PHNC_THIDA
ID PHNC_THIDA Reviewed; 259 AA.
AC Q3SGJ8;
DT 06-FEB-2007, integrated into UniProtKB/Swiss-Prot.
DT 11-OCT-2005, sequence version 1.
DT 03-AUG-2022, entry version 111.
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=Tbd_2299;
OS Thiobacillus denitrificans (strain ATCC 25259).
OC Bacteria; Proteobacteria; Betaproteobacteria; Nitrosomonadales;
OC Thiobacillaceae; Thiobacillus.
OX NCBI_TaxID=292415;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 25259;
RX PubMed=16452431; DOI=10.1128/jb.188.4.1473-1488.2006;
RA Beller H.R., Chain P.S., Letain T.E., Chakicherla A., Larimer F.W.,
RA Richardson P.M., Coleman M.A., Wood A.P., Kelly D.P.;
RT "The genome sequence of the obligately chemolithoautotrophic, facultatively
RT anaerobic bacterium Thiobacillus denitrificans.";
RL J. Bacteriol. 188:1473-1488(2006).
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; CP000116; AAZ98252.1; -; Genomic_DNA.
DR RefSeq; WP_011312811.1; NC_007404.1.
DR AlphaFoldDB; Q3SGJ8; -.
DR SMR; Q3SGJ8; -.
DR STRING; 292415.Tbd_2299; -.
DR PRIDE; Q3SGJ8; -.
DR EnsemblBacteria; AAZ98252; AAZ98252; Tbd_2299.
DR KEGG; tbd:Tbd_2299; -.
DR eggNOG; COG3638; Bacteria.
DR HOGENOM; CLU_000604_1_22_4; -.
DR OMA; SILVTHE; -.
DR OrthoDB; 1181903at2; -.
DR Proteomes; UP000008291; 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..259
FT /note="Phosphonates import ATP-binding protein PhnC"
FT /id="PRO_0000274765"
FT DOMAIN 4..245
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 259 AA; 28231 MW; 9B140BFC7ACDAB35 CRC64;
MSAISIQSVT KRFPNGFEAL KGIDTEIQTG SFTVVLGPSG AGKSTLLRLM NGLETPTTGA
VRIDGETVDG HRLRHIRSKV AMVFQQFNLV ERLSVVTNVL TGRLAQRSWV GSVFYLFRQE
DLGIAREALA RVGLTDKAWS RADKLSGGQQ QRVGIARALA QRPKVILADE PVASLDPVSS
EEIMALLREI CDRDGITVVV NLHQVDLAKR FADRIIGMNA GRVVFDGTPA ELSAQALRTI
YQREGIEDDT SLDLALAYA