UniProtKB - P0AB58 (LAPB_ECOLI)
Protein
Lipopolysaccharide assembly protein B
Gene
lapB
Organism
Escherichia coli (strain K12)
Status
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 key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Metal bindingi | 357 | IronUniRule annotation1 Publication | 1 | |
Metal bindingi | 360 | IronUniRule annotation1 Publication | 1 | |
Metal bindingi | 371 | IronUniRule annotation1 Publication | 1 | |
Metal bindingi | 374 | IronUniRule annotation1 Publication | 1 |
GO - Molecular functioni
- iron ion binding Source: UniProtKB-UniRule
- metal ion binding Source: EcoCyc
GO - Biological processi
- cell division Source: GO_Central
- lipopolysaccharide metabolic process Source: InterPro
- regulation of lipid biosynthetic process Source: UniProtKB-UniRule
Keywordsi
Biological process | Stress response |
Ligand | Iron, Metal-binding |
Enzyme and pathway databases
BioCyci | EcoCyc:EG12691-MONOMER |
Names & Taxonomyi
Protein namesi | Recommended name: Lipopolysaccharide assembly protein B1 PublicationUniRule annotationAlternative name(s): Lipopolysaccharide regulatory proteinUniRule annotation |
Gene namesi | Name:lapB1 PublicationUniRule annotation Synonyms:yciM Ordered Locus Names:b1280, JW1272 |
Organismi | Escherichia coli (strain K12) |
Taxonomic identifieri | 83333 [NCBI] |
Taxonomic lineagei | Bacteria › Proteobacteria › Gammaproteobacteria › Enterobacterales › Enterobacteriaceae › Escherichia › |
Proteomesi |
|
Subcellular locationi
- Cell inner membrane UniRule annotation2 Publications; Single-pass membrane protein UniRule annotation1 Publication; Cytoplasmic side UniRule annotation1 Publication
Topology
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Transmembranei | 1 – 20 | HelicalUniRule annotation1 PublicationAdd BLAST | 20 | |
Topological domaini | 21 – 389 | CytoplasmicUniRule annotation1 PublicationAdd BLAST | 369 |
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-UniRule
Keywords - Cellular componenti
Cell inner membrane, Cell membrane, MembranePathology & 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 key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Mutagenesisi | 184 | C → S: Does not affect metal binding; when associated with S-258. 1 Publication | 1 | |
Mutagenesisi | 258 | C → S: Does not affect metal binding; when associated with S-184. 1 Publication | 1 | |
Mutagenesisi | 357 | C → S: Lack of activity; when associated with S-360; S-371 and S-374. 1 Publication | 1 | |
Mutagenesisi | 360 | C → S: Lack of activity; when associated with S-357; S-371 and S-374. 1 Publication | 1 | |
Mutagenesisi | 371 | C → R: Lack of activity. 1 Publication | 1 | |
Mutagenesisi | 371 | C → S: Lack of activity; when associated with S-357; S-360 and S-374. 1 Publication | 1 | |
Mutagenesisi | 372 | P → L: Lack of activity. 1 Publication | 1 | |
Mutagenesisi | 374 | C → S: Lack of activity; when associated with S-357; S-360 and S-371. 1 Publication | 1 | |
Mutagenesisi | 378 | S → P: Lack of activity. 1 Publication | 1 |
PTM / Processingi
Molecule processing
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
ChainiPRO_0000013830 | 1 – 389 | Lipopolysaccharide assembly protein BAdd BLAST | 389 |
Proteomic databases
jPOSTi | P0AB58 |
PaxDbi | P0AB58 |
PRIDEi | P0AB58 |
Expressioni
Inductioni
Induced by heat shock, via RpoH.2 Publications
Interactioni
Protein-protein interaction databases
BioGRIDi | 4259400, 56 interactors |
DIPi | DIP-48161N |
IntActi | P0AB58, 1 interactor |
STRINGi | 511145.b1280 |
Family & Domainsi
Domains and Repeats
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Repeati | 35 – 68 | TPR 1UniRule annotationAdd BLAST | 34 | |
Repeati | 69 – 102 | TPR 2UniRule annotationAdd BLAST | 34 | |
Repeati | 107 – 140 | TPR 3UniRule annotationAdd BLAST | 34 | |
Repeati | 142 – 174 | TPR 4UniRule annotationAdd BLAST | 33 | |
Repeati | 180 – 213 | TPR 5UniRule annotationAdd BLAST | 34 | |
Repeati | 214 – 247 | TPR 6UniRule annotationAdd BLAST | 34 | |
Repeati | 249 – 282 | TPR 7UniRule annotationAdd BLAST | 34 |
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
Keywords - Domaini
Repeat, TPR repeat, Transmembrane, Transmembrane helixPhylogenomic databases
eggNOGi | COG2956, Bacteria |
HOGENOMi | CLU_059365_1_0_6 |
InParanoidi | P0AB58 |
PhylomeDBi | P0AB58 |
Family and domain databases
Gene3Di | 1.25.40.10, 2 hits |
HAMAPi | MF_00994, LPS_assembly_LapB, 1 hit |
InterProi | View protein in InterPro IPR030865, LapB IPR041166, Rubredoxin_2 IPR013026, TPR-contain_dom IPR011990, TPR-like_helical_dom_sf IPR019734, TPR_repeat |
Pfami | View protein in Pfam PF18073, Rubredoxin_2, 1 hit |
SMARTi | View protein in SMART SM00028, TPR, 5 hits |
SUPFAMi | SSF48452, SSF48452, 2 hits |
PROSITEi | View protein in PROSITE PS50005, TPR, 6 hits PS50293, TPR_REGION, 1 hit |
i Sequence
Sequence statusi: Complete.
P0AB58-1 [UniParc]FASTAAdd to basket
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
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. |
PIRi | C64876 |
RefSeqi | NP_415796.1, NC_000913.3 WP_000891353.1, NZ_STEB01000005.1 |
Genome annotation databases
EnsemblBacteriai | AAC74362; AAC74362; b1280 BAA14834; BAA14834; BAA14834 |
GeneIDi | 58460487 944858 |
KEGGi | ecj:JW1272 eco:b1280 |
PATRICi | fig|1411691.4.peg.1001 |
Similar proteinsi
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. |
PIRi | C64876 |
RefSeqi | NP_415796.1, NC_000913.3 WP_000891353.1, NZ_STEB01000005.1 |
3D structure databases
SMRi | P0AB58 |
ModBasei | Search... |
Protein-protein interaction databases
BioGRIDi | 4259400, 56 interactors |
DIPi | DIP-48161N |
IntActi | P0AB58, 1 interactor |
STRINGi | 511145.b1280 |
Proteomic databases
jPOSTi | P0AB58 |
PaxDbi | P0AB58 |
PRIDEi | P0AB58 |
Genome annotation databases
EnsemblBacteriai | AAC74362; AAC74362; b1280 BAA14834; BAA14834; BAA14834 |
GeneIDi | 58460487 944858 |
KEGGi | ecj:JW1272 eco:b1280 |
PATRICi | fig|1411691.4.peg.1001 |
Organism-specific databases
EchoBASEi | EB2554 |
Phylogenomic databases
eggNOGi | COG2956, Bacteria |
HOGENOMi | CLU_059365_1_0_6 |
InParanoidi | P0AB58 |
PhylomeDBi | P0AB58 |
Enzyme and pathway databases
BioCyci | EcoCyc:EG12691-MONOMER |
Miscellaneous databases
PROi | PR:P0AB58 |
Family and domain databases
Gene3Di | 1.25.40.10, 2 hits |
HAMAPi | MF_00994, LPS_assembly_LapB, 1 hit |
InterProi | View protein in InterPro IPR030865, LapB IPR041166, Rubredoxin_2 IPR013026, TPR-contain_dom IPR011990, TPR-like_helical_dom_sf IPR019734, TPR_repeat |
Pfami | View protein in Pfam PF18073, Rubredoxin_2, 1 hit |
SMARTi | View protein in SMART SM00028, TPR, 5 hits |
SUPFAMi | SSF48452, SSF48452, 2 hits |
PROSITEi | View protein in PROSITE PS50005, TPR, 6 hits PS50293, TPR_REGION, 1 hit |
ProtoNeti | Search... |
MobiDBi | Search... |
Entry informationi
Entry namei | LAPB_ECOLI | |
Accessioni | P0AB58Primary (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: | February 10, 2021 | |
This is version 109 of the entry and version 1 of the sequence. See complete history. | ||
Entry statusi | Reviewed (UniProtKB/Swiss-Prot) | |
Annotation program | Prokaryotic Protein Annotation Program |
Miscellaneousi
Keywords - Technical termi
Reference proteomeDocuments
- SIMILARITY comments
Index of protein domains and families