ID   PHNC_BURP1              Reviewed;         307 AA.
AC   Q3JNY2;
DT   06-FEB-2007, integrated into UniProtKB/Swiss-Prot.
DT   08-NOV-2005, sequence version 1.
DT   03-AUG-2022, entry version 105.
DE   RecName: Full=Phosphonates import ATP-binding protein PhnC {ECO:0000255|HAMAP-Rule:MF_01713};
DE            EC=7.3.2.2 {ECO:0000255|HAMAP-Rule:MF_01713};
GN   Name=phnC {ECO:0000255|HAMAP-Rule:MF_01713};
GN   OrderedLocusNames=BURPS1710b_3350;
OS   Burkholderia pseudomallei (strain 1710b).
OC   Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC   Burkholderiaceae; Burkholderia; pseudomallei group.
OX   NCBI_TaxID=320372;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=1710b;
RX   PubMed=20333227; DOI=10.1093/gbe/evq003;
RA   Losada L., Ronning C.M., DeShazer D., Woods D., Fedorova N., Kim H.S.,
RA   Shabalina S.A., Pearson T.R., Brinkac L., Tan P., Nandi T., Crabtree J.,
RA   Badger J., Beckstrom-Sternberg S., Saqib M., Schutzer S.E., Keim P.,
RA   Nierman W.C.;
RT   "Continuing evolution of Burkholderia mallei through genome reduction and
RT   large-scale rearrangements.";
RL   Genome Biol. Evol. 2:102-116(2010).
CC   -!- FUNCTION: Part of the ABC transporter complex PhnCDE involved in
CC       phosphonates import. Responsible for energy coupling to the transport
CC       system. {ECO:0000255|HAMAP-Rule:MF_01713}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + H2O + phosphonate(out) = ADP + H(+) + phosphate +
CC         phosphonate(in); Xref=Rhea:RHEA:18065, ChEBI:CHEBI:15377,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:16215, ChEBI:CHEBI:30616,
CC         ChEBI:CHEBI:43474, ChEBI:CHEBI:456216; EC=7.3.2.2;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_01713};
CC   -!- SUBUNIT: The complex is composed of two ATP-binding proteins (PhnC),
CC       two transmembrane proteins (PhnE) and a solute-binding protein (PhnD).
CC       {ECO:0000255|HAMAP-Rule:MF_01713}.
CC   -!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000255|HAMAP-
CC       Rule:MF_01713}; Peripheral membrane protein {ECO:0000255|HAMAP-
CC       Rule:MF_01713}.
CC   -!- SIMILARITY: Belongs to the ABC transporter superfamily. Phosphonates
CC       importer (TC 3.A.1.9.1) family. {ECO:0000255|HAMAP-Rule:MF_01713}.
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DR   EMBL; CP000124; ABA48695.1; -; Genomic_DNA.
DR   RefSeq; WP_004527694.1; NC_007434.1.
DR   AlphaFoldDB; Q3JNY2; -.
DR   SMR; Q3JNY2; -.
DR   EnsemblBacteria; ABA48695; ABA48695; BURPS1710b_3350.
DR   GeneID; 56528348; -.
DR   KEGG; bpm:BURPS1710b_3350; -.
DR   HOGENOM; CLU_000604_1_22_4; -.
DR   OMA; GRMPRWR; -.
DR   OrthoDB; 1181903at2; -.
DR   Proteomes; UP000002700; Chromosome I.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0015416; F:ABC-type phosphonate transporter activity; IEA:UniProtKB-EC.
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; Phosphonate transport; Translocase; Transport.
FT   CHAIN           1..307
FT                   /note="Phosphonates import ATP-binding protein PhnC"
FT                   /id="PRO_0000274706"
FT   DOMAIN          4..252
FT                   /note="ABC transporter"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01713"
FT   REGION          265..307
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         37..44
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01713"
SQ   SEQUENCE   307 AA;  33386 MW;  19598DA6C3BF0EBE CRC64;
     MDAIRIERLS KTFPNGRKGL EDIDLAIAPG EMVALIGASG SGKSTLLRQI ASFSSSDARP
     SRIDIFGRSI QRDGRIARDV RRMRRDIGFV FQQFNLVDRL SVETNVLIGA LARVPMWRRL
     AGRFSRADRA LAAQALGEVG IAEHARERAA NLSGGQQQRA ALARALVQRA RIILADEPIA
     SLDPAASRRV MEMLRALNAN HRLTVLVSLH QIDVALRFCP RVVALRAGRI VYDGPSAALT
     RERLHALYGD DAHLPFAVGD EVRPAAREAA GEPARRAPAA FDSAGSPDLP DSQPASPRRM
     LAASSMR