ID   PHNC_ANADE              Reviewed;         498 AA.
AC   Q2IN45;
DT   06-FEB-2007, integrated into UniProtKB/Swiss-Prot.
DT   07-MAR-2006, sequence version 1.
DT   03-AUG-2022, entry version 100.
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=Adeh_0455;
OS   Anaeromyxobacter dehalogenans (strain 2CP-C).
OC   Bacteria; Proteobacteria; Deltaproteobacteria; Myxococcales;
OC   Cystobacterineae; Anaeromyxobacteraceae; Anaeromyxobacter.
OX   NCBI_TaxID=290397;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=2CP-C;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina T.,
RA   Hammon N., Israni S., Pitluck S., Brettin T., Bruce D., Han C., Tapia R.,
RA   Gilna P., Kiss H., Schmutz J., Larimer F., Land M., Kyrpides N.,
RA   Anderson I., Sanford R.A., Ritalahti K.M., Thomas H.S., Kirby J.R.,
RA   Zhulin I.B., Loeffler F.E., Richardson P.;
RT   "Complete sequence of Anaeromyxobacter dehalogenans 2CP-C.";
RL   Submitted (JAN-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}.
CC   -!- CAUTION: The fusion between the ATP-binding domain and LysR substrate
CC       binding domain is unusual. It could be due to a sequencing error.
CC       {ECO:0000305}.
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DR   EMBL; CP000251; ABC80231.1; -; Genomic_DNA.
DR   RefSeq; WP_011419514.1; NC_007760.1.
DR   AlphaFoldDB; Q2IN45; -.
DR   SMR; Q2IN45; -.
DR   STRING; 290397.Adeh_0455; -.
DR   PRIDE; Q2IN45; -.
DR   EnsemblBacteria; ABC80231; ABC80231; Adeh_0455.
DR   KEGG; ade:Adeh_0455; -.
DR   eggNOG; COG0226; Bacteria.
DR   eggNOG; COG3638; Bacteria.
DR   HOGENOM; CLU_041390_0_0_7; -.
DR   OMA; SIPRHVF; -.
DR   Proteomes; UP000001935; 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; IPR005119; LysR_subst-bd.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   Pfam; PF00005; ABC_tran; 1.
DR   Pfam; PF03466; LysR_substrate; 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..498
FT                   /note="Phosphonates import ATP-binding protein PhnC"
FT                   /id="PRO_0000274705"
FT   DOMAIN          28..269
FT                   /note="ABC transporter"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01713"
FT   REGION          1..27
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          270..498
FT                   /note="LysR substrate binding domain"
FT   BINDING         60..67
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01713"
SQ   SEQUENCE   498 AA;  52019 MW;  8350FF341618CE9C CRC64;
     MPQRPEAARA GPVAGPDAAS KPAPGPALTL RGAGRAYGPV RALRPLTLEI RRGERVALLG
     PSGAGKSTLL RLLDTSLAPS EGTVEVLGQP VADTDARRLR ALRARIGTVH QQLLLVPQAT
     AMQNVVAGRL GRTSLARTLA ALVSRREAAR VRAVLDEVGI GDKIFERVDR LSGGEQQRVA
     IARTLYQDPE LILADEPLAS VDPARAADIA ALLARAFAGR TLVVSTHRIE PLLAHVDRVV
     ALREGALAFD KPAAALTLRD LGELYEARRG AADPARAPAA RPPSDPVVAP GGTLRIGASS
     TPGEHLLPSI VRAFARAYPG TRVSLSLSDS AAVTAAVRDG ALDLGFVGAR DDDPALAYED
     VARDEIVLVA APVLELPPEP ITLEVAARLP RVDREPGSGT RAVVEQHLAN MGAALDPAAV
     VLEAGALVAL KAAVVSGMGV AFVSRRAVED DLRGGHVRTV RVEGLSIPRH VFAVLRRSPV
     PSAAARAFLE VARAEVPP