STRINGSTRING
STRING protein interaction network
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.
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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.
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from curated databases
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experimentally determined
co-expression
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gene neighborhood
gene co-occurrence
gene fusions
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iscSCysteine desulfurase; 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 atoms from cysteine 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; Belongs to the class-V pyridoxal-phosphate-dependent aminotransferase family. NifS/IscS subfamily. (404 aa)    
Predicted Functional Partners:
icsU
NifU-like protein; 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.
 
 0.994
hscB
Chaperone protein; 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.
 
 0.984
nifU
Nitrogen fixation protein; May be involved in the formation or repair of [Fe-S] clusters present in iron-sulfur proteins.
 
 0.983
iscR
Putative transcriptional regulator; Regulates the transcription of several operons and genes involved in the biogenesis of Fe-S clusters and Fe-S-containing proteins.
 
 0.975
fdx
Ferredoxin, 2Fe-2S; Similar to Escherichia coli, Escherichia coli O157:H7, and Shigella flexneri ferredoxin, 2fe-2s Fdx or b2525 or z3792 or ecs3391 or sf2572 SWALL:AAN44071 (EMBL:M88654) (111 aa) fasta scores: E(): 6.7e-39, 84.68% id in 111 aa.
 
 0.950
sirA
SirA protein; Sulfur carrier protein involved in sulfur trafficking in the cell. Part of a sulfur-relay system required for 2-thiolation during synthesis of 2-thiouridine of the modified wobble base 5- methylaminomethyl-2-thiouridine (mnm(5)s(2)U) in tRNA. Interacts with IscS and stimulates its cysteine desulfurase activity. Accepts an activated sulfur from IscS, which is then transferred to TusD, and thus determines the direction of sulfur flow from IscS to 2-thiouridine formation. Also appears to be involved in sulfur transfer for the biosynthesis of molybdopterin.
   
 0.943
nfuA
Conserved hypothetical 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.
  
 0.912
hscA
Chaperone 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.
 
 0.893
iscA
Conserved hypothetical protein; 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.
 
 
 0.887
thiI
Thiamine biosynthesis protein; Catalyzes the ATP-dependent transfer of a sulfur to tRNA to produce 4-thiouridine in position 8 of tRNAs, which functions as a near-UV photosensor. Also catalyzes the transfer of sulfur to the sulfur carrier protein ThiS, forming ThiS-thiocarboxylate. This is a step in the synthesis of thiazole, in the thiamine biosynthesis pathway. The sulfur is donated as persulfide by IscS.
  
 0.886
Your Current Organism:
Pectobacterium atrosepticum
NCBI taxonomy Id: 218491
Other names: Erwinia carotovora subsp. atroseptica SCRI1043, Erwinia carotovora subsp. atroseptica str. SCRI1043, P. atrosepticum SCRI1043, Pectobacterium atrosepticum SCRI1043, Pectobacterium atrosepticum str. SCRI1043, Pectobacterium atrosepticum strain SCRI1043, Pectobacterium carotovora subsp. atroseptica SCRI1043, Pectobacterium carotovora subsp. atroseptica str. SCRI1043
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