STRINGSTRING
phoQ phoQ htrB htrB msbA msbA ompX ompX pagP pagP ghmA ghmA pmrF pmrF pqaB pqaB pmrD pmrD ddg ddg nlpD nlpD rfaE rfaE yrbH yrbH yhjW yhjW rfaD rfaD rfaF rfaF rfaC rfaC rfaL rfaL rfaI rfaI kdtA kdtA rfe rfe lsrE lsrE basS basS basR basR yeiU yeiU msbB msbB STM1617 STM1617 galU galU phoP phoP
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:
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)
ompXOuter membrane protease, receptor for phage OX2; Similar to E. coli outer membrane protein X (AAC73901.1); Blastp hit to AAC73901.1 (171 aa), 91% identity in aa 1 - 171. (171 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)
ghmAPhosphoheptose isomerase; Catalyzes the isomerization of sedoheptulose 7-phosphate in D-glycero-D-manno-heptose 7-phosphate; Belongs to the SIS family. GmhA subfamily. (192 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)
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)
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)
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)
nlpDLipoprotein; Activator of the cell wall hydrolase AmiC. Required for septal murein cleavage and daughter cell separation during cell division (By similarity); Belongs to the E.coli NlpD/Haemophilus LppB family. (377 aa)
rfaEPutative sugar nucleotide transferase domain of ADP-L-glycero-D-manno-heptose synthase; Catalyzes the phosphorylation of D-glycero-D-manno-heptose 7- phosphate at the C-1 position to selectively form D-glycero-beta-D- manno-heptose-1,7-bisphosphate; In the N-terminal section; belongs to the carbohydrate kinase PfkB family. (477 aa)
yrbHPutative polysialic acid capsule expression protein; Involved in the biosynthesis of 3-deoxy-D-manno-octulosonate (KDO), a unique 8-carbon sugar component of lipopolysaccharides (LPSs). Catalyzes the reversible aldol-ketol isomerization between D-ribulose 5-phosphate (Ru5P) and D-arabinose 5-phosphate (A5P) (By similarity). (328 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)
rfaDADP-L-glycero-D-mannoheptose-6-epimerase; Catalyzes the interconversion between ADP-D-glycero-beta-D- manno-heptose and ADP-L-glycero-beta-D-manno-heptose via an epimerization at carbon 6 of the heptose. (310 aa)
rfaFADP-heptose; AFP-heptose--lps heptosyltransferase II. (SW:RFAF_SALTY). (348 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)
rfaLO-antigen ligase; Adds the O-antigen on the glucose(II) group of LPS. (404 aa)
rfaIUDP-D-galactose:(glucosyl)lipopolysaccharide- alpha-1,3-D-galactosyltransferase; Adds the galactose(I) group on the glucose(I) group of LPS. (337 aa)
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)
rfeUndecaprenyl-phosphate N-acetylglucosaminyltransferase; Catalyzes the transfer of the GlcNAc-1-phosphate moiety from UDP-GlcNAc onto the carrier lipid undecaprenyl phosphate (C55-P), yielding GlcNAc-pyrophosphoryl-undecaprenyl (GlcNAc-PP-C55). Belongs to the glycosyltransferase 4 family. WecA subfamily. (367 aa)
lsrESimilar to E. coli D-ribulose-5-phosphate 3-epimerase (AAC76411.1); Blastp hit to AAC76411.1 (225 aa), 26% identity in aa 1 - 217. (254 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)
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)
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)
STM1617Putative ribulose-phosphate 3-epimerase; Similar to E. coli putative epimerase (AAC77257.1); Blastp hit to AAC77257.1 (210 aa), 65% identity in aa 1 - 210. (210 aa)
galUSimilar to E. coli glucose-1-phosphate uridylyltransferase (AAC74318.1); Blastp hit to AAC74318.1 (302 aa), 97% identity in aa 1 - 302. (302 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)
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 (18%) [HD]
STRING is a Core Data Resource as designated by Global Biodata Coalition and ELIXIR.