PHNC_STAAS
ID PHNC_STAAS Reviewed; 257 AA.
AC Q6GCY2;
DT 01-FEB-2005, integrated into UniProtKB/Swiss-Prot.
DT 19-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 118.
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=SAS0116;
OS Staphylococcus aureus (strain MSSA476).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcaceae;
OC Staphylococcus.
OX NCBI_TaxID=282459;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MSSA476;
RX PubMed=15213324; DOI=10.1073/pnas.0402521101;
RA Holden M.T.G., Feil E.J., Lindsay J.A., Peacock S.J., Day N.P.J.,
RA Enright M.C., Foster T.J., Moore C.E., Hurst L., Atkin R., Barron A.,
RA Bason N., Bentley S.D., Chillingworth C., Chillingworth T., Churcher C.,
RA Clark L., Corton C., Cronin A., Doggett J., Dowd L., Feltwell T., Hance Z.,
RA Harris B., Hauser H., Holroyd S., Jagels K., James K.D., Lennard N.,
RA Line A., Mayes R., Moule S., Mungall K., Ormond D., Quail M.A.,
RA Rabbinowitsch E., Rutherford K.M., Sanders M., Sharp S., Simmonds M.,
RA Stevens K., Whitehead S., Barrell B.G., Spratt B.G., Parkhill J.;
RT "Complete genomes of two clinical Staphylococcus aureus strains: evidence
RT for the rapid evolution of virulence and drug resistance.";
RL Proc. Natl. Acad. Sci. U.S.A. 101:9786-9791(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 membrane {ECO:0000255|HAMAP-Rule:MF_01713};
CC Peripheral membrane protein {ECO:0000255|HAMAP-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; BX571857; CAG41884.1; -; Genomic_DNA.
DR RefSeq; WP_000078092.1; NC_002953.3.
DR AlphaFoldDB; Q6GCY2; -.
DR SMR; Q6GCY2; -.
DR KEGG; sas:SAS0116; -.
DR HOGENOM; CLU_000604_1_22_9; -.
DR OMA; GRMPRWR; -.
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 membrane; Membrane; Nucleotide-binding;
KW Phosphonate transport; Translocase; Transport.
FT CHAIN 1..257
FT /note="Phosphonates import ATP-binding protein PhnC"
FT /id="PRO_0000092733"
FT DOMAIN 4..248
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 257 AA; 28689 MW; AC1D5581FAF1873B CRC64;
MSQIEFKNVS KVYPNGHVGL KNINLNIEKG EFAVIVGLSG AGKSTLLRSV NRLHDITSGE
IFIQGKSITK AHGKALLEMR RNIGMIFQHF NLVKRSSVLR NVLSGRVGYH PTWKMVLGLF
PKEDKIKAMD ALERVNILDK YNQRSDELSG GQQQRISIAR ALCQESEIIL ADEPVASLDP
LTTKQVMDDL RKINQELGIT ILINLHFVDL AKEYGTRIIG LRDGEVVYDG PASEATDDVF
SEIYGRTIKE DEKLGVN