STRINGSTRING
lpxK lpxK rlpB rlpB pagP pagP lpxH lpxH lpxB lpxB lpxA lpxA fabZ fabZ lpxD lpxD lpxC lpxC imp imp yjdB yjdB basR basR basS basS lpxO lpxO rfaP rfaP rfaB rfaB rfaJ rfaJ rfaY rfaY rfaL rfaL rfaC rfaC rfaF rfaF yhjW yhjW yhbN yhbN yrbK yrbK hflB hflB ddg ddg pmrD pmrD pqaB pqaB yeiU yeiU msbB msbB yciM yciM lpp lpp phoP phoP phoQ phoQ htrB htrB msbA msbA
Nodes:
Network nodes represent proteins
splice isoforms or post-translational modifications are collapsed, i.e. each node represents all the proteins produced by a single, protein-coding gene locus.
Node Color
colored nodes:
query proteins and first shell of interactors
white nodes:
second shell of interactors
Node Content
empty nodes:
proteins of unknown 3D structure
filled nodes:
a 3D structure is known or predicted
Edges:
Edges represent protein-protein associations
associations are meant to be specific and meaningful, i.e. proteins jointly contribute to a shared function; this does not necessarily mean they are physically binding to each other.
Known Interactions
from curated databases
experimentally determined
Predicted Interactions
gene neighborhood
gene fusions
gene co-occurrence
Others
textmining
co-expression
protein homology
Your Input:
lpxKTetraacyldisaccharide 4' kinase; Transfers the gamma-phosphate of ATP to the 4'-position of a tetraacyldisaccharide 1-phosphate intermediate (termed DS-1-P) to form tetraacyldisaccharide 1,4'-bis-phosphate (lipid IVA). (325 aa)
rlpBA minor lipoprotein; Together with LptD, is involved in the assembly of lipopolysaccharide (LPS) at the surface of the outer membrane. Required for the proper assembly of LptD. Binds LPS and may serve as the LPS recognition site at the outer membrane; Belongs to the LptE lipoprotein family. (196 aa)
pagPPhoPQ-activated gene; Transfers a palmitate residue from the sn-1 position of a phospholipid to the N-linked hydroxymyristate on the proximal unit of lipid A or its precursors. Required for resistance to cationic antimicrobial peptides (CAMPs). Modifications of lipid A with a palmitate chain allow to evade host immune defenses by resisting antimicrobial peptides and attenuating the inflammatory response to infection triggered by lipopolysaccharide through the Toll-like receptor 4 (TLR4) signal transduction pathway. (190 aa)
lpxHUDP-2,3-diacylglucosamine hydrolase; Hydrolyzes the pyrophosphate bond of UDP-2,3- diacylglucosamine to yield 2,3-diacylglucosamine 1-phosphate (lipid X) and UMP by catalyzing the attack of water at the alpha-P atom. Involved in the biosynthesis of lipid A, a phosphorylated glycolipid that anchors the lipopolysaccharide to the outer membrane of the cell. (240 aa)
lpxBtetraacyldisaccharide-1-P; Condensation of UDP-2,3-diacylglucosamine and 2,3- diacylglucosamine-1-phosphate to form lipid A disaccharide, a precursor of lipid A, a phosphorylated glycolipid that anchors the lipopolysaccharide to the outer membrane of the cell. (382 aa)
lpxAUDP-N-acetylglucosamine acetyltransferase; Involved in the biosynthesis of lipid A, a phosphorylated glycolipid that anchors the lipopolysaccharide to the outer membrane of the cell. (262 aa)
fabZ(3R)-hydroxymyristol acyl carrier protein dehydratase; Involved in unsaturated fatty acids biosynthesis. Catalyzes the dehydration of short chain beta-hydroxyacyl-ACPs and long chain saturated and unsaturated beta-hydroxyacyl-ACPs (By similarity). (151 aa)
lpxDUDP-3-O-(3-hydroxymyristoyl)-glucosamine n-acyltransferase; Catalyzes the N-acylation of UDP-3-O- (hydroxytetradecanoyl)glucosamine using 3-hydroxytetradecanoyl-ACP as the acyl donor. Is involved in the biosynthesis of lipid A, a phosphorylated glycolipid that anchors the lipopolysaccharide to the outer membrane of the cell. (341 aa)
lpxCUDP-3-O-acyl N-acetylglucosamine deacetylase; Catalyzes the hydrolysis of UDP-3-O-myristoyl-N- acetylglucosamine to form UDP-3-O-myristoylglucosamine and acetate, the committed step in lipid A biosynthesis; Belongs to the LpxC family. (305 aa)
impOrganic solvent tolerance protein; Together with LptE, is involved in the assembly of lipopolysaccharide (LPS) at the surface of the outer membrane. (786 aa)
yjdBPutative integral membrane protein; Catalyzes the addition of a phosphoethanolamine moiety to the lipid A. The phosphoethanolamine modification is required for resistance to polymyxin; Belongs to the phosphoethanolamine transferase family. EptA subfamily. (547 aa)
basRResponse regulator in two-component regulatory system with BasS; Member of the two-component regulatory system BasS/BasR. BasR induces the transcription of the ugd, ais, arnBCADTEF and eptA-basRS loci, all involved in resistance to polymyxin. Represses the transcription of pmrD. Plays a role in the adaptation of the organism to the host environment, in particular to neutrophils, and therefore it plays a role in virulence as well. (222 aa)
basSSensory kinase in two-component regulatory system with BasR; Member of the two-component regulatory system BasS/BasR. Autophosphorylates and activates BasR by phosphorylation. Plays a role in the adaptation of the organism to the host environment, in particular to neutrophils, and therefore it plays a role in virulence as well. (356 aa)
lpxOPutative dioxygenase for synthesis of lipid; Putative dioxygenase; LpxO (gi|9454389). (302 aa)
rfaPLipopolysaccharide core biosynthesis protein; Catalyzes the phosphorylation of heptose(I) of the outer membrane lipopolysaccharide core. (265 aa)
rfaBUDP-D-galactose:(glucosyl)lipopolysaccharide-1, 6-D-galactosyltransferase; Adds a galactose goup to a glucose group of LPS; Belongs to the glycosyltransferase group 1 family. Glycosyltransferase 4 subfamily. (359 aa)
rfaJUDP-D-glucose:(galactosyl)lipopolysaccharide glucosyltransferase; Adds the glucose(II) group on the galactose(I) group of LPS. (336 aa)
rfaYLipopolysaccharide core biosynthesis protein; Catalyzes the phosphorylation of heptose(II) of the outer membrane lipopolysaccharide core; Belongs to the protein kinase superfamily. RfaY/WaaY family. (232 aa)
rfaLO-antigen ligase; Adds the O-antigen on the glucose(II) group of LPS. (404 aa)
rfaCHeptosyl transferase I; Heptose transfer to the lipopolysaccharide core. It transfers the innermost heptose to [4'-P](3-deoxy-D-manno-octulosonic acid)2-IVA; Belongs to the glycosyltransferase 9 family. (317 aa)
rfaFADP-heptose; AFP-heptose--lps heptosyltransferase II. (SW:RFAF_SALTY). (348 aa)
yhjWPutative membrane-associated metal-dependent hydrolase; Catalyzes the addition of a phosphoethanolamine (pEtN) moiety to the outer 3-deoxy-D-manno-octulosonic acid (Kdo) residue of a Kdo(2)-lipid A. Phosphatidylethanolamines with one unsaturated acyl group functions as pEtN donors and the reaction releases diacylglycerol. (563 aa)
yhbNPutative ABC superfamily transport protein; Involved in the assembly of lipopolysaccharide (LPS). Required for the translocation of LPS from the inner membrane to the outer membrane. May form a bridge between the inner membrane and the outer membrane, via interactions with LptC and LptD, thereby facilitating LPS transfer across the periplasm. (184 aa)
yrbKPutative inner membrane protein; Involved in the assembly of lipopolysaccharide (LPS). Required for the translocation of LPS from the inner membrane to the outer membrane. Facilitates the transfer of LPS from the inner membrane to the periplasmic protein LptA. Could be a docking site for LptA. Belongs to the LptC family. (191 aa)
hflBATP-dependent zinc-metallo protease; Acts as a processive, ATP-dependent zinc metallopeptidase for both cytoplasmic and membrane proteins. Plays a role in the quality control of integral membrane proteins; In the central section; belongs to the AAA ATPase family. (644 aa)
ddgCold shock-induced palmitoleoyl transferase; Catalyzes the transfer of palmitoleate from palmitoleoyl-acyl carrier protein (ACP) to Kdo(2)-lipid IV(A) to form Kdo(2)- (palmitoleoyl)-lipid IV(A); Belongs to the LpxL/LpxM/LpxP family. LpxP subfamily. (306 aa)
pmrDPolymyxin resistance protein B; Interacts with phosphorylated BasR protein to mediate transcriptional induction of BasR-activated genes to induce polymyxin resistance; Belongs to the PmrD family. (85 aa)
pqaBPutative melittin resistance protein; Catalyzes the transfer of the L-Ara4N moiety of the glycolipid undecaprenyl phosphate-alpha-L-Ara4N to lipid A. The modified arabinose is attached to lipid A and is required for resistance to polymyxin and cationic antimicrobial peptides. Belongs to the glycosyltransferase 83 family. (548 aa)
yeiUPutative permease; Involved in the modification of the lipid A domain of lipopolysaccharides (LPS). Transfers a phosphate group from undecaprenyl pyrophosphate (C55-PP) to lipid A to form lipid A 1- diphosphate. Contributes to the recycling of undecaprenyl phosphate (C55-P); Belongs to the LpxT phosphotransferase family. (239 aa)
msbBMyristoyl transferase in lipid A biosynthesis; Catalyzes the transfer of myristate from myristoyl-acyl carrier protein (ACP) to Kdo(2)-(lauroyl)-lipid IV(A) to form Kdo(2)- lipid A. (323 aa)
yciMPutative N-acetylglucosaminyl transferase; 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; Belongs to the LapB family. (389 aa)
lppMurein lipoprotein; Plays an important role in virulence. A highly abundant outer membrane lipoprotein that controls the distance between the inner and outer membranes. The only protein known to be covalently linked to the peptidoglycan network (PGN). Also non- covalently binds the PGN. The link between the cell outer membrane and PGN contributes to maintenance of the structural and functional integrity of the cell envelope, and maintains the correct distance between the PGN and the outer membrane (By similarity). (78 aa)
phoPResponse regulator in two-component regulatory system with PhoQ; Member of the two-component regulatory system PhoP/PhoQ which regulates the expression of genes involved in virulence, adaptation to acidic and low Mg(2+) environments and resistance to host defense antimicrobial peptides. Essential for intramacrophage survival of S.typhimurium. In low periplasmic Mg(2+), PhoQ phosphorylates PhoP, resulting in the expression of PhoP-activated genes (PAG) and repression of PhoP-repressed genes (PRG). In high periplasmic Mg(2+), PhoQ dephosphorylates phospho-PhoP, resulting in the repressio [...] (224 aa)
phoQSensory kinase protein in two-component regulatory system with PhoP; Member of the two-component regulatory system PhoP/PhoQ which regulates the expression of genes involved in virulence, adaptation to acidic and low Mg(2+) environments and resistance to host defense antimicrobial peptides. Essential for intramacrophage survival of S.typhimurium. In low periplasmic Mg(2+), PhoQ functions as a membrane- associated protein kinase that undergoes autophosphorylation and subsequently transfers the phosphate to PhoP, resulting in the expression of PhoP-activated genes (PAG) and repression of [...] (487 aa)
htrBLauroyl/myristoyl acyltransferase involved in lipid A biosynthesis; Catalyzes the transfer of laurate from lauroyl-acyl carrier protein (ACP) to Kdo(2)-lipid IV(A) to form Kdo(2)-(lauroyl)-lipid IV(A). (306 aa)
msbAMulticopy repressor of htrB transport protein; Involved in lipid A export and possibly also in glycerophospholipid export and for biogenesis of the outer membrane. Transmembrane domains (TMD) form a pore in the inner membrane and the ATP-binding domain (NBD) is responsible for energy generation. Belongs to the ABC transporter superfamily. Lipid exporter (TC 3.A.1.106) family. (582 aa)
Your Current Organism:
Salmonella enterica Typhimurium
NCBI taxonomy Id: 99287
Other names: S. enterica subsp. enterica serovar Typhimurium str. LT2, Salmonella enterica subsp. enterica serovar Typhimurium LT2, Salmonella enterica subsp. enterica serovar Typhimurium str. LT2, Salmonella enterica subsp. enterica serovar Typhimurium strain LT2, Salmonella enterica subsp. enterica serovar Typhimurium strain LT2-LTL2, Salmonella typhimurium LT2
Server load: low (20%) [HD]
STRING is a Core Data Resource as designated by Global Biodata Coalition and ELIXIR.