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: -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

Miscellaneous

Processed by Prc protease in the C-terminus.

GO - Molecular functioni

  • protein binding, bridging Source: EcoCyc

GO - Biological processi

  • cell cycle Source: UniProtKB-KW
  • cell division Source: EcoCyc

Keywordsi

Biological processCell cycle, Cell division

Enzyme and pathway databases

BioCyciEcoCyc:EG12371-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

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
STRINGi316385.ECDH10B_3336

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[»]
5WQLX-ray2.30A/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

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
InterProiView protein in InterPro
IPR023605 Lipoprotein_NlpI
IPR013026 TPR-contain_dom
IPR011990 TPR-like_helical_dom_sf
IPR013105 TPR_2
IPR019734 TPR_repeat
PfamiView protein in Pfam
PF07719 TPR_2, 1 hit
PF13181 TPR_8, 1 hit
PIRSFiPIRSF004654 NlpI, 1 hit
SMARTiView protein in SMART
SM00028 TPR, 3 hits
SUPFAMiSSF48452 SSF48452, 1 hit
PROSITEiView protein in PROSITE
PS51257 PROKAR_LIPOPROTEIN, 1 hit
PS50005 TPR, 3 hits
PS50293 TPR_REGION, 2 hits

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
PATRICifig|1411691.4.peg.3567

Similar proteinsi

Entry informationi

Entry nameiNLPI_ECOLI
AccessioniPrimary (citable) accession number: P0AFB1
Secondary accession number(s): P39833, Q2M947
Entry historyiIntegrated into UniProtKB/Swiss-Prot: December 20, 2005
Last sequence update: December 20, 2005
Last modified: March 28, 2018
This is version 101 of the entry and version 1 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

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

Cookie policy

We would like to use anonymized google analytics cookies to gather statistics on how uniprot.org is used in aggregate. Learn more

UniProt is an ELIXIR core data resource
Main funding by: National Institutes of Health