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pmrF pmrF phoQ phoQ phoP phoP yobG yobG gnd gnd rfbJ rfbJ rfbG rfbG rfbF rfbF rfbA rfbA rfbD rfbD rfbB rfbB galF galF yfbE yfbE pqaB pqaB arnE arnE arnF arnF pmrD pmrD galP galP argD argD yhjW yhjW rfaD rfaD rfaF rfaF rfaC rfaC rfaL rfaL basS basS basR basR yjdB yjdB
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query proteins and first shell of interactors
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second shell of interactors
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proteins of unknown 3D structure
filled nodes:
a 3D structure is known or predicted
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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)
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)
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)
yobGPutative inner membrane protein; PhoP-regulated transcription is redox-sensitive, being activated when the periplasm becomes more reducing. MgrB acts between DsbA/DsbB and PhoP/PhoQ in this pathway. Represses PhoP/PhoQ signaling, possibly by binding to the periplasmic domain of PhoQ, altering its activity and that of downstream effector PhoP. (47 aa)
gndGluconate-6-phosphate dehydrogenase; Catalyzes the oxidative decarboxylation of 6-phosphogluconate to ribulose 5-phosphate and CO(2), with concomitant reduction of NADP to NADPH. (468 aa)
rfbJLPS side chain defect; CDP-abequose synthase. (SW:RFBJ_SALTY). (299 aa)
rfbGLPS side chain defect; CDP-glucose 4,6-dehydratase. (SW:RFBG_SALTY); Belongs to the NAD(P)-dependent epimerase/dehydratase family. (359 aa)
rfbFGlucose-1-phosphate cytidylyltransferase; Involved in the biosynthesis of the tyvelose, a 3,6- dideoxyhexose found in the O-antigen of the surface lipopolysaccharides. It catalyzes the transfer of a CMP moiety from CTP to glucose 1-phosphate (By similarity). (257 aa)
rfbAdTDP-glucose pyrophosphorylase; Catalyzes the formation of dTDP-glucose, from dTTP and glucose 1-phosphate, as well as its pyrophosphorolysis. Is also able to convert non natural substrates such as a wide array of alpha-D- hexopyranosyl, deoxy-alpha-D-glucopyranosyl, aminodeoxy-alpha-D- hexopyranosyl and acetamidodeoxy-alpha-D-hexopyranosyl phosphates to their corresponding dTDP- and UDP-nucleotide sugars. (292 aa)
rfbDTDP-rhamnose synthetase; Involved in the biosynthesis of the dTDP-L-rhamnose which is an important component of lipopolysaccharide (LPS). Catalyzes the reduction of dTDP-6-deoxy-L-lyxo-4-hexulose to yield dTDP-L-rhamnose. RmlD uses NADH and NADPH nearly equally well. (299 aa)
rfbBdTDP-glucose 4,6 dehydratase; Catalyzes the dehydration of dTDP-D-glucose to form dTDP-6- deoxy-D-xylo-4-hexulose via a three-step process involving oxidation, dehydration and reduction; Belongs to the NAD(P)-dependent epimerase/dehydratase family. dTDP-glucose dehydratase subfamily. (361 aa)
galFPutative glucose-1-phosphate uridylyltransferase, non-catalytic subunit; May play a role in stationary phase survival; Belongs to the UDPGP type 2 family. (297 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)
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)
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)
galPMFS family galactose:proton symporter; Similar to E. coli galactose-proton symport of transport system (AAC75980.1); Blastp hit to AAC75980.1 (464 aa), 97% identity in aa 1 - 464; Belongs to the major facilitator superfamily. Sugar transporter (TC 2.A.1.1) family. (464 aa)
argDAcetylornithine transaminase; Involved in both the arginine and lysine biosynthetic pathways. (405 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)
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)
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)
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
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