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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 lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacteralesEnterobacteriaceaeEscherichia
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)DescriptionActionsGraphical viewLength
Mutagenesisi103G → D: Loss of interaction with Prc and IbpB leading to thermosensitivity. 1 Publication1
Mutagenesisi282 – 294Missing : Loss of activity leading to thermosensitivity. 1 PublicationAdd BLAST13
Mutagenesisi283 – 294Missing : No phenotype. 1 PublicationAdd BLAST12
Mutagenesisi284 – 294Missing : No phenotype. 1 PublicationAdd BLAST11

Chemistry databases

DrugBankiDB03754. Tris.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Signal peptidei1 – 18Add BLAST18
ChainiPRO_000003569219 – 294Lipoprotein NlpIAdd BLAST276

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Lipidationi19N-palmitoyl cysteinePROSITE-ProRule annotation1 Publication1
Lipidationi19S-diacylglycerol cysteinePROSITE-ProRule annotation1 Publication1

Keywords - PTMi

Lipoprotein, Palmitate

Proteomic databases

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 interactors.
DIPiDIP-48051N.
IntActiP0AFB1. 1 interactor.
STRINGi511145.b3163.

Structurei

Secondary structure

1294
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi27 – 29Combined sources3
Helixi38 – 51Combined sources14
Helixi58 – 74Combined sources17
Helixi78 – 91Combined sources14
Helixi96 – 108Combined sources13
Helixi112 – 125Combined sources14
Helixi131 – 142Combined sources12
Helixi146 – 159Combined sources14
Helixi164 – 177Combined sources14
Helixi179 – 192Combined sources14
Helixi199 – 206Combined sources8
Helixi212 – 222Combined sources11
Helixi226 – 246Combined sources21
Helixi250 – 261Combined sources12
Helixi269 – 283Combined sources15

3D structure databases

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

Miscellaneous databases

EvolutionaryTraceiP0AFB1.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Repeati62 – 95TPR 1PROSITE-ProRule annotation1 PublicationAdd BLAST34
Repeati96 – 129TPR 2PROSITE-ProRule annotation1 PublicationAdd BLAST34
Repeati234 – 267TPR 3PROSITE-ProRule annotation1 PublicationAdd BLAST34

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.
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
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1XNFX-ray1.98A/B20-294[»]
ProteinModelPortaliP0AFB1.
SMRiP0AFB1.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi4262430. 258 interactors.
DIPiDIP-48051N.
IntActiP0AFB1. 1 interactor.
STRINGi511145.b3163.

Chemistry databases

DrugBankiDB03754. Tris.

Proteomic databases

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.
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...

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: November 2, 2016
This is version 94 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.