PHNC_PSEST
ID PHNC_PSEST Reviewed; 276 AA.
AC Q6RCE0;
DT 01-MAR-2005, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 77.
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};
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=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 PhnCDE involved in
CC phosphonates import. Responsible for energy coupling to the transport
CC system (Probable). {ECO:0000305|PubMed:15231805}.
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; AY505177; AAR91731.1; -; Genomic_DNA.
DR RefSeq; WP_014818580.1; NZ_PJJZ01000007.1.
DR AlphaFoldDB; Q6RCE0; -.
DR SMR; Q6RCE0; -.
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..276
FT /note="Phosphonates import ATP-binding protein PhnC"
FT /id="PRO_0000092723"
FT DOMAIN 5..253
FT /note="ABC transporter"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01713"
FT BINDING 37..44
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01713"
SQ SEQUENCE 276 AA; 29961 MW; 1BBE5E8B2EEF1DCF CRC64;
MNAAIRVERL NKTFAGKQAL FDLGLAIQPG EMVALIGASG SGKSTLLRHL AGLACCDRSA
GGRIEVLGRE VQATGRLHGE VRRLRADIGY IFQQFNLVTR LSVLDNVLLG FLGRMPRWRG
SLGMFSDEQK RQAMAALERV GLAERAAQRA STLSGGQQQR VAIARALTQQ AEVILADEPI
ASLDPESARK VMEILADINR QDGKTVVVTL HQVDYALRYC SRAVALKGGR IHYDGPSAAL
SDRLLNDLYG ADLDASLLFS DRARNAEPRS LQLVNG