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PHNC_BORPA
ID   PHNC_BORPA              Reviewed;         256 AA.
AC   Q7W148;
DT   01-MAR-2005, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2003, 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=BPP0853;
OS   Bordetella parapertussis (strain 12822 / ATCC BAA-587 / NCTC 13253).
OC   Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC   Alcaligenaceae; Bordetella.
OX   NCBI_TaxID=257311;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=12822 / ATCC BAA-587 / NCTC 13253;
RX   PubMed=12910271; DOI=10.1038/ng1227;
RA   Parkhill J., Sebaihia M., Preston A., Murphy L.D., Thomson N.R.,
RA   Harris D.E., Holden M.T.G., Churcher C.M., Bentley S.D., Mungall K.L.,
RA   Cerdeno-Tarraga A.-M., Temple L., James K.D., Harris B., Quail M.A.,
RA   Achtman M., Atkin R., Baker S., Basham D., Bason N., Cherevach I.,
RA   Chillingworth T., Collins M., Cronin A., Davis P., Doggett J., Feltwell T.,
RA   Goble A., Hamlin N., Hauser H., Holroyd S., Jagels K., Leather S.,
RA   Moule S., Norberczak H., O'Neil S., Ormond D., Price C., Rabbinowitsch E.,
RA   Rutter S., Sanders M., Saunders D., Seeger K., Sharp S., Simmonds M.,
RA   Skelton J., Squares R., Squares S., Stevens K., Unwin L., Whitehead S.,
RA   Barrell B.G., Maskell D.J.;
RT   "Comparative analysis of the genome sequences of Bordetella pertussis,
RT   Bordetella parapertussis and Bordetella bronchiseptica.";
RL   Nat. Genet. 35:32-40(2003).
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; BX640425; CAE40262.1; -; Genomic_DNA.
DR   RefSeq; WP_010927715.1; NC_002928.3.
DR   AlphaFoldDB; Q7W148; -.
DR   SMR; Q7W148; -.
DR   EnsemblBacteria; CAE40262; CAE40262; BPP0853.
DR   KEGG; bpa:BPP0853; -.
DR   HOGENOM; CLU_000604_1_22_4; -.
DR   OMA; ATMLKPN; -.
DR   Proteomes; UP000001421; 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; Translocase; Transport.
FT   CHAIN           1..256
FT                   /note="Phosphonates import ATP-binding protein PhnC"
FT                   /id="PRO_0000092699"
FT   DOMAIN          5..253
FT                   /note="ABC transporter"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01713"
FT   BINDING         38..45
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01713"
SQ   SEQUENCE   256 AA;  27890 MW;  9D74480ACEA56EDE CRC64;
     MATSLRITGL VKEYRAGKPV LNGIDLDIAG QGLTAIIGPS GTGKSTLLRC INRLIEPTSG
     EIVLKDAEGT VDLARVRGQS LRRARRRIGM VFQEYNLVER LTVMENLLTG RLGYTSALNA
     WMRRFDPADI ERAFQLLDTV GLAGFADQRA DALSGGQRQR VGIARALMQR PQLLLADEPT
     SSLDPKTSVE IMKLLTEQGS VNGIPVLVNI HDVELARRYA NRIVGMSGGH VVYDGDGKGL
     DATMLKTIYG GESWLE
 
 
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