HPPA_AGRFC
ID HPPA_AGRFC Reviewed; 714 AA.
AC Q8UG67; Q8VPZ1; Q93AR6; Q93AR7;
DT 25-JUL-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2002, sequence version 1.
DT 03-AUG-2022, entry version 119.
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};
DE Flags: Precursor;
GN Name=hppA {ECO:0000255|HAMAP-Rule:MF_01129}; Synonyms=vppA;
GN OrderedLocusNames=Atu1174; ORFNames=AGR_C_2169;
OS Agrobacterium fabrum (strain C58 / ATCC 33970) (Agrobacterium tumefaciens
OS (strain C58)).
OC Bacteria; Proteobacteria; Alphaproteobacteria; Hyphomicrobiales;
OC Rhizobiaceae; Rhizobium/Agrobacterium group; Agrobacterium;
OC Agrobacterium tumefaciens complex.
OX NCBI_TaxID=176299;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C58 / ATCC 33970;
RX PubMed=11743193; DOI=10.1126/science.1066804;
RA Wood D.W., Setubal J.C., Kaul R., Monks D.E., Kitajima J.P., Okura V.K.,
RA Zhou Y., Chen L., Wood G.E., Almeida N.F. Jr., Woo L., Chen Y.,
RA Paulsen I.T., Eisen J.A., Karp P.D., Bovee D. Sr., Chapman P.,
RA Clendenning J., Deatherage G., Gillet W., Grant C., Kutyavin T., Levy R.,
RA Li M.-J., McClelland E., Palmieri A., Raymond C., Rouse G.,
RA Saenphimmachak C., Wu Z., Romero P., Gordon D., Zhang S., Yoo H., Tao Y.,
RA Biddle P., Jung M., Krespan W., Perry M., Gordon-Kamm B., Liao L., Kim S.,
RA Hendrick C., Zhao Z.-Y., Dolan M., Chumley F., Tingey S.V., Tomb J.-F.,
RA Gordon M.P., Olson M.V., Nester E.W.;
RT "The genome of the natural genetic engineer Agrobacterium tumefaciens
RT C58.";
RL Science 294:2317-2323(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C58 / ATCC 33970;
RX PubMed=11743194; DOI=10.1126/science.1066803;
RA Goodner B., Hinkle G., Gattung S., Miller N., Blanchard M., Qurollo B.,
RA Goldman B.S., Cao Y., Askenazi M., Halling C., Mullin L., Houmiel K.,
RA Gordon J., Vaudin M., Iartchouk O., Epp A., Liu F., Wollam C., Allinger M.,
RA Doughty D., Scott C., Lappas C., Markelz B., Flanagan C., Crowell C.,
RA Gurson J., Lomo C., Sear C., Strub G., Cielo C., Slater S.;
RT "Genome sequence of the plant pathogen and biotechnology agent
RT Agrobacterium tumefaciens C58.";
RL Science 294:2323-2328(2001).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 248-454 AND 480-700.
RA Jumas-Bilak E., Michaux-Charachon S., Teyssier C., Ramuz M.;
RT "High prevalence of the H+-proton-pumping pyrophosphatase gene in alpha
RT proteobacteria and evidence of lateral transfer during its phylogeny.";
RL Submitted (SEP-2001) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 441-644.
RA Perez-Castineira J.R., Losada M., Serrano A.;
RT "Presence of proton-translocating pyrophosphatase genes in root nodule-
RT making bacteria (Rhizobia) and pathogenic tumour-making bacteria
RT (Agrobacterium).";
RL Submitted (DEC-1999) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP CHARACTERIZATION, AND SUBCELLULAR LOCATION.
RX PubMed=12783865; DOI=10.1074/jbc.m304548200;
RA Seufferheld M., Vieira M.C.F., Ruiz F.A., Rodrigues C.O., Moreno S.N.J.,
RA Docampo R.;
RT "Identification of organelles in bacteria similar to acidocalcisomes of
RT unicellular eukaryotes.";
RL J. Biol. Chem. 278:29971-29978(2003).
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: Acidocalcisome membrane
CC {ECO:0000269|PubMed:12783865}; Multi-pass membrane protein
CC {ECO:0000255|HAMAP-Rule:MF_01129, ECO:0000269|PubMed:12783865}.
CC -!- SIMILARITY: Belongs to the H(+)-translocating pyrophosphatase (TC
CC 3.A.10) family. K(+)-insensitive subfamily. {ECO:0000255|HAMAP-
CC Rule:MF_01129}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAK86977.2; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AE007869; AAK86977.2; ALT_INIT; Genomic_DNA.
DR EMBL; AF417520; AAL14977.1; -; Genomic_DNA.
DR EMBL; AF417521; AAL14978.1; -; Genomic_DNA.
DR EMBL; AJ251784; CAC80978.1; -; Genomic_DNA.
DR PIR; AD2721; AD2721.
DR PIR; H97502; H97502.
DR RefSeq; NP_354192.2; NC_003062.2.
DR AlphaFoldDB; Q8UG67; -.
DR SMR; Q8UG67; -.
DR STRING; 176299.Atu1174; -.
DR EnsemblBacteria; AAK86977; AAK86977; Atu1174.
DR KEGG; atu:Atu1174; -.
DR PATRIC; fig|176299.10.peg.1194; -.
DR eggNOG; COG3808; Bacteria.
DR HOGENOM; CLU_008743_3_1_5; -.
DR OMA; MATTAMQ; -.
DR Proteomes; UP000000813; Chromosome circular.
DR GO; GO:0033102; C:acidocalcisome membrane; IEA:UniProtKB-SubCell.
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; Hydrogen ion transport; Ion transport; Magnesium; Membrane;
KW Metal-binding; Reference proteome; Signal; Translocase; Transmembrane;
KW Transmembrane helix; Transport.
FT SIGNAL 1..20
FT /evidence="ECO:0000255"
FT CHAIN 21..714
FT /note="K(+)-insensitive pyrophosphate-energized proton
FT pump"
FT /id="PRO_0000013525"
FT TRANSMEM 52..74
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01129"
FT TRANSMEM 85..105
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01129"
FT TRANSMEM 128..148
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01129"
FT TRANSMEM 166..186
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01129"
FT TRANSMEM 238..258
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01129"
FT TRANSMEM 263..283
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01129"
FT TRANSMEM 298..318
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01129"
FT TRANSMEM 333..353
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01129"
FT TRANSMEM 383..403
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01129"
FT TRANSMEM 411..431
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01129"
FT TRANSMEM 470..490
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01129"
FT TRANSMEM 522..542
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01129"
FT TRANSMEM 591..611
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01129"
FT TRANSMEM 618..638
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01129"
FT TRANSMEM 693..713
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01129"
FT BINDING 188
FT /ligand="substrate"
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 195
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 218
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
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 439
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 680
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250"
FT BINDING 684
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250"
FT BINDING 687
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT SITE 180
FT /note="Important for ion transport"
FT /evidence="ECO:0000250"
FT SITE 225
FT /note="Important for ion transport"
FT /evidence="ECO:0000250"
FT SITE 232
FT /note="Important for ion transport"
FT /evidence="ECO:0000250"
FT SITE 469
FT /note="Determinant of potassium independence"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01129"
FT SITE 688
FT /note="Important for ion transport"
FT /evidence="ECO:0000250"
FT SITE 699
FT /note="Important for ion transport"
FT /evidence="ECO:0000250"
FT CONFLICT 385
FT /note="A -> T (in Ref. 3; AAL14977)"
FT /evidence="ECO:0000305"
FT CONFLICT 409
FT /note="G -> A (in Ref. 3; AAL14977)"
FT /evidence="ECO:0000305"
FT CONFLICT 450..452
FT /note="LDP -> VDR (in Ref. 3; AAL14977)"
FT /evidence="ECO:0000305"
FT CONFLICT 639..640
FT /note="SM -> PC (in Ref. 4; CAC80978)"
FT /evidence="ECO:0000305"
FT CONFLICT 697..700
FT /note="AIKI -> GHQD (in Ref. 3; AAL14978)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 714 AA; 72792 MW; 41C8F6721FBE19CD CRC64;
MRMTVIPIVI LCGVLSVVYA VWTTKSVLDA DQGNERMREI AGYIREGAQA YLTRQYLTIA
IVGLIVAVLA WYLLSAIAAI GFVIGAVLSG VAGFVGMHVS VRANLRTAQA ASHSLGAGLD
IAFKSGAITG MLVAGLALLG VSIYYFVLTS VLGHPPGSRA VIDALVSLGF GASLISIFAR
LGGGIFTKGA DVGGDLVGKV EAGIPEDDPR NPATIADNVG DNVGDCAGMA ADLFETYAVS
VVATMVLAAI FFAGTPILES AMVYPLAICG ACILTSIAGT FFVKLGTNNS IMGALYKGLI
ATGVFSVAGL AVATYATVGW GTIGTVAGME ITGTNLFFCG LVGLVVTALI VVITEYYTGT
NKRPVNSIAQ ASVTGHGTNV IQGLAVSLES TALPAIVIVG GIIGTYQLGG LFGTGIAVTA
MLGLAGMIVA LDAFGPVTDN AGGIAEMAGL DPDVRKATDA LDAVGNTTKA VTKGYAIGSA
GLGALVLFAA YANDLSYFAA NGDTYPYFKD IGEISFSLAN PYVVAGLLFG GLIPYLFGGI
AMTAVGKAAS AIVEEVRRQF REKPGIMAGT EKPDYGRAVD LLTKAAIREM VIPSLLPVLA
PLVVYFGVLL ISGSKASAFA ALGASLLGVI INGLFVAISM TSGGGAWDNA KKSFEDGFID
KDGVRHVKGS EAHKASVTGD TVGDPYKDTA GPAVNPAIKI TNIVALLLLA VLAH