STRINGSTRING
ytfM ytfM yaeT yaeT rcsF rcsF STM1131 STM1131 lppB lppB lpp lpp yncD yncD cirA cirA yfiO yfiO smpA smpA fepA fepA iroN iroN pldA pldA yshA yshA yiiY yiiY btuB btuB lamB lamB
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:
ytfMPutative outer membrane protein; Similar to E. coli orf, hypothetical protein (AAC77177.1); Blastp hit to AAC77177.1 (577 aa), 90% identity in aa 3 - 577. (577 aa)
yaeTPutative outer membrane antigen; Part of the outer membrane protein assembly complex, which is involved in assembly and insertion of beta-barrel proteins into the outer membrane. Constitutes, with BamD, the core component of the assembly machinery. (804 aa)
rcsFRegulator in colanic acid synthesis; Essential component of the Rcs signaling system, which controls transcription of numerous genes. Plays a role in signal transduction from the cell surface to the histidine kinase RcsC. May detect outer membrane defects; Belongs to the RcsF family. (134 aa)
STM1131Putative outer membrane protein; Similar to E. coli orf, hypothetical protein (AAC77267.1); Blastp hit to AAC77267.1 (241 aa), 26% identity in aa 4 - 239. (230 aa)
lppBPutative methyl-accepting chemotaxis protein; 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). (79 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)
yncDSimilar to E. coli putative outer membrane receptor for iron transport (AAC74533.1); Blastp hit to AAC74533.1 (700 aa), 84% identity in aa 1 - 700. (706 aa)
cirAOuter membrane porin; Receptor for colicin I; requires TonB; similar to E. coli outer membrane receptor for iron-regulated colicin I receptor; porin; requires tonB gene product (AAC75216.1); Blastp hit to AAC75216.1 (663 aa), 88% identity in aa 1 - 663. (663 aa)
yfiOPutative lipoprotein; Part of the outer membrane protein assembly complex, which is involved in assembly and insertion of beta-barrel proteins into the outer membrane. Constitutes, with BamA, the core component of the assembly machinery. (245 aa)
smpASmall membrane protein A; Part of the outer membrane protein assembly complex, which is involved in assembly and insertion of beta-barrel proteins into the outer membrane. (112 aa)
fepASimilar to E. coli outer membrane receptor for ferric enterobactin (enterochelin) and colicins B and D (AAC73685.1); Blastp hit to AAC73685.1 (746 aa), 81% identity in aa 1 - 746. (751 aa)
iroNTonB-dependent siderophore receptor protein; Similar to E. coli outer membrane receptor for ferric enterobactin (enterochelin) and colicins B and D (AAC73685.1); Blastp hit to AAC73685.1 (746 aa), 52% identity in aa 3 - 728, 44% identity in aa 245 - 746. (726 aa)
pldAOuter membrane phospholipase A; Hydrolysis of phosphatidylcholine with phospholipase A2 (EC 3.1.1.4) and phospholipase A1 (EC 3.1.1.32) activities; Belongs to the phospholipase A1 family. (289 aa)
yshAPutative outer membrane protein; Outer membrane channel protein that allows an efficient diffusion of low-molecular-weight solutes such as small sugars and tetraglycine. However, the specific substrate recognized by the OmpL channel is unknown (By similarity); Belongs to the oligogalacturonate-specific porin KdgM (TC 1.B.35) family. OmpL subfamily. (230 aa)
yiiYPutative outer membrane protein; Hypothetical 15.6 Kda protein in RHAT 5'region. (SW:YIIY_SALTY). (227 aa)
btuBOuter membrane receptor for transport of vitamin B12, E colicins, and bacteriophage BF23; Involved in the active translocation of vitamin B12 (cyanocobalamin) across the outer membrane to the periplasmic space. It derives its energy for transport by interacting with the trans- periplasmic membrane protein TonB; Belongs to the TonB-dependent receptor family. BtuB (TC 1.B.14.3.1) subfamily. (614 aa)
lamBPhage lambda receptor protein; Involved in the transport of maltose and maltodextrins. Does not act as a receptor for phages; Belongs to the porin LamB (TC 1.B.3) family. (452 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.