Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

Lipoprotein NlpI

Gene

nlpI

Organism
Escherichia coli (strain K12)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

May be involved in cell division. May play a role in bacterial septation or regulation of cell wall degradation during cell division. Negatively controls the production of extracellular DNA (eDNA).2 Publications

GO - Molecular functioni

  • protein binding, bridging Source: EcoCyc

GO - Biological processi

  • cell cycle Source: UniProtKB-KW
  • cell division Source: EcoCyc
Complete GO annotation...

Keywords - Biological processi

Cell cycle, Cell division

Enzyme and pathway databases

BioCyciEcoCyc:EG12371-MONOMER.
ECOL316407:JW3132-MONOMER.

Names & Taxonomyi

Protein namesi
Recommended name:
Lipoprotein NlpI
Gene namesi
Name:nlpI
Synonyms:yhbM
Ordered Locus Names:b3163, JW3132
OrganismiEscherichia coli (strain K12)
Taxonomic identifieri83333 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia
Proteomesi
  • UP000000318 Componenti: Chromosome
  • UP000000625 Componenti: Chromosome

Organism-specific databases

EcoGeneiEG12371. nlpI.

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cell membrane, Membrane

Pathology & Biotechi

Disruption phenotypei

Highly sensitive to osmotic conditions in low-salt medium and also thermosensitive under low-salt conditions. Shows pronounced filamentation at 42 degree Celsius under low osmolarity, but not at 30 or 37 degrees. Growth in low-salt medium is severely restricted at 30 degrees and no growth is observed at 37 and 42 degree Celsius. Shows increased eDNA production. Produces 100-fold more outer-membrane vesicles making the organism more resistant to toxins, and enhancing survival under stress. Higher sensitivity to ultra high pressure than wild-type counterparts (PubMed:16597971). Strongly represses cell swarming but no effect on cell swimming (PubMed:17122336).7 Publications

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi103 – 1031G → D: Loss of interaction with Prc and IbpB leading to thermosensitivity. 1 Publication
Mutagenesisi282 – 29413Missing : Loss of activity leading to thermosensitivity. 1 PublicationAdd
BLAST
Mutagenesisi283 – 29412Missing : No phenotype. 1 PublicationAdd
BLAST
Mutagenesisi284 – 29411Missing : No phenotype. 1 PublicationAdd
BLAST

Chemistry

DrugBankiDB03754. Tris.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 1818Add
BLAST
Chaini19 – 294276Lipoprotein NlpIPRO_0000035692Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Lipidationi19 – 191N-palmitoyl cysteinePROSITE-ProRule annotation1 Publication
Lipidationi19 – 191S-diacylglycerol cysteinePROSITE-ProRule annotation1 Publication

Keywords - PTMi

Lipoprotein, Palmitate

Proteomic databases

EPDiP0AFB1.
PaxDbiP0AFB1.
PRIDEiP0AFB1.

Expressioni

Inductioni

By L-arabinose. By high-pressure at 400MPa for 5 minutes.2 Publications

Interactioni

Subunit structurei

Homodimer. Interacts with Prc and IbpB.2 Publications

GO - Molecular functioni

  • protein binding, bridging Source: EcoCyc

Protein-protein interaction databases

BioGridi4262430. 258 interactions.
DIPiDIP-48051N.
IntActiP0AFB1. 1 interaction.
STRINGi511145.b3163.

Structurei

Secondary structure

1
294
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi27 – 293Combined sources
Helixi38 – 5114Combined sources
Helixi58 – 7417Combined sources
Helixi78 – 9114Combined sources
Helixi96 – 10813Combined sources
Helixi112 – 12514Combined sources
Helixi131 – 14212Combined sources
Helixi146 – 15914Combined sources
Helixi164 – 17714Combined sources
Helixi179 – 19214Combined sources
Helixi199 – 2068Combined sources
Helixi212 – 22211Combined sources
Helixi226 – 24621Combined sources
Helixi250 – 26112Combined sources
Helixi269 – 28315Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1XNFX-ray1.98A/B20-294[»]
ProteinModelPortaliP0AFB1.
SMRiP0AFB1. Positions 23-284.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP0AFB1.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Repeati62 – 9534TPR 1PROSITE-ProRule annotation1 PublicationAdd
BLAST
Repeati96 – 12934TPR 2PROSITE-ProRule annotation1 PublicationAdd
BLAST
Repeati234 – 26734TPR 3PROSITE-ProRule annotation1 PublicationAdd
BLAST

Sequence similaritiesi

Contains 3 TPR repeats.PROSITE-ProRule annotation

Keywords - Domaini

Repeat, Signal, TPR repeat

Phylogenomic databases

eggNOGiENOG4105RT1. Bacteria.
COG4785. LUCA.
HOGENOMiHOG000276076.
InParanoidiP0AFB1.
KOiK05803.
OMAiYEAFDST.
OrthoDBiEOG6P8TKS.
PhylomeDBiP0AFB1.

Family and domain databases

Gene3Di1.25.40.10. 1 hit.
InterProiIPR023605. Lipoprotein_NlpI.
IPR013026. TPR-contain_dom.
IPR011990. TPR-like_helical_dom.
IPR013105. TPR_2.
IPR019734. TPR_repeat.
[Graphical view]
PfamiPF07719. TPR_2. 1 hit.
PF13181. TPR_8. 1 hit.
[Graphical view]
PIRSFiPIRSF004654. NlpI. 1 hit.
SMARTiSM00028. TPR. 3 hits.
[Graphical view]
SUPFAMiSSF48452. SSF48452. 1 hit.
PROSITEiPS51257. PROKAR_LIPOPROTEIN. 1 hit.
PS50005. TPR. 3 hits.
PS50293. TPR_REGION. 2 hits.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

P0AFB1-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MKPFLRWCFV ATALTLAGCS NTSWRKSEVL AVPLQPTLQQ EVILARMEQI
60 70 80 90 100
LASRALTDDE RAQLLYERGV LYDSLGLRAL ARNDFSQALA IRPDMPEVFN
110 120 130 140 150
YLGIYLTQAG NFDAAYEAFD SVLELDPTYN YAHLNRGIAL YYGGRDKLAQ
160 170 180 190 200
DDLLAFYQDD PNDPFRSLWL YLAEQKLDEK QAKEVLKQHF EKSDKEQWGW
210 220 230 240 250
NIVEFYLGNI SEQTLMERLK ADATDNTSLA EHLSETNFYL GKYYLSLGDL
260 270 280 290
DSATALFKLA VANNVHNFVE HRYALLELSL LGQDQDDLAE SDQQ
Length:294
Mass (Da):33,621
Last modified:December 20, 2005 - v1
Checksum:i4CA6724327A9CEE7
GO

Sequence cautioni

The sequence M63288 differs from that shown. Reason: Frameshift at several positions. Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U18997 Genomic DNA. Translation: AAA57966.1.
U00096 Genomic DNA. Translation: AAC76197.1.
AP009048 Genomic DNA. Translation: BAE77209.1.
M63288 Genomic DNA. No translation available.
J02638 Genomic DNA. Translation: AAA83906.1.
PIRiG65106.
RefSeqiNP_417632.1. NC_000913.3.
WP_000802080.1. NZ_LN832404.1.

Genome annotation databases

EnsemblBacteriaiAAC76197; AAC76197; b3163.
BAE77209; BAE77209; BAE77209.
GeneIDi947673.
KEGGiecj:JW3132.
eco:b3163.
PATRICi32121744. VBIEscCol129921_3258.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U18997 Genomic DNA. Translation: AAA57966.1.
U00096 Genomic DNA. Translation: AAC76197.1.
AP009048 Genomic DNA. Translation: BAE77209.1.
M63288 Genomic DNA. No translation available.
J02638 Genomic DNA. Translation: AAA83906.1.
PIRiG65106.
RefSeqiNP_417632.1. NC_000913.3.
WP_000802080.1. NZ_LN832404.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1XNFX-ray1.98A/B20-294[»]
ProteinModelPortaliP0AFB1.
SMRiP0AFB1. Positions 23-284.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi4262430. 258 interactions.
DIPiDIP-48051N.
IntActiP0AFB1. 1 interaction.
STRINGi511145.b3163.

Chemistry

DrugBankiDB03754. Tris.

Proteomic databases

EPDiP0AFB1.
PaxDbiP0AFB1.
PRIDEiP0AFB1.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAC76197; AAC76197; b3163.
BAE77209; BAE77209; BAE77209.
GeneIDi947673.
KEGGiecj:JW3132.
eco:b3163.
PATRICi32121744. VBIEscCol129921_3258.

Organism-specific databases

EchoBASEiEB2274.
EcoGeneiEG12371. nlpI.

Phylogenomic databases

eggNOGiENOG4105RT1. Bacteria.
COG4785. LUCA.
HOGENOMiHOG000276076.
InParanoidiP0AFB1.
KOiK05803.
OMAiYEAFDST.
OrthoDBiEOG6P8TKS.
PhylomeDBiP0AFB1.

Enzyme and pathway databases

BioCyciEcoCyc:EG12371-MONOMER.
ECOL316407:JW3132-MONOMER.

Miscellaneous databases

EvolutionaryTraceiP0AFB1.
PROiP0AFB1.

Family and domain databases

Gene3Di1.25.40.10. 1 hit.
InterProiIPR023605. Lipoprotein_NlpI.
IPR013026. TPR-contain_dom.
IPR011990. TPR-like_helical_dom.
IPR013105. TPR_2.
IPR019734. TPR_repeat.
[Graphical view]
PfamiPF07719. TPR_2. 1 hit.
PF13181. TPR_8. 1 hit.
[Graphical view]
PIRSFiPIRSF004654. NlpI. 1 hit.
SMARTiSM00028. TPR. 3 hits.
[Graphical view]
SUPFAMiSSF48452. SSF48452. 1 hit.
PROSITEiPS51257. PROKAR_LIPOPROTEIN. 1 hit.
PS50005. TPR. 3 hits.
PS50293. TPR_REGION. 2 hits.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: K12 / MG1655 / ATCC 47076.
  2. "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655 and W3110."
    Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S., Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.
    Mol. Syst. Biol. 2:E1-E5(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
  3. "deaD, a new Escherichia coli gene encoding a presumed ATP-dependent RNA helicase, can suppress a mutation in rpsB, the gene encoding ribosomal protein S2."
    Toone W.M., Rudd K.E., Friesen J.D.
    J. Bacteriol. 173:3291-3302(1991) [PubMed] [Europe PMC] [Abstract]
    Cited for: PRELIMINARY NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  4. "Nucleotide sequence of the pnp gene of Escherichia coli encoding polynucleotide phosphorylase. Homology of the primary structure of the protein with the RNA-binding domain of ribosomal protein S1."
    Regnier P., Grunberg-Manago M., Portier C.
    J. Biol. Chem. 262:63-68(1987) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-41.
    Strain: JCH5/JC553.
  5. "Interaction of the Escherichia coli lipoprotein NlpI with periplasmic Prc (Tsp) protease."
    Tadokoro A., Hayashi H., Kishimoto T., Makino Y., Fujisaki S., Nishimura Y.
    J. Biochem. 135:185-191(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 47-78; 83-92; 137-145 AND 221-272, MUTAGENESIS OF GLY-103; 282-GLY--GLN-294; 283-GLN--GLN-294 AND 284-ASP--GLN-294, INTERACTION WITH PRC AND IBPB, DISRUPTION PHENOTYPE, IDENTIFICATION BY MASS SPECTROMETRY.
  6. "Intrinsic and extrinsic approaches for detecting genes in a bacterial genome."
    Borodovsky M., Rudd K.E., Koonin E.V.
    Nucleic Acids Res. 22:4756-4767(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION.
  7. "Identification and characterization of a new lipoprotein, NlpI, in Escherichia coli K-12."
    Ohara M., Wu H.C., Sankaran K., Rick P.D.
    J. Bacteriol. 181:4318-4325(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INDUCTION, DIACYLGLYCEROL AT CYS-19, PALMITOYLATION AT CYS-19, DISRUPTION PHENOTYPE.
    Strain: K12.
  8. "Outer membrane vesicle production by Escherichia coli is independent of membrane instability."
    McBroom A.J., Johnson A.P., Vemulapalli S., Kuehn M.J.
    J. Bacteriol. 188:5385-5392(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: DISRUPTION PHENOTYPE.
  9. "Genes of Escherichia coli O157:H7 that are involved in high-pressure resistance."
    Malone A.S., Chung Y.K., Yousef A.E.
    Appl. Environ. Microbiol. 72:2661-2671(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: INDUCTION BY HIGH PRESSURE, DISRUPTION PHENOTYPE.
  10. "Genome-wide screening of genes required for swarming motility in Escherichia coli K-12."
    Inoue T., Shingaki R., Hirose S., Waki K., Mori H., Fukui K.
    J. Bacteriol. 189:950-957(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: DISRUPTION PHENOTYPE.
    Strain: K12 / BW25113.
  11. "Release of outer membrane vesicles by Gram-negative bacteria is a novel envelope stress response."
    McBroom A.J., Kuehn M.J.
    Mol. Microbiol. 63:545-558(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: DISRUPTION PHENOTYPE.
  12. "Global regulator H-NS and lipoprotein NlpI influence production of extracellular DNA in Escherichia coli."
    Sanchez-Torres V., Maeda T., Wood T.K.
    Biochem. Biophys. Res. Commun. 401:197-202(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, DISRUPTION PHENOTYPE.
  13. "The crystal structure of NlpI. A prokaryotic tetratricopeptide repeat protein with a globular fold."
    Wilson C.G., Kajander T., Regan L.
    FEBS J. 272:166-179(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.98 ANGSTROMS) OF 20-294, SUBUNIT, TPR REPEATS.

Entry informationi

Entry nameiNLPI_ECOLI
AccessioniPrimary (citable) accession number: P0AFB1
Secondary accession number(s): P39833, Q2M947
Entry historyi
Integrated into UniProtKB/Swiss-Prot: December 20, 2005
Last sequence update: December 20, 2005
Last modified: May 11, 2016
This is version 91 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Miscellaneous

Processed by Prc protease in the C-terminus.

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. Escherichia coli
    Escherichia coli (strain K12): entries and cross-references to EcoGene
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.