HPPA_STRCO
ID HPPA_STRCO Reviewed; 794 AA.
AC Q9X913;
DT 25-JUL-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1999, sequence version 1.
DT 03-AUG-2022, entry version 109.
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:19628678};
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=SCO3547;
GN ORFNames=SCH5.10c;
OS Streptomyces coelicolor (strain ATCC BAA-471 / A3(2) / M145).
OC Bacteria; Actinobacteria; Streptomycetales; Streptomycetaceae;
OC Streptomyces; Streptomyces albidoflavus group.
OX NCBI_TaxID=100226;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-471 / A3(2) / M145;
RX PubMed=12000953; DOI=10.1038/417141a;
RA Bentley S.D., Chater K.F., Cerdeno-Tarraga A.-M., Challis G.L.,
RA Thomson N.R., James K.D., Harris D.E., Quail M.A., Kieser H., Harper D.,
RA Bateman A., Brown S., Chandra G., Chen C.W., Collins M., Cronin A.,
RA Fraser A., Goble A., Hidalgo J., Hornsby T., Howarth S., Huang C.-H.,
RA Kieser T., Larke L., Murphy L.D., Oliver K., O'Neil S., Rabbinowitsch E.,
RA Rajandream M.A., Rutherford K.M., Rutter S., Seeger K., Saunders D.,
RA Sharp S., Squares R., Squares S., Taylor K., Warren T., Wietzorrek A.,
RA Woodward J.R., Barrell B.G., Parkhill J., Hopwood D.A.;
RT "Complete genome sequence of the model actinomycete Streptomyces coelicolor
RT A3(2).";
RL Nature 417:141-147(2002).
RN [2]
RP FUNCTION, CATALYTIC ACTIVITY, AND MUTAGENESIS OF PHE-388 AND ALA-514.
RC STRAIN=A3(2) / NRRL B-16638;
RX PubMed=19628678; DOI=10.1093/jb/mvp114;
RA Hirono M., Maeshima M.;
RT "Functional enhancement by single-residue substitution of Streptomyces
RT coelicolor A3(2) H+-translocating pyrophosphatase.";
RL J. Biochem. 146:617-621(2009).
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, ECO:0000269|PubMed:19628678}.
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:19628678};
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; AL939117; CAB38484.1; -; Genomic_DNA.
DR PIR; T36668; T36668.
DR RefSeq; NP_627745.1; NC_003888.3.
DR RefSeq; WP_011029076.1; NZ_VNID01000003.1.
DR AlphaFoldDB; Q9X913; -.
DR SMR; Q9X913; -.
DR STRING; 100226.SCO3547; -.
DR GeneID; 1098983; -.
DR KEGG; sco:SCO3547; -.
DR PATRIC; fig|100226.15.peg.3603; -.
DR eggNOG; COG3808; Bacteria.
DR HOGENOM; CLU_008743_3_1_11; -.
DR InParanoid; Q9X913; -.
DR OMA; MATTAMQ; -.
DR PhylomeDB; Q9X913; -.
DR BRENDA; 7.1.3.1; 5998.
DR Proteomes; UP000001973; 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..794
FT /note="K(+)-insensitive pyrophosphate-energized proton
FT pump"
FT /id="PRO_0000217032"
FT TRANSMEM 20..40
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01129"
FT TRANSMEM 74..94
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01129"
FT TRANSMEM 102..122
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01129"
FT TRANSMEM 163..183
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01129"
FT TRANSMEM 194..214
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01129"
FT TRANSMEM 264..284
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01129"
FT TRANSMEM 285..305
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01129"
FT TRANSMEM 321..341
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01129"
FT TRANSMEM 365..385
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01129"
FT TRANSMEM 422..442
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01129"
FT TRANSMEM 446..466
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 564..584
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01129"
FT TRANSMEM 641..661
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01129"
FT TRANSMEM 717..737
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01129"
FT TRANSMEM 747..767
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01129"
FT BINDING 215
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 218
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 222
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 245
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 248
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 476
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 678
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250"
FT BINDING 704
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250"
FT BINDING 708
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250"
FT BINDING 711
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT SITE 207
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 259
FT /note="Important for ion transport"
FT /evidence="ECO:0000250"
FT SITE 507
FT /note="Determinant of potassium independence"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01129"
FT SITE 712
FT /note="Important for ion transport"
FT /evidence="ECO:0000250"
FT SITE 723
FT /note="Important for ion transport"
FT /evidence="ECO:0000250"
FT MUTAGEN 388
FT /note="F->Y: Increased PPase activity and H(+) pump
FT activity. The coupling ratio is approximately two-fold that
FT of the wild-type."
FT /evidence="ECO:0000269|PubMed:19628678"
FT MUTAGEN 514
FT /note="A->S: Increased PPase activity and H(+) pump
FT activity. The coupling ratio is approximately two-fold that
FT of the wild-type."
FT /evidence="ECO:0000269|PubMed:19628678"
SQ SEQUENCE 794 AA; 80650 MW; 1525557A88198CA8 CRC64;
MAELPTSHLA AAVLTDGNRA LVAVIAVVAL AALVLAGVLV RQVLAAGEGT DSMKKIAAAV
QEGANAYLAR QLRTLGVFAV VVFFLLMLLP ADDWNQRAGR SIFFLIGAAF SAATGYIGMW
LAVRSNVRVA AAAREATPAP GEPEKDLALV SHKATKIAFR TGGVVGMFTV GLGLLGACCV
VLVYAADAPK VLEGFGLGAA LIAMFMRVGG GIFTKAADVG ADLVGKVEQG IPEDDPRNAA
TIADNVGDNV GDCAGMAADL FESYAVTLVA ALILGKVAFG DFGLAFPLLV PAIGVLTAMI
GIFAVAPRRS DRSGMSAINR GFFISAVISL VLVAVAVFVY LPGKYADLDG VTDAAIAGKS
GDPRILALVA VAIGIVLAAL IQQLTGYFTE TTRRPVKDIG KSSLTGPATV VLAGISLGLE
SAVYTALLIG LGVYGAFLLG GTSIMLALFA VALAGTGLLT TVGVIVAMDT FGPVSDNAQG
IAEMSGDVEG AGAQVLTDLD AVGNTTKAIT KGIAIATAVL AAAALFGSYR DAITTGAADV
GEKLSGEGAP MTLMMDISQP NNLVGLIAGA AVVFLFSGLA INAVSRSAGA VVYEVRRQFR
ERPGIMDYSE KPEYGKVVDI CTRDALRELA TPGLLAVMAP IFIGFTLGVG ALGAFLAGAI
GAGTLMAVFL ANSGGSWDNA KKLVEDGHHG GKGSEAHAAT VIGDTVGDPF KDTAGPAINP
LLKVMNLVAL LIAPAVIKFS YGADKSVVVR VLIAVVAFAV IAAAVYVSKR RGIAMGDEDD
ADPEPKSADP AVVS
