Protein Domain : IPR010440

Type:  Family Name:  Lipopolysaccharide kinase
Description:  Protein phosphorylation, which plays a key role in most cellular activities, is a reversible process mediated by protein kinases and phosphoprotein phosphatases. Protein kinases catalyse the transfer of the gamma phosphate from nucleotide triphosphates (often ATP) to one or more amino acid residues in a protein substrate side chain, resulting in a conformational change affecting protein function. Phosphoprotein phosphatases catalyse the reverse process. Protein kinases fall into three broad classes, characterised with respect to substrate specificity []:Serine/threonine-protein kinasesTyrosine-protein kinasesDual specificity protein kinases (e.g. MEK - phosphorylates both Thr and Tyr on target proteins)Protein kinase function is evolutionarily conserved from Escherichia coli to human []. Protein kinases play a role in a multitude of cellular processes, including division, proliferation, apoptosis, and differentiation []. Phosphorylation usually results in a functional change of the target protein by changing enzyme activity, cellular location, or association with other proteins. The catalytic subunits of protein kinases are highly conserved, and several structures have been solved [], leading to large screens to develop kinase-specific inhibitors for the treatments of a number of diseases [].This entry represents lipopolysaccharide kinases which are related to protein kinases . This family includes waaP (rfaP) gene product is required for the addition of phosphate to O-4 of the first heptose residue of the lipopolysaccharide (LPS) inner core region. It has previously been shown that WaaP is necessary for resistance to hydrophobic and polycationic antimicrobials in E. coli and that it is required for virulence in invasive strains of Salmonella enterica[]. Short Name:  LipoPS_kinase

3 Child Features

DB identifier Type Name
IPR027023 Family Putative lipopolysaccharide kinase InaA
IPR017172 Family Lipopolysaccharide core heptose(I) kinase rfaP
IPR022826 Family 3-deoxy-D-manno-octulosonic acid kinase

0 Contains

1 Cross References


0 Found In

3 GO Annotations

GO Term Gene Name Organism
GO:0005524 IPR010440
GO:0016773 IPR010440
GO:0016020 IPR010440

0 Parent Features

1185 Proteins

DB identifier UniProt Accession Secondary Identifier Organism Name Length
73433 PAC:15406844 Selaginella moellendorffii 532  
34528 D8QYG2 PAC:15404011 Selaginella moellendorffii 275  
75282 D8QQG3 PAC:15411391 Selaginella moellendorffii 370  
82473 PAC:15411314 Selaginella moellendorffii 513  
74687 PAC:15411530 Selaginella moellendorffii 474  
173444 D8RR32 PAC:15414880 Selaginella moellendorffii 579  
92726 D8RF67 PAC:15420653 Selaginella moellendorffii 504  
evm.TU.contig_29215.1 PAC:16429681 Carica papaya 597  
evm.model.supercontig_122.29 PAC:16407076 Carica papaya 677  
evm.model.supercontig_1289.1 PAC:16407508 Carica papaya 227  
evm.model.supercontig_6.174 PAC:16423347 Carica papaya 372  
27964.m000350 B9SVE4 PAC:16799638 Ricinus communis 602  
29659.m000143 B9T0M6 PAC:16804989 Ricinus communis 321  
29682.m000597 B9SRC8 PAC:16805689 Ricinus communis 627  
29733.m000739 B9S840 PAC:16807073 Ricinus communis 512  
29989.m000415 B9SR58 PAC:16815192 Ricinus communis 606  
30089.m001020 B9RPG6 PAC:16817534 Ricinus communis 589  
30147.m014057 B9R931 PAC:16820071 Ricinus communis 549  
30170.m013789 B9R7Z1 PAC:16821634 Ricinus communis 372  
34736.m000026 B9TEJ3 PAC:16826335 Ricinus communis 273  
30226.m002047 B9REN6 PAC:16824290 Ricinus communis 508  
31196.m000015 B9TGW4 PAC:16824878 Ricinus communis 416  
Cucsa.366440.2 PAC:16981501 Cucumis sativus 607  
Cucsa.185440.1 A0A0A0KEC4 PAC:16967691 Cucumis sativus 606  
Cucsa.185440.2 PAC:16967692 Cucumis sativus 552  
Cucsa.126740.1 PAC:16961965 Cucumis sativus 438  
Cucsa.019360.2 A0A0A0KMF1 PAC:16951860 Cucumis sativus 467  
Cucsa.019360.6 PAC:16951864 Cucumis sativus 370  
Cucsa.019360.1 A0A0A0KMF1 PAC:16951858 Cucumis sativus 467  
Cucsa.019360.3 A0A0A0KMF1 PAC:16951861 Cucumis sativus 467  

6 Publications

First Author Title Year Journal Volume Pages PubMed ID