NLPI_ECOLI
ID NLPI_ECOLI Reviewed; 294 AA.
AC P0AFB1; P39833; Q2M947;
DT 20-DEC-2005, integrated into UniProtKB/Swiss-Prot.
DT 20-DEC-2005, sequence version 1.
DT 03-AUG-2022, entry version 124.
DE RecName: Full=Lipoprotein NlpI;
DE Flags: Precursor;
GN Name=nlpI; Synonyms=yhbM; OrderedLocusNames=b3163, JW3132;
OS Escherichia coli (strain K12).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=83333;
RN [1]
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 [2]
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 [3]
RP PRELIMINARY NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=2045359; DOI=10.1128/jb.173.11.3291-3302.1991;
RA Toone W.M., Rudd K.E., Friesen J.D.;
RT "deaD, a new Escherichia coli gene encoding a presumed ATP-dependent RNA
RT helicase, can suppress a mutation in rpsB, the gene encoding ribosomal
RT protein S2.";
RL J. Bacteriol. 173:3291-3302(1991).
RN [4]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-41.
RC STRAIN=JCH5/JC553;
RX PubMed=2432069; DOI=10.1016/s0021-9258(19)75888-8;
RA Regnier P., Grunberg-Manago M., Portier C.;
RT "Nucleotide sequence of the pnp gene of Escherichia coli encoding
RT polynucleotide phosphorylase. Homology of the primary structure of the
RT protein with the RNA-binding domain of ribosomal protein S1.";
RL J. Biol. Chem. 262:63-68(1987).
RN [5]
RP PROTEIN SEQUENCE OF 47-78; 83-92; 137-145 AND 221-272, MUTAGENESIS OF
RP GLY-103; 282-GLY--GLN-294; 283-GLN--GLN-294 AND 284-ASP--GLN-294,
RP INTERACTION WITH PRC AND IBPB, DISRUPTION PHENOTYPE, AND IDENTIFICATION BY
RP MASS SPECTROMETRY.
RX PubMed=15047720; DOI=10.1093/jb/mvh022;
RA Tadokoro A., Hayashi H., Kishimoto T., Makino Y., Fujisaki S.,
RA Nishimura Y.;
RT "Interaction of the Escherichia coli lipoprotein NlpI with periplasmic Prc
RT (Tsp) protease.";
RL J. Biochem. 135:185-191(2004).
RN [6]
RP IDENTIFICATION.
RX PubMed=7984428; DOI=10.1093/nar/22.22.4756;
RA Borodovsky M., Rudd K.E., Koonin E.V.;
RT "Intrinsic and extrinsic approaches for detecting genes in a bacterial
RT genome.";
RL Nucleic Acids Res. 22:4756-4767(1994).
RN [7]
RP FUNCTION, INDUCTION, DIACYLGLYCEROL AT CYS-19, PALMITOYLATION AT CYS-19,
RP AND DISRUPTION PHENOTYPE.
RC STRAIN=K12;
RX PubMed=10400590; DOI=10.1128/jb.181.14.4318-4325.1999;
RA Ohara M., Wu H.C., Sankaran K., Rick P.D.;
RT "Identification and characterization of a new lipoprotein, NlpI, in
RT Escherichia coli K-12.";
RL J. Bacteriol. 181:4318-4325(1999).
RN [8]
RP DISRUPTION PHENOTYPE.
RX PubMed=16855227; DOI=10.1128/jb.00498-06;
RA McBroom A.J., Johnson A.P., Vemulapalli S., Kuehn M.J.;
RT "Outer membrane vesicle production by Escherichia coli is independent of
RT membrane instability.";
RL J. Bacteriol. 188:5385-5392(2006).
RN [9]
RP INDUCTION BY HIGH PRESSURE, AND DISRUPTION PHENOTYPE.
RX PubMed=16597971; DOI=10.1128/aem.72.4.2661-2671.2006;
RA Malone A.S., Chung Y.K., Yousef A.E.;
RT "Genes of Escherichia coli O157:H7 that are involved in high-pressure
RT resistance.";
RL Appl. Environ. Microbiol. 72:2661-2671(2006).
RN [10]
RP DISRUPTION PHENOTYPE.
RC STRAIN=K12 / BW25113;
RX PubMed=17122336; DOI=10.1128/jb.01294-06;
RA Inoue T., Shingaki R., Hirose S., Waki K., Mori H., Fukui K.;
RT "Genome-wide screening of genes required for swarming motility in
RT Escherichia coli K-12.";
RL J. Bacteriol. 189:950-957(2007).
RN [11]
RP DISRUPTION PHENOTYPE.
RX PubMed=17163978; DOI=10.1111/j.1365-2958.2006.05522.x;
RA McBroom A.J., Kuehn M.J.;
RT "Release of outer membrane vesicles by Gram-negative bacteria is a novel
RT envelope stress response.";
RL Mol. Microbiol. 63:545-558(2007).
RN [12]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=20833130; DOI=10.1016/j.bbrc.2010.09.026;
RA Sanchez-Torres V., Maeda T., Wood T.K.;
RT "Global regulator H-NS and lipoprotein NlpI influence production of
RT extracellular DNA in Escherichia coli.";
RL Biochem. Biophys. Res. Commun. 401:197-202(2010).
RN [13]
RP X-RAY CRYSTALLOGRAPHY (1.98 ANGSTROMS) OF 20-294, SUBUNIT, AND TPR REPEATS.
RX PubMed=15634341; DOI=10.1111/j.1432-1033.2004.04397.x;
RA Wilson C.G., Kajander T., Regan L.;
RT "The crystal structure of NlpI. A prokaryotic tetratricopeptide repeat
RT protein with a globular fold.";
RL FEBS J. 272:166-179(2005).
CC -!- FUNCTION: May be involved in cell division. May play a role in
CC bacterial septation or regulation of cell wall degradation during cell
CC division. Negatively controls the production of extracellular DNA
CC (eDNA). {ECO:0000269|PubMed:10400590, ECO:0000269|PubMed:20833130}.
CC -!- SUBUNIT: Homodimer. Interacts with Prc and IbpB.
CC {ECO:0000269|PubMed:15047720, ECO:0000269|PubMed:15634341}.
CC -!- SUBCELLULAR LOCATION: Cell membrane; Lipid-anchor.
CC -!- INDUCTION: By L-arabinose. By high-pressure at 400MPa for 5 minutes.
CC {ECO:0000269|PubMed:10400590, ECO:0000269|PubMed:16597971}.
CC -!- DISRUPTION PHENOTYPE: Highly sensitive to osmotic conditions in low-
CC salt medium and also thermosensitive under low-salt conditions. Shows
CC pronounced filamentation at 42 degree Celsius under low osmolarity, but
CC not at 30 or 37 degrees. Growth in low-salt medium is severely
CC restricted at 30 degrees and no growth is observed at 37 and 42 degree
CC Celsius. Shows increased eDNA production. Produces 100-fold more outer-
CC membrane vesicles making the organism more resistant to toxins, and
CC enhancing survival under stress. Higher sensitivity to ultra high
CC pressure than wild-type counterparts (PubMed:16597971). Strongly
CC represses cell swarming but no effect on cell swimming
CC (PubMed:17122336). {ECO:0000269|PubMed:10400590,
CC ECO:0000269|PubMed:15047720, ECO:0000269|PubMed:16597971,
CC ECO:0000269|PubMed:16855227, ECO:0000269|PubMed:17122336,
CC ECO:0000269|PubMed:17163978, ECO:0000269|PubMed:20833130}.
CC -!- MISCELLANEOUS: Processed by Prc protease in the C-terminus.
CC -!- SEQUENCE CAUTION:
CC Sequence=M63288; Type=Frameshift; Evidence={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; U18997; AAA57966.1; -; Genomic_DNA.
DR EMBL; U00096; AAC76197.1; -; Genomic_DNA.
DR EMBL; AP009048; BAE77209.1; -; Genomic_DNA.
DR EMBL; M63288; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; J02638; AAA83906.1; -; Genomic_DNA.
DR PIR; G65106; G65106.
DR RefSeq; NP_417632.1; NC_000913.3.
DR RefSeq; WP_000802080.1; NZ_STEB01000012.1.
DR PDB; 1XNF; X-ray; 1.98 A; A/B=20-294.
DR PDB; 5WQL; X-ray; 2.30 A; A/B=20-294.
DR PDB; 6IQQ; X-ray; 2.80 A; A/B=20-294.
DR PDB; 6IQS; X-ray; 2.69 A; A/B=20-294.
DR PDB; 6IQU; X-ray; 2.90 A; A=20-294.
DR PDBsum; 1XNF; -.
DR PDBsum; 5WQL; -.
DR PDBsum; 6IQQ; -.
DR PDBsum; 6IQS; -.
DR PDBsum; 6IQU; -.
DR AlphaFoldDB; P0AFB1; -.
DR SMR; P0AFB1; -.
DR BioGRID; 4262430; 258.
DR DIP; DIP-48051N; -.
DR IntAct; P0AFB1; 1.
DR STRING; 511145.b3163; -.
DR jPOST; P0AFB1; -.
DR PaxDb; P0AFB1; -.
DR PRIDE; P0AFB1; -.
DR EnsemblBacteria; AAC76197; AAC76197; b3163.
DR EnsemblBacteria; BAE77209; BAE77209; BAE77209.
DR GeneID; 67414899; -.
DR GeneID; 947673; -.
DR KEGG; ecj:JW3132; -.
DR KEGG; eco:b3163; -.
DR PATRIC; fig|1411691.4.peg.3567; -.
DR EchoBASE; EB2274; -.
DR eggNOG; COG4785; Bacteria.
DR HOGENOM; CLU_071600_0_0_6; -.
DR InParanoid; P0AFB1; -.
DR OMA; VEHRYSF; -.
DR PhylomeDB; P0AFB1; -.
DR BioCyc; EcoCyc:EG12371-MON; -.
DR EvolutionaryTrace; P0AFB1; -.
DR PRO; PR:P0AFB1; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; Chromosome.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0030674; F:protein-macromolecule adaptor activity; IDA:EcoCyc.
DR GO; GO:0007049; P:cell cycle; IEA:UniProtKB-KW.
DR GO; GO:0051301; P:cell division; IMP:EcoCyc.
DR GO; GO:0000270; P:peptidoglycan metabolic process; IDA:EcoCyc.
DR Gene3D; 1.25.40.10; -; 1.
DR InterPro; IPR023605; Lipoprotein_NlpI.
DR InterPro; IPR011990; TPR-like_helical_dom_sf.
DR InterPro; IPR013105; TPR_2.
DR InterPro; IPR019734; TPR_repeat.
DR Pfam; PF07719; TPR_2; 1.
DR Pfam; PF13181; TPR_8; 1.
DR PIRSF; PIRSF004654; NlpI; 1.
DR SMART; SM00028; TPR; 3.
DR SUPFAM; SSF48452; SSF48452; 1.
DR PROSITE; PS51257; PROKAR_LIPOPROTEIN; 1.
DR PROSITE; PS50005; TPR; 3.
DR PROSITE; PS50293; TPR_REGION; 2.
PE 1: Evidence at protein level;
KW 3D-structure; Cell cycle; Cell division; Cell membrane;
KW Direct protein sequencing; Lipoprotein; Membrane; Palmitate;
KW Reference proteome; Repeat; Signal; TPR repeat.
FT SIGNAL 1..18
FT CHAIN 19..294
FT /note="Lipoprotein NlpI"
FT /id="PRO_0000035692"
FT REPEAT 62..95
FT /note="TPR 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00339,
FT ECO:0000269|PubMed:15634341"
FT REPEAT 96..129
FT /note="TPR 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00339,
FT ECO:0000269|PubMed:15634341"
FT REPEAT 234..267
FT /note="TPR 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00339,
FT ECO:0000269|PubMed:15634341"
FT LIPID 19
FT /note="N-palmitoyl cysteine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00303,
FT ECO:0000269|PubMed:10400590"
FT LIPID 19
FT /note="S-diacylglycerol cysteine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00303,
FT ECO:0000269|PubMed:10400590"
FT MUTAGEN 103
FT /note="G->D: Loss of interaction with Prc and IbpB leading
FT to thermosensitivity."
FT /evidence="ECO:0000269|PubMed:15047720"
FT MUTAGEN 282..294
FT /note="Missing: Loss of activity leading to
FT thermosensitivity."
FT /evidence="ECO:0000269|PubMed:15047720"
FT MUTAGEN 283..294
FT /note="Missing: No phenotype."
FT /evidence="ECO:0000269|PubMed:15047720"
FT MUTAGEN 284..294
FT /note="Missing: No phenotype."
FT /evidence="ECO:0000269|PubMed:15047720"
FT HELIX 27..29
FT /evidence="ECO:0007829|PDB:1XNF"
FT HELIX 38..51
FT /evidence="ECO:0007829|PDB:1XNF"
FT HELIX 58..74
FT /evidence="ECO:0007829|PDB:1XNF"
FT HELIX 78..91
FT /evidence="ECO:0007829|PDB:1XNF"
FT HELIX 96..108
FT /evidence="ECO:0007829|PDB:1XNF"
FT HELIX 112..125
FT /evidence="ECO:0007829|PDB:1XNF"
FT HELIX 131..142
FT /evidence="ECO:0007829|PDB:1XNF"
FT HELIX 146..159
FT /evidence="ECO:0007829|PDB:1XNF"
FT HELIX 164..177
FT /evidence="ECO:0007829|PDB:1XNF"
FT HELIX 179..192
FT /evidence="ECO:0007829|PDB:1XNF"
FT HELIX 199..206
FT /evidence="ECO:0007829|PDB:1XNF"
FT HELIX 212..222
FT /evidence="ECO:0007829|PDB:1XNF"
FT HELIX 226..246
FT /evidence="ECO:0007829|PDB:1XNF"
FT HELIX 250..261
FT /evidence="ECO:0007829|PDB:1XNF"
FT HELIX 269..283
FT /evidence="ECO:0007829|PDB:1XNF"
SQ SEQUENCE 294 AA; 33621 MW; 4CA6724327A9CEE7 CRC64;
MKPFLRWCFV ATALTLAGCS NTSWRKSEVL AVPLQPTLQQ EVILARMEQI LASRALTDDE
RAQLLYERGV LYDSLGLRAL ARNDFSQALA IRPDMPEVFN YLGIYLTQAG NFDAAYEAFD
SVLELDPTYN YAHLNRGIAL YYGGRDKLAQ DDLLAFYQDD PNDPFRSLWL YLAEQKLDEK
QAKEVLKQHF EKSDKEQWGW NIVEFYLGNI SEQTLMERLK ADATDNTSLA EHLSETNFYL
GKYYLSLGDL DSATALFKLA VANNVHNFVE HRYALLELSL LGQDQDDLAE SDQQ
