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HPPA_CHLAA
ID   HPPA_CHLAA              Reviewed;         775 AA.
AC   Q8VNW3; A9W9P8;
DT   25-JUL-2003, integrated into UniProtKB/Swiss-Prot.
DT   18-MAR-2008, sequence version 2.
DT   03-AUG-2022, entry version 99.
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=vppA;
GN   OrderedLocusNames=Caur_1306;
OS   Chloroflexus aurantiacus (strain ATCC 29366 / DSM 635 / J-10-fl).
OC   Bacteria; Chloroflexi; Chloroflexia; Chloroflexales; Chloroflexineae;
OC   Chloroflexaceae; Chloroflexus.
OX   NCBI_TaxID=324602;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 29366 / DSM 635 / J-10-fl;
RX   PubMed=21714912; DOI=10.1186/1471-2164-12-334;
RA   Tang K.H., Barry K., Chertkov O., Dalin E., Han C.S., Hauser L.J.,
RA   Honchak B.M., Karbach L.E., Land M.L., Lapidus A., Larimer F.W.,
RA   Mikhailova N., Pitluck S., Pierson B.K., Blankenship R.E.;
RT   "Complete genome sequence of the filamentous anoxygenic phototrophic
RT   bacterium Chloroflexus aurantiacus.";
RL   BMC Genomics 12:334-334(2011).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 474-673.
RA   Perez-Castineira J.R., Losada M., Serrano A.;
RT   "Evidence for a wide distribution of proton-translocating pyrophosphatases
RT   among photosynthetic organisms.";
RL   Submitted (DEC-1999) 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 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; CP000909; ABY34534.1; -; Genomic_DNA.
DR   EMBL; AJ251370; CAC80905.1; -; Genomic_DNA.
DR   RefSeq; WP_012257190.1; NC_010175.1.
DR   RefSeq; YP_001634923.1; NC_010175.1.
DR   AlphaFoldDB; Q8VNW3; -.
DR   SMR; Q8VNW3; -.
DR   STRING; 324602.Caur_1306; -.
DR   EnsemblBacteria; ABY34534; ABY34534; Caur_1306.
DR   KEGG; cau:Caur_1306; -.
DR   PATRIC; fig|324602.8.peg.1495; -.
DR   eggNOG; COG3808; Bacteria.
DR   HOGENOM; CLU_008743_3_1_0; -.
DR   InParanoid; Q8VNW3; -.
DR   OMA; MATTAMQ; -.
DR   Proteomes; UP000002008; 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 membrane; Hydrogen ion transport; Ion transport; Magnesium;
KW   Membrane; Metal-binding; Reference proteome; Translocase; Transmembrane;
KW   Transmembrane helix; Transport.
FT   CHAIN           1..775
FT                   /note="K(+)-insensitive pyrophosphate-energized proton
FT                   pump"
FT                   /id="PRO_0000217014"
FT   TRANSMEM        9..29
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01129"
FT   TRANSMEM        65..85
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01129"
FT   TRANSMEM        108..128
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01129"
FT   TRANSMEM        160..180
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01129"
FT   TRANSMEM        185..205
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01129"
FT   TRANSMEM        259..279
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01129"
FT   TRANSMEM        288..308
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01129"
FT   TRANSMEM        327..347
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01129"
FT   TRANSMEM        359..379
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        442..462
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01129"
FT   TRANSMEM        508..528
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01129"
FT   TRANSMEM        555..575
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01129"
FT   TRANSMEM        622..642
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01129"
FT   TRANSMEM        644..664
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01129"
FT   TRANSMEM        710..730
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01129"
FT   TRANSMEM        735..755
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01129"
FT   BINDING         208
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         211
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250"
FT   BINDING         215
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250"
FT   BINDING         241
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250"
FT   BINDING         472
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250"
FT   BINDING         671
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /evidence="ECO:0000250"
FT   BINDING         697
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /evidence="ECO:0000250"
FT   BINDING         701
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /evidence="ECO:0000250"
FT   BINDING         704
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   SITE            200
FT                   /note="Important for ion transport"
FT                   /evidence="ECO:0000250"
FT   SITE            245
FT                   /note="Important for ion transport"
FT                   /evidence="ECO:0000250"
FT   SITE            252
FT                   /note="Important for ion transport"
FT                   /evidence="ECO:0000250"
FT   SITE            502
FT                   /note="Determinant of potassium independence"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01129"
FT   SITE            705
FT                   /note="Important for ion transport"
FT                   /evidence="ECO:0000250"
FT   SITE            716
FT                   /note="Important for ion transport"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   775 AA;  80486 MW;  509F7B985C75D931 CRC64;
     MQDLNAVQSL AVWAVLVISL LGIGYAFFIR SQILAQDTGT PKMREVWGFI KTGANAYLSQ
     QFRTISILIV ILTFVLAASV FIIPPTTEAV ERFGSKEAAT IWVAIGRAVA FLMGSLFSYA
     VGFVGMNVAV EGNVRVAAAA RKGYNPALQV AYKSGSVTGM LTVGLGLLGG TLIFMVFGIA
     APDALLGFGF GGSLIALFMR VGGGIYTKAA DVGADLVGKV EAGIPEDDPR NAAVIADLVG
     DNVGDCAGMA ADVFESFEVT LVSALILGLV LGDAVVGTIG DGAYDLRFII FPLVLRAIGV
     VASVIGNLFV TTDERKRNAM AAMNRGFYIA AGLAIAASAA ATPVFMVNEA TGEVDWRPFF
     ATLSGVVLAI VLDKLTEYFT STHFSPVKET SKASQTGSAT NILSGLALGM ESSVWAILVI
     SASIFTSVLI YAGEPAATQF TAILYGVSLT GIGMLLLTGN TISMDSFGPI SDNANGIGEM
     AGLDKNARNV MDDLDAVGNT TKAVTKGIAI GSAVIAAVAL YGSYFTDVNK VLQQMINEGR
     QGIELLASIN VAAPPVFIGL LIGGAVPFLF SALTIRAVSR AAAQIVNEVR RQFRIPGLME
     GKVQPDYARA VQISTTAAQK ELISLGLIAV MVPIIVGFTL GVEALGGFLA GIILTGQLMA
     VFQANAGGAW DNAKKYIEEG NFGGKHSEPH KAAVVGDTVG DPLKDTAGPA LNPMIKVINL
     VALIIAPIVV TIEPGSPGVI IAMIICGAAL VWAIWQSKRE SEALKEIAQA PASAD
 
 
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