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PHNC_ECOLI
ID   PHNC_ECOLI              Reviewed;         262 AA.
AC   P16677; Q2M6J8;
DT   01-AUG-1990, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1991, sequence version 2.
DT   03-AUG-2022, entry version 165.
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};
GN   OrderedLocusNames=b4106, JW4067;
OS   Escherichia coli (strain K12).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=83333;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=B;
RX   PubMed=2155230; DOI=10.1016/s0021-9258(19)39587-0;
RA   Chen C.-M., Ye Q.-Z., Zhu Z., Wanner B.L., Walsh C.T.;
RT   "Molecular biology of carbon-phosphorus bond cleavage. Cloning and
RT   sequencing of the phn (psiD) genes involved in alkylphosphonate uptake and
RT   C-P lyase activity in Escherichia coli B.";
RL   J. Biol. Chem. 265:4461-4471(1990).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=K12;
RX   PubMed=1840580; DOI=10.1128/jb.173.8.2665-2672.1991;
RA   Makino K., Kim S.K., Shinagawa H., Amemura M., Nakata A.;
RT   "Molecular analysis of the cryptic and functional phn operons for
RT   phosphonate use in Escherichia coli K-12.";
RL   J. Bacteriol. 173:2665-2672(1991).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=K12 / MG1655 / ATCC 47076;
RX   PubMed=7610040; DOI=10.1093/nar/23.12.2105;
RA   Burland V.D., Plunkett G. III, Sofia H.J., Daniels D.L., Blattner F.R.;
RT   "Analysis of the Escherichia coli genome VI: DNA sequence of the region
RT   from 92.8 through 100 minutes.";
RL   Nucleic Acids Res. 23:2105-2119(1995).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=K12 / MG1655 / ATCC 47076;
RX   PubMed=9278503; DOI=10.1126/science.277.5331.1453;
RA   Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V.,
RA   Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F.,
RA   Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B.,
RA   Shao Y.;
RT   "The complete genome sequence of Escherichia coli K-12.";
RL   Science 277:1453-1462(1997).
RN   [5]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX   PubMed=16738553; DOI=10.1038/msb4100049;
RA   Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S.,
RA   Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.;
RT   "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655
RT   and W3110.";
RL   Mol. Syst. Biol. 2:E1-E5(2006).
RN   [6]
RP   FUNCTION.
RX   PubMed=1846145; DOI=10.1128/jb.173.2.587-600.1991;
RA   Metcalf W.W., Wanner B.L.;
RT   "Involvement of the Escherichia coli phn (psiD) gene cluster in
RT   assimilation of phosphorus in the form of phosphonates, phosphite, Pi
RT   esters, and Pi.";
RL   J. Bacteriol. 173:587-600(1991).
RN   [7]
RP   FUNCTION.
RX   PubMed=8388873; DOI=10.1128/jb.175.11.3430-3442.1993;
RA   Metcalf W.W., Wanner B.L.;
RT   "Mutational analysis of an Escherichia coli fourteen-gene operon for
RT   phosphonate degradation, using TnphoA' elements.";
RL   J. Bacteriol. 175:3430-3442(1993).
CC   -!- FUNCTION: Part of the ABC transporter complex PhnCDE involved in
CC       phosphonates, phosphate esters, phosphite and phosphate import.
CC       Responsible for energy coupling to the transport system.
CC       {ECO:0000269|PubMed:1846145, ECO:0000269|PubMed:8388873}.
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   -!- MISCELLANEOUS: Phosphonates utilization is cryptic in strain K12.
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; J05260; AAA24339.1; -; Genomic_DNA.
DR   EMBL; D90227; BAA14262.1; -; Genomic_DNA.
DR   EMBL; U14003; AAA97005.1; -; Genomic_DNA.
DR   EMBL; U00096; AAC77067.1; -; Genomic_DNA.
DR   EMBL; AP009048; BAE78108.1; -; Genomic_DNA.
DR   PIR; A65220; A65220.
DR   RefSeq; NP_418530.1; NC_000913.3.
DR   RefSeq; WP_001193409.1; NZ_SSZK01000016.1.
DR   AlphaFoldDB; P16677; -.
DR   SMR; P16677; -.
DR   IntAct; P16677; 1.
DR   STRING; 511145.b4106; -.
DR   TCDB; 3.A.1.9.1; the atp-binding cassette (abc) superfamily.
DR   PaxDb; P16677; -.
DR   PRIDE; P16677; -.
DR   EnsemblBacteria; AAC77067; AAC77067; b4106.
DR   EnsemblBacteria; BAE78108; BAE78108; BAE78108.
DR   GeneID; 948623; -.
DR   KEGG; ecj:JW4067; -.
DR   KEGG; eco:b4106; -.
DR   PATRIC; fig|1411691.4.peg.2594; -.
DR   EchoBASE; EB0707; -.
DR   eggNOG; COG3638; Bacteria.
DR   HOGENOM; CLU_000604_1_22_6; -.
DR   InParanoid; P16677; -.
DR   OMA; GRMPRWR; -.
DR   PhylomeDB; P16677; -.
DR   BioCyc; EcoCyc:PHNC-MON; -.
DR   PRO; PR:P16677; -.
DR   Proteomes; UP000000318; Chromosome.
DR   Proteomes; UP000000625; 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..262
FT                   /note="Phosphonates import ATP-binding protein PhnC"
FT                   /id="PRO_0000092706"
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"
FT   VARIANT         60
FT                   /note="V -> A (in strain: B)"
FT   VARIANT         87
FT                   /note="H -> N (in strain: B)"
FT   VARIANT         127
FT                   /note="G -> R (in strain: B)"
FT   VARIANT         255
FT                   /note="V -> I (in strain: B)"
SQ   SEQUENCE   262 AA;  29431 MW;  393EF8F30FD18D6C CRC64;
     MQTIIRVEKL AKTFNQHQAL HAVDLNIHHG EMVALLGPSG SGKSTLLRHL SGLITGDKSV
     GSHIELLGRT VQREGRLARD IRKSRAHTGY IFQQFNLVNR LSVLENVLIG ALGSTPFWRT
     CFSWFTGEQK QRALQALTRV GMVHFAHQRV STLSGGQQQR VAIARALMQQ AKVILADEPI
     ASLDPESARI VMDTLRDINQ NDGITVVVTL HQVDYALRYC ERIVALRQGH VFYDGSSQQF
     DNERFDHLYR SINRVEENAK AA
 
 
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