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PHND_ECOLI
ID   PHND_ECOLI              Reviewed;         338 AA.
AC   P16682; Q2M6J9;
DT   01-AUG-1990, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1991, sequence version 2.
DT   03-AUG-2022, entry version 149.
DE   RecName: Full=Phosphonates-binding periplasmic protein;
DE   Flags: Precursor;
GN   Name=phnD; Synonyms=psiD; OrderedLocusNames=b4105, JW4066;
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.
RC   STRAIN=K12 / XL1-Blue;
RX   PubMed=16751609; DOI=10.1110/ps.062135206;
RA   Rizk S.S., Cuneo M.J., Hellinga H.W.;
RT   "Identification of cognate ligands for the Escherichia coli phnD protein
RT   product and engineering of a reagentless fluorescent biosensor for
RT   phosphonates.";
RL   Protein Sci. 15:1745-1751(2006).
CC   -!- FUNCTION: Phosphonate binding protein that is part of the phosphonate
CC       uptake system. Exhibits high affinity for 2-aminoethylphosphonate, and
CC       somewhat less affinity to ethylphosphonate, methylphosphonate,
CC       phosphonoacetate and phenylphosphonate. {ECO:0000269|PubMed:16751609}.
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:0000305}.
CC   -!- SUBCELLULAR LOCATION: Periplasm {ECO:0000305}.
CC   -!- MISCELLANEOUS: The sequence shown is that of strain K12.
CC   -!- SIMILARITY: Belongs to the phosphate/phosphite/phosphonate binding
CC       protein family. {ECO:0000305}.
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DR   EMBL; J05260; AAA24340.1; -; Genomic_DNA.
DR   EMBL; D90227; BAA14263.1; -; Genomic_DNA.
DR   EMBL; U14003; AAA97004.1; -; Genomic_DNA.
DR   EMBL; U00096; AAC77066.1; -; Genomic_DNA.
DR   EMBL; AP009048; BAE78107.1; -; Genomic_DNA.
DR   PIR; S56333; S56333.
DR   RefSeq; NP_418529.1; NC_000913.3.
DR   RefSeq; WP_000992002.1; NZ_SSZK01000016.1.
DR   AlphaFoldDB; P16682; -.
DR   BioGRID; 4263091; 145.
DR   DIP; DIP-10483N; -.
DR   IntAct; P16682; 4.
DR   STRING; 511145.b4105; -.
DR   TCDB; 3.A.1.9.1; the atp-binding cassette (abc) superfamily.
DR   PaxDb; P16682; -.
DR   PRIDE; P16682; -.
DR   EnsemblBacteria; AAC77066; AAC77066; b4105.
DR   EnsemblBacteria; BAE78107; BAE78107; BAE78107.
DR   GeneID; 66671985; -.
DR   GeneID; 948624; -.
DR   KEGG; ecj:JW4066; -.
DR   KEGG; eco:b4105; -.
DR   PATRIC; fig|1411691.4.peg.2595; -.
DR   EchoBASE; EB0708; -.
DR   eggNOG; COG3221; Bacteria.
DR   HOGENOM; CLU_051472_2_0_6; -.
DR   InParanoid; P16682; -.
DR   OMA; QGMRFDK; -.
DR   PhylomeDB; P16682; -.
DR   BioCyc; EcoCyc:PHND-MON; -.
DR   PRO; PR:P16682; -.
DR   Proteomes; UP000000318; Chromosome.
DR   Proteomes; UP000000625; Chromosome.
DR   GO; GO:0043190; C:ATP-binding cassette (ABC) transporter complex; IEA:InterPro.
DR   GO; GO:0042597; C:periplasmic space; IEA:UniProtKB-SubCell.
DR   GO; GO:0015716; P:organic phosphonate transport; IEA:UniProtKB-KW.
DR   GO; GO:0055085; P:transmembrane transport; IEA:InterPro.
DR   InterPro; IPR005770; PhnD.
DR   InterPro; IPR017797; Phosphnate-bd.
DR   PANTHER; PTHR30043:SF1; PTHR30043:SF1; 1.
DR   TIGRFAMs; TIGR01098; 3A0109s03R; 1.
DR   TIGRFAMs; TIGR03431; PhnD; 1.
PE   3: Inferred from homology;
KW   Periplasm; Phosphonate transport; Reference proteome; Signal; Transport.
FT   SIGNAL          1..26
FT                   /evidence="ECO:0000255"
FT   CHAIN           27..338
FT                   /note="Phosphonates-binding periplasmic protein"
FT                   /id="PRO_0000031836"
FT   VARIANT         312
FT                   /note="E -> A (in strain: B)"
SQ   SEQUENCE   338 AA;  37371 MW;  84B4366AE8D1BF62 CRC64;
     MNAKIIASLA FTSMFSLSTL LSPAHAEEQE KALNFGIIST ESQQNLKPQW TPFLQDMEKK
     LGVKVNAFFA PDYAGIIQGM RFNKVDIAWY GNLSAMEAVD RANGQVFAQT VAADGSPGYW
     SVLIVNKDSP INNLNDLLAK RKDLTFGNGD PNSTSGFLVP GYYVFAKNNI SASDFKRTVN
     AGHETNALAV ANKQVDVATN NTENLDKLKT SAPEKLKELK VIWKSPLIPG DPIVWRKNLS
     ETTKDKIYDF FMNYGKTPEE KAVLERLGWA PFRASSDLQL VPIRQLALFK EMQGVKSNKG
     LNEQDKLAKT TEIQAQLDDL DRLNNALSAM SSVSKAVQ
 
 
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