STRINGSTRING
yfhF yfhF nifU nifU yfhJ yfhJ csdA csdA cyaY cyaY yhgI yhgI sufA sufA ygfZ ygfZ mrp mrp nifS nifS hscA hscA hscB hscB ynhA ynhA sufD sufD yadR yadR sufB sufB
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:
yfhFPutative regulator; Is able to transfer iron-sulfur clusters to apo-ferredoxin. Multiple cycles of [2Fe2S] cluster formation and transfer are observed, suggesting that IscA acts catalytically. Recruits intracellular free iron so as to provide iron for the assembly of transient iron-sulfur cluster in IscU in the presence of IscS, L-cysteine and the thioredoxin reductase system TrxA/TrxB. (107 aa)
nifUNifU homolog; A scaffold on which IscS assembles Fe-S clusters. It is likely that Fe-S cluster coordination is flexible as the role of this complex is to build and then hand off Fe-S clusters. (128 aa)
yfhJHypothetical protein; Believed to be involved in assembly of Fe-S clusters; similar to E. coli orf, hypothetical protein (AAC75577.1); Blastp hit to AAC75577.1 (66 aa), 92% identity in aa 1 - 66. (66 aa)
csdAPutative selenocysteine lyase; Similar to E. coli orf, hypothetical protein (AAC75852.1); Blastp hit to AAC75852.1 (401 aa), 89% identity in aa 1 - 401. (401 aa)
cyaYPutative frataxin family transport protein; Involved in iron-sulfur (Fe-S) cluster assembly. May act as a regulator of Fe-S biogenesis. (106 aa)
yhgIPutative thioredoxin-like proteins and domain protein; Involved in iron-sulfur cluster biogenesis. Binds a 4Fe-4S cluster, can transfer this cluster to apoproteins, and thereby intervenes in the maturation of Fe/S proteins. Could also act as a scaffold/chaperone for damaged Fe/S proteins. (191 aa)
sufAPutative HesB-like domain protein; Similar to E. coli orf, hypothetical protein (AAC74754.1); Blastp hit to AAC74754.1 (122 aa), 84% identity in aa 1 - 122; Belongs to the HesB/IscA family. (122 aa)
ygfZPutative aminomethyltransferase; Folate-binding protein involved in regulating the level of ATP-DnaA and in the modification of some tRNAs. It is probably a key factor in regulatory networks that act via tRNA modification, such as initiation of chromosomal replication; Belongs to the tRNA-modifying YgfZ family. (326 aa)
mrpPutative ATP-binding protein; Binds and transfers iron-sulfur (Fe-S) clusters to target apoproteins. Can hydrolyze ATP. Both activities are required for function in vivo, but the ability to hydrolyze ATP is not necessary for Fe-S cluster transfer. (369 aa)
nifSPutative aminotransferase class-V; Master enzyme that delivers sulfur to a number of partners involved in Fe-S cluster assembly, tRNA modification or cofactor biosynthesis. Catalyzes the removal of elemental sulfur and selenium atoms from cysteine and selenocysteine to produce alanine. Functions as a sulfur delivery protein for Fe-S cluster synthesis onto IscU, an Fe-S scaffold assembly protein, as well as other S acceptor proteins. Also functions as a selenium delivery protein in the pathway for the biosynthesis of selenophosphate; Belongs to the class-V pyridoxal-phosphate-dependent [...] (404 aa)
hscAChaperone protein; Chaperone involved in the maturation of iron-sulfur cluster- containing proteins. Has a low intrinsic ATPase activity which is markedly stimulated by HscB. Involved in the maturation of IscU. (616 aa)
hscBCo-chaperone protein Hsc20; Co-chaperone involved in the maturation of iron-sulfur cluster-containing proteins. Seems to help targeting proteins to be folded toward HscA; Belongs to the HscB family. (171 aa)
ynhAPutative SufE protein; Participates in cysteine desulfuration mediated by SufS. Cysteine desulfuration mobilizes sulfur from L-cysteine to yield L- alanine and constitutes an essential step in sulfur metabolism for biosynthesis of a variety of sulfur-containing biomolecules. Functions as a sulfur acceptor for SufS, by mediating the direct transfer of the sulfur atom from the S-sulfanylcysteine of SufS, an intermediate product of cysteine desulfuration process; Belongs to the SufE family. (138 aa)
sufDIron-sulfur component of FhuF stability protein; Similar to E. coli orf, hypothetical protein (AAC74751.1); Blastp hit to AAC74751.1 (423 aa), 79% identity in aa 1 - 421. (423 aa)
yadRPutative HesB-like domain protein; Required for insertion of 4Fe-4S clusters for at least IspG. (129 aa)
sufBPutative ABC transporter; Similar to E. coli orf, hypothetical protein (AAC74753.1); Blastp hit to AAC74753.1 (508 aa), 96% identity in aa 14 - 508. (495 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 (34%) [HD]
STRING is a Core Data Resource as designated by Global Biodata Coalition and ELIXIR.