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Protein

Lipopolysaccharide assembly protein B

Gene

lapB

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

Functioni

Modulates cellular lipopolysaccharide (LPS) levels by regulating LpxC, which is involved in lipid A biosynthesis. May act by modulating the proteolytic activity of FtsH towards LpxC. May also coordinate assembly of proteins involved in LPS synthesis at the plasma membrane.UniRule annotation2 Publications

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi357 – 3571IronUniRule annotation1 Publication
Metal bindingi360 – 3601IronUniRule annotation1 Publication
Metal bindingi371 – 3711IronUniRule annotation1 Publication
Metal bindingi374 – 3741IronUniRule annotation1 Publication

GO - Molecular functioni

  • iron ion binding Source: UniProtKB-HAMAP
  • metal ion binding Source: EcoCyc

GO - Biological processi

  • lipopolysaccharide metabolic process Source: EcoCyc
  • regulation of lipid biosynthetic process Source: UniProtKB-HAMAP
Complete GO annotation...

Keywords - Biological processi

Stress response

Keywords - Ligandi

Iron, Metal-binding

Enzyme and pathway databases

BioCyciEcoCyc:EG12691-MONOMER.
ECOL316407:JW1272-MONOMER.

Names & Taxonomyi

Protein namesi
Recommended name:
Lipopolysaccharide assembly protein B1 PublicationUniRule annotation
Alternative name(s):
Lipopolysaccharide regulatory proteinUniRule annotation
Gene namesi
Name:lapB1 PublicationUniRule annotation
Synonyms:yciM
Ordered Locus Names:b1280, JW1272
OrganismiEscherichia coli (strain K12)
Taxonomic identifieri83333 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia
Proteomesi
  • UP000000318 Componenti: Chromosome
  • UP000000625 Componenti: Chromosome

Organism-specific databases

EcoGeneiEG12691. yciM.

Subcellular locationi

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Transmembranei1 – 2020HelicalUniRule annotation1 PublicationAdd
BLAST
Topological domaini21 – 389369CytoplasmicUniRule annotation1 PublicationAdd
BLAST

GO - Cellular componenti

  • cytosol Source: EcoCyc
  • integral component of plasma membrane Source: EcoCyc
  • intrinsic component of the cytoplasmic side of the plasma membrane Source: UniProtKB-HAMAP
Complete GO annotation...

Keywords - Cellular componenti

Cell inner membrane, Cell membrane, Membrane

Pathology & Biotechi

Disruption phenotypei

Deletion leads to changes in cell morphology and to the formation of bulges that contain cytoplasmic material and cause cell lysis. Mutants exhibit increased sensitivity to rifampicin and novobiocin, and to a mixture of SDS and EDTA. Growth is severely affected by osmolarity and temperature (PubMed:24187084). Mutant accumulates precursor forms of LPS and exhibits elevated levels of LpxC (PubMed:24722986).2 Publications

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi184 – 1841C → S: Does not affect metal binding; when associated with S-258. 1 Publication
Mutagenesisi258 – 2581C → S: Does not affect metal binding; when associated with S-184. 1 Publication
Mutagenesisi357 – 3571C → S: Lack of activity; when associated with S-360; S-371 and S-374. 1 Publication
Mutagenesisi360 – 3601C → S: Lack of activity; when associated with S-357; S-371 and S-374. 1 Publication
Mutagenesisi371 – 3711C → R: Lack of activity. 1 Publication
Mutagenesisi371 – 3711C → S: Lack of activity; when associated with S-357; S-360 and S-374. 1 Publication
Mutagenesisi372 – 3721P → L: Lack of activity. 1 Publication
Mutagenesisi374 – 3741C → S: Lack of activity; when associated with S-357; S-360 and S-371. 1 Publication
Mutagenesisi378 – 3781S → P: Lack of activity. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 389389Lipopolysaccharide assembly protein BPRO_0000013830Add
BLAST

Proteomic databases

PaxDbiP0AB58.

Expressioni

Inductioni

Induced by heat shock, via RpoH.2 Publications

Interactioni

Protein-protein interaction databases

BioGridi4259400. 42 interactions.
DIPiDIP-48161N.
IntActiP0AB58. 1 interaction.
STRINGi511145.b1280.

Structurei

3D structure databases

ProteinModelPortaliP0AB58.
SMRiP0AB58. Positions 210-317.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Repeati35 – 6834TPR 1UniRule annotationAdd
BLAST
Repeati69 – 10234TPR 2UniRule annotationAdd
BLAST
Repeati107 – 14034TPR 3UniRule annotationAdd
BLAST
Repeati142 – 17433TPR 4UniRule annotationAdd
BLAST
Repeati180 – 21334TPR 5UniRule annotationAdd
BLAST
Repeati214 – 24734TPR 6UniRule annotationAdd
BLAST
Repeati249 – 28234TPR 7UniRule annotationAdd
BLAST

Domaini

The membrane anchor N-terminal domain is required for activity. The iron-binding domain is required for protein stability and function.1 Publication

Sequence similaritiesi

Belongs to the LapB family.UniRule annotationCurated
Contains 7 TPR repeats.UniRule annotation

Keywords - Domaini

Repeat, TPR repeat, Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiENOG4105CFV. Bacteria.
COG2956. LUCA.
HOGENOMiHOG000257806.
InParanoidiP0AB58.
KOiK19804.
OMAiRYRCAAC.
PhylomeDBiP0AB58.

Family and domain databases

Gene3Di1.25.40.10. 3 hits.
HAMAPiMF_00994. LPS_assembly_LapB. 1 hit.
InterProiIPR030865. LapB.
IPR013026. TPR-contain_dom.
IPR011990. TPR-like_helical_dom.
IPR019734. TPR_repeat.
[Graphical view]
SMARTiSM00028. TPR. 5 hits.
[Graphical view]
SUPFAMiSSF48452. SSF48452. 2 hits.
PROSITEiPS50005. TPR. 6 hits.
PS50293. TPR_REGION. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P0AB58-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MLELLFLLLP VAAAYGWYMG RRSAQQNKQD EANRLSRDYV AGVNFLLSNQ
60 70 80 90 100
QDKAVDLFLD MLKEDTGTVE AHLTLGNLFR SRGEVDRAIR IHQTLMESAS
110 120 130 140 150
LTYEQRLLAI QQLGRDYMAA GLYDRAEDMF NQLTDETDFR IGALQQLLQI
160 170 180 190 200
YQATSEWQKA IDVAERLVKL GKDKQRVEIA HFYCELALQH MASDDLDRAM
210 220 230 240 250
TLLKKGAAAD KNSARVSIMM GRVFMAKGEY AKAVESLQRV ISQDRELVSE
260 270 280 290 300
TLEMLQTCYQ QLGKTAEWAE FLQRAVEENT GADAELMLAD IIEARDGSEA
310 320 330 340 350
AQVYITRQLQ RHPTMRVFHK LMDYHLNEAE EGRAKESLMV LRDMVGEKVR
360 370 380
SKPRYRCQKC GFTAYTLYWH CPSCRAWSTI KPIRGLDGL
Length:389
Mass (Da):44,531
Last modified:October 11, 2005 - v1
Checksum:iF4D1B9E2A526BCC3
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U00096 Genomic DNA. Translation: AAC74362.1.
AP009048 Genomic DNA. Translation: BAA14834.1.
M23250 Genomic DNA. No translation available.
PIRiC64876.
RefSeqiNP_415796.1. NC_000913.3.
WP_000891353.1. NZ_LN832404.1.

Genome annotation databases

EnsemblBacteriaiAAC74362; AAC74362; b1280.
BAA14834; BAA14834; BAA14834.
GeneIDi944858.
KEGGiecj:JW1272.
eco:b1280.
PATRICi32117822. VBIEscCol129921_1331.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U00096 Genomic DNA. Translation: AAC74362.1.
AP009048 Genomic DNA. Translation: BAA14834.1.
M23250 Genomic DNA. No translation available.
PIRiC64876.
RefSeqiNP_415796.1. NC_000913.3.
WP_000891353.1. NZ_LN832404.1.

3D structure databases

ProteinModelPortaliP0AB58.
SMRiP0AB58. Positions 210-317.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi4259400. 42 interactions.
DIPiDIP-48161N.
IntActiP0AB58. 1 interaction.
STRINGi511145.b1280.

Proteomic databases

PaxDbiP0AB58.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAC74362; AAC74362; b1280.
BAA14834; BAA14834; BAA14834.
GeneIDi944858.
KEGGiecj:JW1272.
eco:b1280.
PATRICi32117822. VBIEscCol129921_1331.

Organism-specific databases

EchoBASEiEB2554.
EcoGeneiEG12691. yciM.

Phylogenomic databases

eggNOGiENOG4105CFV. Bacteria.
COG2956. LUCA.
HOGENOMiHOG000257806.
InParanoidiP0AB58.
KOiK19804.
OMAiRYRCAAC.
PhylomeDBiP0AB58.

Enzyme and pathway databases

BioCyciEcoCyc:EG12691-MONOMER.
ECOL316407:JW1272-MONOMER.

Miscellaneous databases

PROiP0AB58.

Family and domain databases

Gene3Di1.25.40.10. 3 hits.
HAMAPiMF_00994. LPS_assembly_LapB. 1 hit.
InterProiIPR030865. LapB.
IPR013026. TPR-contain_dom.
IPR011990. TPR-like_helical_dom.
IPR019734. TPR_repeat.
[Graphical view]
SMARTiSM00028. TPR. 5 hits.
[Graphical view]
SUPFAMiSSF48452. SSF48452. 2 hits.
PROSITEiPS50005. TPR. 6 hits.
PS50293. TPR_REGION. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiLAPB_ECOLI
AccessioniPrimary (citable) accession number: P0AB58
Secondary accession number(s): P45576, P76836
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 11, 2005
Last sequence update: October 11, 2005
Last modified: September 7, 2016
This is version 84 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Escherichia coli
    Escherichia coli (strain K12): entries and cross-references to EcoGene
  2. 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.