ID   HTXD_PSEST              Reviewed;         341 AA.
AC   O69063;
DT   01-MAR-2005, integrated into UniProtKB/Swiss-Prot.
DT   01-AUG-1998, sequence version 1.
DT   03-AUG-2022, entry version 90.
DE   RecName: Full=Hypophosphite import ATP-binding protein HtxD;
DE            EC=7.6.2.-;
GN   Name=htxD;
OS   Pseudomonas stutzeri (Pseudomonas perfectomarina).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC   Pseudomonadaceae; Pseudomonas.
OX   NCBI_TaxID=316;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND FUNCTION.
RC   STRAIN=WM88;
RX   PubMed=9791102; DOI=10.1128/jb.180.21.5547-5558.1998;
RA   Metcalf W.W., Wolfe R.S.;
RT   "Molecular genetic analysis of phosphite and hypophosphite oxidation by
RT   Pseudomonas stutzeri WM88.";
RL   J. Bacteriol. 180:5547-5558(1998).
RN   [2]
RP   FUNCTION.
RC   STRAIN=WM88;
RX   PubMed=15231805; DOI=10.1128/jb.186.14.4730-4739.2004;
RA   White A.K., Metcalf W.W.;
RT   "Two C-P lyase operons in Pseudomonas stutzeri and their roles in the
RT   oxidation of phosphonates, phosphite, and hypophosphite.";
RL   J. Bacteriol. 186:4730-4739(2004).
CC   -!- FUNCTION: Part of the ABC transporter complex HtxBCDE involved in
CC       hypophosphite import. Responsible for energy coupling to the transport
CC       system (Probable). {ECO:0000305|PubMed:15231805,
CC       ECO:0000305|PubMed:9791102}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + H2O + phosphinate(out) = ADP + H(+) + phosphate +
CC         phosphinate(in); Xref=Rhea:RHEA:48512, ChEBI:CHEBI:15377,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:29198, ChEBI:CHEBI:30616,
CC         ChEBI:CHEBI:43474, ChEBI:CHEBI:456216;
CC   -!- SUBUNIT: The complex is composed of two ATP-binding proteins (HtxD),
CC       two transmembrane proteins (HtxC and HtxE) and a solute-binding protein
CC       (HtxB). {ECO:0000305}.
CC   -!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000250}; Peripheral
CC       membrane protein {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the ABC transporter superfamily. Phosphonates
CC       importer (TC 3.A.1.9.1) family. {ECO:0000305}.
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DR   EMBL; AF061267; AAC71714.1; -; Genomic_DNA.
DR   AlphaFoldDB; O69063; -.
DR   SMR; O69063; -.
DR   TCDB; 3.A.1.9.4; the atp-binding cassette (abc) superfamily.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0015416; F:ABC-type phosphonate transporter activity; IEA:InterPro.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   CDD; cd03256; ABC_PhnC_transporter; 1.
DR   Gene3D; 3.40.50.300; -; 1.
DR   InterPro; IPR003593; AAA+_ATPase.
DR   InterPro; IPR003439; ABC_transporter-like_ATP-bd.
DR   InterPro; IPR017871; ABC_transporter-like_CS.
DR   InterPro; IPR012693; ABC_transpr_PhnC.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   Pfam; PF00005; ABC_tran; 1.
DR   SMART; SM00382; AAA; 1.
DR   SUPFAM; SSF52540; SSF52540; 1.
DR   TIGRFAMs; TIGR02315; ABC_phnC; 1.
DR   PROSITE; PS00211; ABC_TRANSPORTER_1; 1.
DR   PROSITE; PS50893; ABC_TRANSPORTER_2; 1.
DR   PROSITE; PS51249; PHNC; 1.
PE   3: Inferred from homology;
KW   ATP-binding; Cell inner membrane; Cell membrane; Membrane;
KW   Nucleotide-binding; Translocase; Transport.
FT   CHAIN           1..341
FT                   /note="Hypophosphite import ATP-binding protein HtxD"
FT                   /id="PRO_0000092393"
FT   DOMAIN          6..249
FT                   /note="ABC transporter"
FT   REGION          278..341
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        310..333
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         38..45
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   341 AA;  37310 MW;  825B00A913542773 CRC64;
     MKDVALQLKN VGKSYGNKVV LESIDFEVRH GSMVALLGTS GAGKSTLFRC LTGLEPIDSG
     SIVALGESIH ELSPARLRAV RGQIGFVFQQ LHLVKRFSAL ENVLGARLAE MPIWRVTLKS
     FSRADKVLAF ECLDRVGMLD YANTPTQLLS GGQQQRIAIA RALAQKPKII IADEPVSSLD
     PLTARSVLQT LKAAATDLNV AVLCSLHQVD LAREFGDRIV GMRDGRVVFD GTPAEFTDER
     VHALYQVPAG KMHQRPRATR STRWPVWLWH EGRSDDHIHT PHTRAAPGHR TALAPERALQ
     RQTSAGADRR HGAVVRDRTT HRNGPHGGHD GTGRGQDRGP G