STRINGSTRING
mdoB mdoB polB polB lpxC lpxC entD entD STM0718 STM0718 yciM yciM yejM yejM hflB hflB acpT acpT yjdB yjdB
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:
mdoBPhosphoglycerol transferase I; Transfers a phosphoglycerol residue from phosphatidylglycerol to the membrane-bound nascent glucan backbones; Belongs to the OpgB family. (750 aa)
polBDNA polymerase II; 3'->5' exonuclease; similar to E. coli DNA polymerase II (AAC73171.1); Blastp hit to AAC73171.1 (783 aa), 89% identity in aa 1 - 783. (783 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)
entDEnterochelin synthetase, component D (phoshpantetheinyltransferase); Involved in the biosynthesis of the siderophore enterobactin (enterochelin), which is a macrocyclic trimeric lactone of N-(2,3- dihydroxybenzoyl)-serine. The serine trilactone serves as a scaffolding for the three catechol functionalities that provide hexadentate coordination for the tightly ligated iron(2+) atoms. Plays an essential role in the assembly of the enterobactin by catalyzing the transfer of the 4'-phosphopantetheine (Ppant) moiety from coenzyme A to the apo- domains of both EntB (ArCP domain) and EntF (PC [...] (234 aa)
STM0718Putative cytoplasmic protein. (246 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)
yejMPutative hydrolase of alkaline phosphatase superfamily; Hypothetical protein in rplY-proL intergenic region. (SW:YEJM_SALTY). (586 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)
acpTPutative phosphopantetheinyl transferase; May be involved in an alternative pathway for phosphopantetheinyl transfer and holo-ACP synthesis. The native apo- protein substrate is unknown; Belongs to the P-Pant transferase superfamily. Gsp/Sfp/HetI/AcpT family. (192 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
Server load: low (32%) [HD]
STRING is a Core Data Resource as designated by Global Biodata Coalition and ELIXIR.