ID   PHNC2_ALBFT             Reviewed;         277 AA.
AC   Q21Y06;
DT   06-FEB-2007, integrated into UniProtKB/Swiss-Prot.
DT   18-APR-2006, sequence version 1.
DT   03-AUG-2022, entry version 99.
DE   RecName: Full=Phosphonates import ATP-binding protein PhnC 2 {ECO:0000255|HAMAP-Rule:MF_01713};
DE            EC=7.3.2.2 {ECO:0000255|HAMAP-Rule:MF_01713};
GN   Name=phnC2 {ECO:0000255|HAMAP-Rule:MF_01713}; OrderedLocusNames=Rfer_1616;
OS   Albidiferax ferrireducens (strain ATCC BAA-621 / DSM 15236 / T118)
OS   (Rhodoferax ferrireducens).
OC   Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC   Comamonadaceae; Rhodoferax.
OX   NCBI_TaxID=338969;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-621 / DSM 15236 / T118;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA   Glavina del Rio T., Hammon N., Israni S., Pitluck S., Brettin T., Bruce D.,
RA   Han C., Tapia R., Gilna P., Kiss H., Schmutz J., Larimer F., Land M.,
RA   Kyrpides N., Ivanova N., Richardson P.;
RT   "Complete sequence of chromosome of Rhodoferax ferrireducens DSM 15236.";
RL   Submitted (FEB-2006) to the EMBL/GenBank/DDBJ databases.
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; CP000267; ABD69347.1; -; Genomic_DNA.
DR   RefSeq; WP_011463915.1; NC_007908.1.
DR   AlphaFoldDB; Q21Y06; -.
DR   SMR; Q21Y06; -.
DR   STRING; 338969.Rfer_1616; -.
DR   EnsemblBacteria; ABD69347; ABD69347; Rfer_1616.
DR   KEGG; rfr:Rfer_1616; -.
DR   eggNOG; COG3638; Bacteria.
DR   HOGENOM; CLU_000604_1_22_4; -.
DR   OMA; IGTLWQD; -.
DR   OrthoDB; 1181903at2; -.
DR   Proteomes; UP000008332; 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   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; IPR027417; P-loop_NTPase.
DR   Pfam; PF00005; ABC_tran; 1.
DR   SMART; SM00382; AAA; 1.
DR   SUPFAM; SSF52540; SSF52540; 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..277
FT                   /note="Phosphonates import ATP-binding protein PhnC 2"
FT                   /id="PRO_0000274740"
FT   DOMAIN          3..251
FT                   /note="ABC transporter"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01713"
FT   BINDING         40..47
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01713"
SQ   SEQUENCE   277 AA;  29679 MW;  A59633F7D7A0A569 CRC64;
     MKISLNGISV QHPSAKPGAV PALREQNLTV RAGEQLAIIG PSGAGKTTLL HLLACALKPS
     AGSMLLNDQD PWQLSRGALQ KLRGALFLAP QVPPLPPRQR VVTAVLAGRL PNESLWASLR
     SLFYPTDIAL AERALAGFDV GDKLFDRVDR LSGGERQRVG LARALVSQAS LILVDEPLSA
     LDPTRSQHAI ETLTRAAQER GATLVATLHH VEMALAHFPR IVGLRDGQVA FDLPAAEVTP
     ELLQALYAQH LHELTGLANL EADDLPTDPA PVVMHCR