STRINGSTRING
kdtA kdtA pagP pagP lpxK lpxK htrB htrB acpP acpP yeiU yeiU yfbE yfbE pmrF pmrF yfbG yfbG arnD arnD pqaB pqaB arnE arnE arnF arnF ddg ddg iacP iacP lpxD lpxD fabZ fabZ lpxC lpxC lpxH lpxH lpxA lpxA lpxB lpxB yjdB yjdB yhjW yhjW glmU glmU
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:
kdtA3-deoxy-D-manno-octulosonic-acid transferase; Involved in lipopolysaccharide (LPS) biosynthesis. Catalyzes the transfer of 3-deoxy-D-manno-octulosonate (Kdo) residue(s) from CMP- Kdo to lipid IV(A), the tetraacyldisaccharide-1,4'-bisphosphate precursor of lipid A; Belongs to the glycosyltransferase group 1 family. (425 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)
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)
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)
acpPAcyl carrier protein; Carrier of the growing fatty acid chain in fatty acid biosynthesis; Belongs to the acyl carrier protein (ACP) family. (78 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)
yfbEPutative DegT/DnrJ/EryC1/StrS family; Catalyzes the conversion of UDP-4-keto-arabinose (UDP-Ara4O) to UDP-4-amino-4-deoxy-L-arabinose (UDP-L-Ara4N). The modified arabinose is attached to lipid A and is required for resistance to polymyxin and cationic antimicrobial peptides (By similarity); Belongs to the DegT/DnrJ/EryC1 family. ArnB subfamily. (385 aa)
pmrFPutative glycosyl transferase; Catalyzes the transfer of 4-deoxy-4-formamido-L-arabinose from UDP to undecaprenyl phosphate. The modified arabinose is attached to lipid A and is required for resistance to polymyxin and cationic antimicrobial peptides. Plays an important role in pathogenesis by providing resistance to antimicrobial peptides within macrophages or at other anatomic sites encountered during infection. Belongs to the glycosyltransferase 2 family. (327 aa)
yfbGPutative transformylase; Bifunctional enzyme that catalyzes the oxidative decarboxylation of UDP-glucuronic acid (UDP-GlcUA) to UDP-4-keto- arabinose (UDP-Ara4O) and the addition of a formyl group to UDP-4- amino-4-deoxy-L-arabinose (UDP-L-Ara4N) to form UDP-L-4-formamido- arabinose (UDP-L-Ara4FN). The modified arabinose is attached to lipid A and is required for resistance to polymyxin and cationic antimicrobial peptides (By similarity); In the N-terminal section; belongs to the Fmt family. UDP- L-Ara4N formyltransferase subfamily. (660 aa)
arnDPutative cytoplasmic protein; Catalyzes the deformylation of 4-deoxy-4-formamido-L- arabinose-phosphoundecaprenol to 4-amino-4-deoxy-L-arabinose- phosphoundecaprenol. The modified arabinose is attached to lipid A and is required for resistance to polymyxin and cationic antimicrobial peptides (Probable). (299 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)
arnEPutative inner membrane protein; Translocates 4-amino-4-deoxy-L-arabinose-phosphoundecaprenol (alpha-L-Ara4N-phosphoundecaprenol) from the cytoplasmic to the periplasmic side of the inner membrane; Belongs to the ArnE family. (111 aa)
arnFPutative inner membrane protein; Translocates 4-amino-4-deoxy-L-arabinose-phosphoundecaprenol (alpha-L-Ara4N-phosphoundecaprenol) from the cytoplasmic to the periplasmic side of the inner membrane. (125 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)
iacPPutative acyl carrier protein; Acyl carrier protein. (82 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)
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)
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)
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)
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)
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)
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)
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)
glmUN-acetyl glucosamine-1-phosphate uridyltransferase; Catalyzes the last two sequential reactions in the de novo biosynthetic pathway for UDP-N-acetylglucosamine (UDP-GlcNAc). The C- terminal domain catalyzes the transfer of acetyl group from acetyl coenzyme A to glucosamine-1-phosphate (GlcN-1-P) to produce N- acetylglucosamine-1-phosphate (GlcNAc-1-P), which is converted into UDP-GlcNAc by the transfer of uridine 5-monophosphate (from uridine 5- triphosphate), a reaction catalyzed by the N-terminal domain. In the C-terminal section; belongs to the transferase hexapeptide repeat family. (456 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 (16%) [HD]
STRING is a Core Data Resource as designated by Global Biodata Coalition and ELIXIR.