rule:MF_01129};
GN   OrderedLocusNames=Tfu_0134 {ECO:0000313|EMBL:AAZ54172.1};
OS   Thermobifida fusca (strain YX).
OC   Bacteria; Actinobacteria; Streptosporangiales; Nocardiopsaceae;
OC   Thermobifida.
OX   NCBI_TaxID=269800 {ECO:0000313|EMBL:AAZ54172.1, ECO:0000313|Proteomes:UP000000434};
RN   [1] {ECO:0000313|Proteomes:UP000000434}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=YX {ECO:0000313|Proteomes:UP000000434};
RX   PubMed=17209016; DOI=10.1128/JB.01899-06;
RA   Lykidis A., Mavromatis K., Ivanova N., Anderson I., Land M.,
RA   DiBartolo G., Martinez M., Lapidus A., Lucas S., Copeland A.,
RA   Richardson P., Wilson D.B., Kyrpides N.;
RT   "Genome sequence and analysis of the soil cellulolytic actinomycete
RT   Thermobifida fusca YX.";
RL   J. Bacteriol. 189:2477-2486(2007).
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:0000256|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:0000256|HAMAP-Rule:MF_01129};
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000256|HAMAP-
CC         Rule:MF_01129};
CC   -!- SUBUNIT: Homodimer. {ECO:0000256|HAMAP-Rule:MF_01129}.
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000256|HAMAP-
CC       Rule:MF_01129}; Multi-pass membrane protein {ECO:0000256|HAMAP-
CC       Rule:MF_01129}.
CC   -!- SIMILARITY: Belongs to the H(+)-translocating pyrophosphatase
CC       (TC 3.A.10) family. K(+)-insensitive subfamily.
CC       {ECO:0000256|HAMAP-Rule:MF_01129}.
CC   -!- CAUTION: Lacks conserved residue(s) required for the propagation
CC       of feature annotation. {ECO:0000256|HAMAP-Rule:MF_01129}.
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DR   EMBL; CP000088; AAZ54172.1; -; Genomic_DNA.
DR   STRING; 269800.Tfu_0134; -.
DR   EnsemblBacteria; AAZ54172; AAZ54172; Tfu_0134.
DR   KEGG; tfu:Tfu_0134; -.
DR   eggNOG; ENOG4105EAY; Bacteria.
DR   eggNOG; COG3808; LUCA.
DR   HOGENOM; HOG000007098; -.
DR   KO; K15987; -.
DR   OMA; MATTAMQ; -.
DR   Proteomes; UP000000434; Chromosome.
DR   GO; GO:0005887; C:integral component of plasma membrane; IEA:UniProtKB-UniRule.
DR   GO; GO:0009678; F:hydrogen-translocating pyrophosphatase activity; 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:1902600; P:proton transmembrane transport; 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;
DR   PRODOM; Q47TP2.
DR   SWISS-2DPAGE; Q47TP2.
KW   Cell membrane {ECO:0000256|HAMAP-Rule:MF_01129};
KW   Complete proteome {ECO:0000313|Proteomes:UP000000434};
KW   Hydrogen ion transport {ECO:0000256|HAMAP-Rule:MF_01129};
KW   Hydrolase {ECO:0000313|EMBL:AAZ54172.1};
KW   Ion transport {ECO:0000256|HAMAP-Rule:MF_01129};
KW   Magnesium {ECO:0000256|HAMAP-Rule:MF_01129};
KW   Membrane {ECO:0000256|HAMAP-Rule:MF_01129};
KW   Reference proteome {ECO:0000313|Proteomes:UP000000434};
KW   Translocase {ECO:0000256|HAMAP-Rule:MF_01129};
KW   Transmembrane {ECO:0000256|HAMAP-Rule:MF_01129};
KW   Transmembrane helix {ECO:0000256|HAMAP-Rule:MF_01129};
KW   Transport {ECO:0000256|HAMAP-Rule:MF_01129}.
FT   TRANSMEM     49     70       Helical. {ECO:0000256|HAMAP-Rule:
FT                                MF_01129}.
FT   TRANSMEM    102    120       Helical. {ECO:0000256|HAMAP-Rule:
FT                                MF_01129}.
FT   TRANSMEM    132    153       Helical. {ECO:0000256|HAMAP-Rule:
FT                                MF_01129}.
FT   TRANSMEM    174    201       Helical. {ECO:0000256|HAMAP-Rule:
FT                                MF_01129}.
FT   TRANSMEM    207    225       Helical. {ECO:0000256|HAMAP-Rule:
FT                                MF_01129}.
FT   TRANSMEM    278    296       Helical. {ECO:0000256|HAMAP-Rule:
FT                                MF_01129}.
FT   TRANSMEM    302    322       Helical. {ECO:0000256|HAMAP-Rule:
FT                                MF_01129}.
FT   TRANSMEM    334    358       Helical. {ECO:0000256|HAMAP-Rule:
FT                                MF_01129}.
FT   TRANSMEM    381    405       Helical. {ECO:0000256|HAMAP-Rule:
FT                                MF_01129}.
FT   TRANSMEM    426    454       Helical. {ECO:0000256|HAMAP-Rule:
FT                                MF_01129}.
FT   TRANSMEM    460    483       Helical. {ECO:0000256|HAMAP-Rule:
FT                                MF_01129}.
FT   TRANSMEM    529    548       Helical. {ECO:0000256|HAMAP-Rule:
FT                                MF_01129}.
FT   TRANSMEM    568    589       Helical. {ECO:0000256|HAMAP-Rule:
FT                                MF_01129}.
FT   TRANSMEM    634    652       Helical. {ECO:0000256|HAMAP-Rule:
FT                                MF_01129}.
FT   TRANSMEM    658    677       Helical. {ECO:0000256|HAMAP-Rule:
FT                                MF_01129}.
FT   TRANSMEM    726    744       Helical. {ECO:0000256|HAMAP-Rule:
FT                                MF_01129}.
FT   TRANSMEM    750    768       Helical. {ECO:0000256|HAMAP-Rule:
FT                                MF_01129}.
FT   SITE        523    523       Determinant of potassium independence.
FT                                {ECO:0000256|HAMAP-Rule:MF_01129}.
SQ   SEQUENCE   812 AA;  82734 MW;  D76002499FADDAB2 CRC64;
     MLEGDPSGKP WTAERAPGRG PARLEEDGLT GLNLAADSGA ELALLGMDLT LVIVVLAVAL
     LALAVAGTLV REVLAASQGT ERMQNIARAV QEGAAAYLKR QFRTLAVFVI IIPLLLLLLP
     ADTEAVRWGR SIFFAIGALF SAMTGFLGMW LAVRGNLRVA AAARAGEARA AMRIAFRTGG
     VAGMFTVGLG LLGAALVVLI YRADAPIVLE GFGFGAALLA MFMRVGGGIF TKAADVGADL
     VGKVEHHIPE DDPRNAATIA DNVGDNVGDC AGMAADLFES YAVVLVASLV LGRVAFGTEG
     LVFPLLVPMI GVITAIIGIF VVSPRARDAN AMAAINRGFF ISAVISAVLV VGAALLYLPD
     TFAELEGVPA DIAALDGNPQ LIAIGAVLIG LLLAAAIQLL TGYFTETNRP PVREIGESSR
     SGPATVVLAG VSVGLESAVY SALLIAGAVY AAFLLGGGNI TVSLFAVALA GTGLLTTVGV
     IVAMDTFGPV ADNAQGIAEM SGDVEGSGAE VLNSLDAVGN TTKAITKGIA IATAVLAATA
     LFGAFRTAVE AELGATEFSL SVDQPDVLVG VIIGAAVVFL FSGLAIMAVG RAAGRVVHEV
     REQFRTRPGI MDGTEKPEYG RVVDICTRDS LRELITPGLL AVLTPIALGF ALGYAPLGAF
     LGGGIAAGAL MAVFLANSGG AWDNAKKLVE DGHYGGKGSE AHEATVIGDT IGDPFKDTAG
     PAINPLLKVM NLVALLIAPS VVIYADNLAL RLGITVASVA LLVGVIVWSK RRSTDGSFAA
     EATKTQPEAP AADQGAAKEE PVSQGGGASS QE
//

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