位置:首页 > 蛋白库 > PHNK_ECOLI
PHNK_ECOLI
ID   PHNK_ECOLI              Reviewed;         252 AA.
AC   P16678; Q2M6K6;
DT   01-AUG-1990, integrated into UniProtKB/Swiss-Prot.
DT   01-AUG-1990, sequence version 1.
DT   03-AUG-2022, entry version 162.
DE   RecName: Full=Putative phosphonates utilization ATP-binding protein PhnK;
GN   Name=phnK; OrderedLocusNames=b4097, JW5727;
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   SEQUENCE REVISION TO 47.
RX   PubMed=16397293; DOI=10.1093/nar/gkj405;
RA   Riley M., Abe T., Arnaud M.B., Berlyn M.K.B., Blattner F.R.,
RA   Chaudhuri R.R., Glasner J.D., Horiuchi T., Keseler I.M., Kosuge T.,
RA   Mori H., Perna N.T., Plunkett G. III, Rudd K.E., Serres M.H., Thomas G.H.,
RA   Thomson N.R., Wishart D., Wanner B.L.;
RT   "Escherichia coli K-12: a cooperatively developed annotation snapshot
RT   -- 2005.";
RL   Nucleic Acids Res. 34:1-9(2006).
RN   [6]
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   [7]
RP   NO FUNCTION IN RPNTP SYNTHESIS.
RC   STRAIN=K12;
RX   PubMed=22089136; DOI=10.1038/nature10622;
RA   Kamat S.S., Williams H.J., Raushel F.M.;
RT   "Intermediates in the transformation of phosphonates to phosphate by
RT   bacteria.";
RL   Nature 480:570-573(2011).
RN   [8]
RP   SUBUNIT.
RC   STRAIN=K12;
RX   PubMed=21705661; DOI=10.1073/pnas.1104922108;
RA   Jochimsen B., Lolle S., McSorley F.R., Nabi M., Stougaard J., Zechel D.L.,
RA   Hove-Jensen B.;
RT   "Five phosphonate operon gene products as components of a multi-subunit
RT   complex of the carbon-phosphorus lyase pathway.";
RL   Proc. Natl. Acad. Sci. U.S.A. 108:11393-11398(2011).
CC   -!- FUNCTION: Belongs to an operon involved in alkylphosphonate uptake and
CC       C-P lyase. Exact function not known. PhnK is not required for the
CC       ribophosphonate triphosphate (RPnTP) synthase reaction.
CC   -!- SUBUNIT: Forms a complex with PhnG, PhnH, PhnI and PhnJ with the
CC       suggested composition PhnG(4)H(2)I(2)J(2)K.
CC       {ECO:0000269|PubMed:21705661}.
CC   -!- SIMILARITY: Belongs to the ABC transporter superfamily. {ECO:0000305}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; J05260; AAA24349.1; -; Genomic_DNA.
DR   EMBL; D90227; BAA14271.1; -; Genomic_DNA.
DR   EMBL; U14003; AAA96996.1; -; Genomic_DNA.
DR   EMBL; U00096; AAT48240.1; -; Genomic_DNA.
DR   EMBL; AP009048; BAE78100.1; -; Genomic_DNA.
DR   PIR; S56325; S56325.
DR   RefSeq; WP_001075514.1; NZ_SSZK01000016.1.
DR   RefSeq; YP_026282.1; NC_000913.3.
DR   AlphaFoldDB; P16678; -.
DR   SMR; P16678; -.
DR   BioGRID; 4262020; 12.
DR   BioGRID; 852904; 2.
DR   ComplexPortal; CPX-1929; PhnGHIJKL complex.
DR   DIP; DIP-10490N; -.
DR   IntAct; P16678; 6.
DR   STRING; 511145.b4097; -.
DR   PaxDb; P16678; -.
DR   PRIDE; P16678; -.
DR   DNASU; 948611; -.
DR   EnsemblBacteria; AAT48240; AAT48240; b4097.
DR   EnsemblBacteria; BAE78100; BAE78100; BAE78100.
DR   GeneID; 58459672; -.
DR   GeneID; 948611; -.
DR   KEGG; ecj:JW5727; -.
DR   KEGG; eco:b4097; -.
DR   PATRIC; fig|1411691.4.peg.2603; -.
DR   EchoBASE; EB0714; -.
DR   eggNOG; COG4107; Bacteria.
DR   HOGENOM; CLU_000604_1_23_6; -.
DR   InParanoid; P16678; -.
DR   OMA; TDWGFVR; -.
DR   PhylomeDB; P16678; -.
DR   BioCyc; EcoCyc:PHNK-MON; -.
DR   BioCyc; MetaCyc:PHNK-MON; -.
DR   PRO; PR:P16678; -.
DR   Proteomes; UP000000318; Chromosome.
DR   Proteomes; UP000000625; Chromosome.
DR   GO; GO:0061694; C:alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase complex; IPI:ComplexPortal.
DR   GO; GO:1904176; C:carbon phosphorus lyase complex; IDA:EcoCyc.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0019700; P:organic phosphonate catabolic process; IMP:EcoCyc.
DR   GO; GO:0019634; P:organic phosphonate metabolic process; IDA:ComplexPortal.
DR   GO; GO:0015716; P:organic phosphonate transport; IDA:ComplexPortal.
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; IPR012700; CP_lyase_PhnK.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   Pfam; PF00005; ABC_tran; 1.
DR   PIRSF; PIRSF037116; CP_lyase_PhnK; 1.
DR   SMART; SM00382; AAA; 1.
DR   SUPFAM; SSF52540; SSF52540; 1.
DR   TIGRFAMs; TIGR02323; CP_lyasePhnK; 1.
DR   PROSITE; PS00211; ABC_TRANSPORTER_1; 1.
DR   PROSITE; PS50893; ABC_TRANSPORTER_2; 1.
PE   1: Evidence at protein level;
KW   ATP-binding; Nucleotide-binding; Reference proteome; Transport.
FT   CHAIN           1..252
FT                   /note="Putative phosphonates utilization ATP-binding
FT                   protein PhnK"
FT                   /id="PRO_0000092744"
FT   DOMAIN          6..246
FT                   /note="ABC transporter"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00434"
FT   BINDING         38..45
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00434"
FT   CONFLICT        47
FT                   /note="L -> Q (in Ref. 3; AAA96996)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   252 AA;  27831 MW;  3B8677F22C472A9F CRC64;
     MNQPLLSVNN LTHLYAPGKG FSDVSFDLWP GEVLGIVGES GSGKTTLLKS ISARLTPQQG
     EIHYENRSLY AMSEADRRRL LRTEWGVVHQ HPLDGLRRQV SAGGNIGERL MATGARHYGD
     IRATAQKWLE EVEIPANRID DLPTTFSGGM QQRLQIARNL VTHPKLVFMD EPTGGLDVSV
     QARLLDLLRG LVVELNLAVV IVTHDLGVAR LLADRLLVMK QGQVVESGLT DRVLDDPHHP
     YTQLLVSSVL QN
 
 
维奥蛋白资源库 - 中文蛋白资源 CopyRight © 2010-2024