NLPE_ECOLI
ID NLPE_ECOLI Reviewed; 236 AA.
AC P40710;
DT 01-FEB-1995, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1995, sequence version 1.
DT 03-AUG-2022, entry version 150.
DE RecName: Full=Lipoprotein NlpE {ECO:0000303|PubMed:7635808};
DE AltName: Full=Copper homeostasis protein CutF {ECO:0000303|PubMed:7635807};
DE Flags: Precursor;
GN Name=nlpE {ECO:0000303|PubMed:7635808};
GN Synonyms=cutF {ECO:0000303|PubMed:7635807};
GN OrderedLocusNames=b0192, JW0188;
OS Escherichia coli (strain K12).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=83333;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], SUBCELLULAR LOCATION, DISRUPTION
RP PHENOTYPE, AND PALMITOYLATION AT CYS-21.
RC STRAIN=K12 / MC4100 / ATCC 35695 / DSM 6574;
RX PubMed=7635808; DOI=10.1128/jb.177.15.4216-4223.1995;
RA Snyder W.B., Davis L.J., Danese P.N., Cosma C.L., Silhavy T.J.;
RT "Overproduction of NlpE, a new outer membrane lipoprotein, suppresses the
RT toxicity of periplasmic LacZ by activation of the Cpx signal transduction
RT pathway.";
RL J. Bacteriol. 177:4216-4223(1995).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, AND DISRUPTION PHENOTYPE.
RC STRAIN=K12 / MC4100 / ATCC 35695 / DSM 6574;
RX PubMed=7635807; DOI=10.1128/jb.177.15.4207-4215.1995;
RA Gupta S.D., Lee B.T.O., Camakaris J., Wu H.C.;
RT "Identification of cutC and cutF (nlpE) genes involved in copper tolerance
RT in Escherichia coli.";
RL J. Bacteriol. 177:4207-4215(1995).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RA Yamamoto Y.;
RL Submitted (DEC-1995) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RA Takemoto K., Mori H., Murayama N., Kataoka K., Yano M., Itoh T.,
RA Yamamoto Y., Inokuchi H., Miki T., Hatada E., Fukuda R., Ichihara S.,
RA Mizuno T., Makino K., Nakata A., Yura T., Sampei G., Mizobuchi K.;
RT "Systematic sequencing of the Escherichia coli genome: analysis of the 4.0
RT - 6.0 min (189,987 - 281,416bp) region.";
RL Submitted (FEB-1996) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / MG1655 / ATCC 47076;
RA Chung E., Allen E., Araujo R., Aparicio A.M., Davis K., Duncan M.,
RA Federspiel N., Hyman R., Kalman S., Komp C., Kurdi O., Lew H., Lin D.,
RA Namath A., Oefner P., Roberts D., Schramm S., Davis R.W.;
RT "Sequence of minutes 4-25 of Escherichia coli.";
RL Submitted (JAN-1997) to the EMBL/GenBank/DDBJ databases.
RN [6]
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 [7]
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 [8]
RP FUNCTION IN BIOFILM FORMATION, AND DISRUPTION PHENOTYPE.
RC STRAIN=K12 / MC4100 / ATCC 35695 / DSM 6574;
RX PubMed=11830644; DOI=10.1073/pnas.042521699;
RA Otto K., Silhavy T.J.;
RT "Surface sensing and adhesion of Escherichia coli controlled by the Cpx-
RT signaling pathway.";
RL Proc. Natl. Acad. Sci. U.S.A. 99:2287-2292(2002).
RN [9]
RP FUNCTION IN DEGP EXPRESSION, SUBCELLULAR LOCATION, AND MUTAGENESIS OF
RP CYS-21 AND 22-ASN-ASN-23.
RC STRAIN=K12 / MC4100 / ATCC 35695 / DSM 6574;
RX PubMed=15252048; DOI=10.1074/jbc.m406390200;
RA Miyadai H., Tanaka-Masuda K., Matsuyama S., Tokuda H.;
RT "Effects of lipoprotein overproduction on the induction of DegP (HtrA)
RT involved in quality control in the Escherichia coli periplasm.";
RL J. Biol. Chem. 279:39807-39813(2004).
RN [10]
RP X-RAY CRYSTALLOGRAPHY (2.60 ANGSTROMS) OF 21-236 IN MUTANT ALA-21,
RP FUNCTION, SUBUNIT, DOMAIN, DISULFIDE BOND, AND MUTAGENESIS OF
RP 51-CYS--CYS-54; CYS-51; CYS-54; CYS-165 AND CYS-231.
RX PubMed=17698001; DOI=10.1016/j.str.2007.06.014;
RA Hirano Y., Hossain M.M., Takeda K., Tokuda H., Miki K.;
RT "Structural studies of the Cpx pathway activator NlpE on the outer membrane
RT of Escherichia coli.";
RL Structure 15:963-976(2007).
CC -!- FUNCTION: Involved in copper homeostasis, could be involved in both
CC copper efflux and the delivery of copper to copper-dependent enzymes
CC (PubMed:7635807). Required for efficient binding of stationary phase
CC cells to hydrophobic surfaces, part of the process of biofilm formation
CC (PubMed:11830644). Functions during envelope stress responses; when
CC overproduced induces degP through the activation of the two-component
CC envelope stress response system CpxA/CpxR (PubMed:7635808,
CC PubMed:15252048). DegP induction seems to require membrane anchoring of
CC this protein (PubMed:15252048). Structural changes and/or interaction
CC of the CXXC motif with its environment may lead to activation of the
CC Cpx stress response (PubMed:17698001). {ECO:0000269|PubMed:11830644,
CC ECO:0000269|PubMed:15252048, ECO:0000269|PubMed:17698001,
CC ECO:0000269|PubMed:7635808}.
CC -!- SUBUNIT: Probably exists as a monomer in vivo, can however form
CC homodimers which swap domains (PubMed:17698001).
CC {ECO:0000269|PubMed:17698001}.
CC -!- INTERACTION:
CC P40710; P40710: nlpE; NbExp=3; IntAct=EBI-1116525, EBI-1116525;
CC -!- SUBCELLULAR LOCATION: Cell outer membrane {ECO:0000269|PubMed:15252048,
CC ECO:0000305|PubMed:7635808}; Lipid-anchor {ECO:0000305|PubMed:15252048,
CC ECO:0000305|PubMed:7635808}.
CC -!- DOMAIN: The mature protein has 2 domains, the N-terminus (residues 21-
CC 100) and the C-terminus (residues 126-236) joined by a flexible linker;
CC both domains form beta-barrels. In the crystal structure of the soluble
CC mutant (Ala-21) the N-terminus of 1 subunit interacts with the C-
CC terminus of the other. {ECO:0000269|PubMed:17698001}.
CC -!- PTM: Palmitoylated. {ECO:0000269|PubMed:7635808}.
CC -!- PTM: Seems to only form a disulfide bond between Cys-165 and Cys-231.
CC The 2 other cysteine residues may however be chemically active.
CC {ECO:0000269|Ref.4}.
CC -!- DISRUPTION PHENOTYPE: No visible phenotype (PubMed:7635808). Slightly
CC copper sensitive (PubMed:7635807). Decreased numbers of stationary
CC phase cells bind to hydrophobic surfaces, cellular adhesion has altered
CC dynamic properties; no induction of cpxR when cells bind to hydrophobic
CC surfaces (PubMed:11830644). {ECO:0000269|PubMed:11830644,
CC ECO:0000269|PubMed:7635807, ECO:0000269|PubMed:7635808}.
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DR EMBL; U18345; AAA86093.1; -; Genomic_DNA.
DR EMBL; L38619; AAA82972.1; -; Genomic_DNA.
DR EMBL; D49445; BAA08433.1; -; Genomic_DNA.
DR EMBL; U70214; AAB08620.1; -; Genomic_DNA.
DR EMBL; U00096; AAC73303.1; -; Genomic_DNA.
DR EMBL; AP009048; BAA77868.1; -; Genomic_DNA.
DR PIR; H64743; H64743.
DR RefSeq; NP_414734.1; NC_000913.3.
DR RefSeq; WP_000239163.1; NZ_SSZK01000004.1.
DR PDB; 2Z4H; X-ray; 2.80 A; A/B=21-236.
DR PDB; 2Z4I; X-ray; 2.60 A; A/B=21-236.
DR PDBsum; 2Z4H; -.
DR PDBsum; 2Z4I; -.
DR AlphaFoldDB; P40710; -.
DR SMR; P40710; -.
DR BioGRID; 4260842; 209.
DR DIP; DIP-9353N; -.
DR IntAct; P40710; 3.
DR STRING; 511145.b0192; -.
DR jPOST; P40710; -.
DR PaxDb; P40710; -.
DR PRIDE; P40710; -.
DR EnsemblBacteria; AAC73303; AAC73303; b0192.
DR EnsemblBacteria; BAA77868; BAA77868; BAA77868.
DR GeneID; 946782; -.
DR KEGG; ecj:JW0188; -.
DR KEGG; eco:b0192; -.
DR PATRIC; fig|1411691.4.peg.2086; -.
DR EchoBASE; EB2058; -.
DR eggNOG; COG3015; Bacteria.
DR HOGENOM; CLU_1219320_0_0_6; -.
DR InParanoid; P40710; -.
DR OMA; GTWVMNQ; -.
DR BioCyc; EcoCyc:EG12137-MON; -.
DR EvolutionaryTrace; P40710; -.
DR PRO; PR:P40710; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; Chromosome.
DR GO; GO:0009279; C:cell outer membrane; IDA:EcoCyc.
DR GO; GO:0042802; F:identical protein binding; IPI:IntAct.
DR GO; GO:0007155; P:cell adhesion; IEA:UniProtKB-KW.
DR GO; GO:0010810; P:regulation of cell-substrate adhesion; IMP:EcoCyc.
DR GO; GO:1990169; P:stress response to copper ion; IMP:EcoCyc.
DR Gene3D; 2.40.128.300; -; 1.
DR Gene3D; 2.40.50.540; -; 1.
DR InterPro; IPR007298; Cu-R_lipoprotein_NlpE.
DR InterPro; IPR033450; NlpE_C.
DR InterPro; IPR038139; NlpE_C_sf.
DR InterPro; IPR043176; NlpE_N_sf.
DR Pfam; PF04170; NlpE; 1.
DR Pfam; PF17185; NlpE_C; 1.
DR PROSITE; PS51257; PROKAR_LIPOPROTEIN; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Cell adhesion; Cell outer membrane; Copper; Disulfide bond;
KW Lipoprotein; Membrane; Palmitate; Reference proteome; Signal.
FT SIGNAL 1..20
FT CHAIN 21..236
FT /note="Lipoprotein NlpE"
FT /id="PRO_0000018036"
FT TOPO_DOM 21..236
FT /note="Periplasmic"
FT /evidence="ECO:0000305|PubMed:7635808"
FT REGION 21..100
FT /note="N-terminal domain"
FT /evidence="ECO:0000303|PubMed:17698001"
FT REGION 126..236
FT /note="C-terminal domain"
FT /evidence="ECO:0000303|PubMed:17698001"
FT REGION 144..156
FT /note="Could contain a copper-binding motif"
FT /evidence="ECO:0000303|PubMed:7635807"
FT MOTIF 51..54
FT /note="CXXC"
FT /evidence="ECO:0000303|PubMed:17698001"
FT LIPID 21
FT /note="N-palmitoyl cysteine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00303,
FT ECO:0000305|PubMed:7635808"
FT LIPID 21
FT /note="S-diacylglycerol cysteine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00303"
FT DISULFID 165..231
FT /evidence="ECO:0000305|PubMed:17698001"
FT MUTAGEN 21
FT /note="C->A: No longer induces degP when overexpressed,
FT targeted to the periplasm."
FT /evidence="ECO:0000269|PubMed:15252048"
FT MUTAGEN 22..23
FT /note="NN->DD: Slightly stronger than normal induction of
FT degP when overexpressed, mistargeted to inner membrane."
FT /evidence="ECO:0000269|PubMed:15252048"
FT MUTAGEN 51..54
FT /note="CADC->SADS: Forms oxidized monomers."
FT /evidence="ECO:0000269|PubMed:17698001"
FT MUTAGEN 51
FT /note="C->S: Forms oxidized monomers."
FT /evidence="ECO:0000269|PubMed:17698001"
FT MUTAGEN 54
FT /note="C->S: Forms oxidized monomers."
FT /evidence="ECO:0000269|PubMed:17698001"
FT MUTAGEN 165
FT /note="C->S: No oxidized monomer forms; when associated
FT with Ser-231."
FT /evidence="ECO:0000269|PubMed:17698001"
FT MUTAGEN 231
FT /note="C->S: No oxidized monomer forms; when associated
FT with Ser-165."
FT /evidence="ECO:0000269|PubMed:17698001"
FT STRAND 44..51
FT /evidence="ECO:0007829|PDB:2Z4I"
FT STRAND 54..63
FT /evidence="ECO:0007829|PDB:2Z4I"
FT STRAND 67..76
FT /evidence="ECO:0007829|PDB:2Z4I"
FT STRAND 80..92
FT /evidence="ECO:0007829|PDB:2Z4I"
FT STRAND 95..102
FT /evidence="ECO:0007829|PDB:2Z4I"
FT STRAND 107..113
FT /evidence="ECO:0007829|PDB:2Z4I"
FT STRAND 116..120
FT /evidence="ECO:0007829|PDB:2Z4I"
FT STRAND 128..131
FT /evidence="ECO:0007829|PDB:2Z4I"
FT STRAND 134..137
FT /evidence="ECO:0007829|PDB:2Z4I"
FT STRAND 147..155
FT /evidence="ECO:0007829|PDB:2Z4I"
FT STRAND 160..164
FT /evidence="ECO:0007829|PDB:2Z4I"
FT TURN 165..167
FT /evidence="ECO:0007829|PDB:2Z4I"
FT STRAND 170..173
FT /evidence="ECO:0007829|PDB:2Z4I"
FT HELIX 177..187
FT /evidence="ECO:0007829|PDB:2Z4I"
FT STRAND 189..191
FT /evidence="ECO:0007829|PDB:2Z4H"
FT STRAND 194..205
FT /evidence="ECO:0007829|PDB:2Z4I"
FT TURN 208..210
FT /evidence="ECO:0007829|PDB:2Z4I"
FT STRAND 214..221
FT /evidence="ECO:0007829|PDB:2Z4I"
FT STRAND 225..228
FT /evidence="ECO:0007829|PDB:2Z4I"
SQ SEQUENCE 236 AA; 25844 MW; 016DAD52EBBE366C CRC64;
MVKKAIVTAM AVISLFTLMG CNNRAEVDTL SPAQAAELKP MPQSWRGVLP CADCEGIETS
LFLEKDGTWV MNERYLGARE EPSSFASYGT WARTADKLVL TDSKGEKSYY RAKGDALEML
DREGNPIESQ FNYTLEAAQS SLPMTPMTLR GMYFYMADAA TFTDCATGKR FMVANNAELE
RSYLAARGHS EKPVLLSVEG HFTLEGNPDT GAPTKVLAPD TAGKFYPNQD CSSLGQ
