ID   PHNC_BDEBA              Reviewed;         261 AA.
AC   Q6MIP7;
DT   01-MAR-2005, integrated into UniProtKB/Swiss-Prot.
DT   05-JUL-2004, sequence version 1.
DT   03-AUG-2022, entry version 109.
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}; OrderedLocusNames=Bd3104;
OS   Bdellovibrio bacteriovorus (strain ATCC 15356 / DSM 50701 / NCIMB 9529 /
OS   HD100).
OC   Bacteria; Proteobacteria; Oligoflexia; Bdellovibrionales;
OC   Bdellovibrionaceae; Bdellovibrio.
OX   NCBI_TaxID=264462;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 15356 / DSM 50701 / NCIMB 9529 / HD100;
RX   PubMed=14752164; DOI=10.1126/science.1093027;
RA   Rendulic S., Jagtap P., Rosinus A., Eppinger M., Baar C., Lanz C.,
RA   Keller H., Lambert C., Evans K.J., Goesmann A., Meyer F., Sockett R.E.,
RA   Schuster S.C.;
RT   "A predator unmasked: life cycle of Bdellovibrio bacteriovorus from a
RT   genomic perspective.";
RL   Science 303:689-692(2004).
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; BX842654; CAE80866.1; -; Genomic_DNA.
DR   RefSeq; WP_011165470.1; NC_005363.1.
DR   AlphaFoldDB; Q6MIP7; -.
DR   SMR; Q6MIP7; -.
DR   STRING; 264462.Bd3104; -.
DR   EnsemblBacteria; CAE80866; CAE80866; Bd3104.
DR   KEGG; bba:Bd3104; -.
DR   eggNOG; COG3638; Bacteria.
DR   HOGENOM; CLU_000604_1_22_7; -.
DR   OMA; VFQRPFV; -.
DR   OrthoDB; 1181903at2; -.
DR   Proteomes; UP000008080; Chromosome.
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; Reference proteome; Translocase;
KW   Transport.
FT   CHAIN           1..261
FT                   /note="Phosphonates import ATP-binding protein PhnC"
FT                   /id="PRO_0000092697"
FT   DOMAIN          8..253
FT                   /note="ABC transporter"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01713"
FT   BINDING         41..48
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01713"
SQ   SEQUENCE   261 AA;  29197 MW;  52B898AC7263E1FF CRC64;
     MIVSEPLLRV ENLSKTYPNG VQALKNINLE VHPGEFLVVI GLSGSGKSTL LRCLNRLQEP
     TSGNIYFSGQ EIGQVQDAEK IRSVRSKMAM IFQHFNLIPR QSVLKNVLMG RLAAKSTWQS
     LWGMFSDAER IEAKENLRLV GIAEKASLRA DQLSGGQKQR VAIARALMQK PVLLLADEPV
     SSLDPATCHV VMDYLRRINQ EMGITVIANL HFLSLVRKYA TRVVALKDGE IVFRGKPEEI
     TEEWFRRIYG EGAQDVAPND I