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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.
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:
Neighborhood
Gene Fusion
Cooccurrence
Coexpression
Experiments
Databases
Textmining
[Homology]
Score
CKO_00252Hypothetical 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. (128 aa)    
Predicted Functional Partners:
iscS
Hypothetical protein; 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.
 
 0.999
hscB
Hypothetical 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.
 
 
 0.994
cyaY
Hypothetical protein; Involved in iron-sulfur (Fe-S) cluster assembly. May act as a regulator of Fe-S biogenesis.
  
 
 0.992
CKO_00256
Hypothetical protein; KEGG: eci:UTI89_C2847 7.5e-56 fdx; ferredoxin, 2Fe-2S K04755; COG: COG0633 Ferredoxin; Psort location: Cytoplasmic, score:8.96.
 
 0.991
sufS
Hypothetical protein; Cysteine desulfurases mobilize the sulfur from L-cysteine to yield L-alanine, an essential step in sulfur metabolism for biosynthesis of a variety of sulfur-containing biomolecules. Component of the suf operon, which is activated and required under specific conditions such as oxidative stress and iron limitation. Acts as a potent selenocysteine lyase in vitro, that mobilizes selenium from L- selenocysteine. Selenocysteine lyase activity is however unsure in vivo.
  
 0.984
hscA
Hypothetical 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.
 
 
 0.974
CKO_04174
Hypothetical protein; KEGG: ssn:SSO_2967 3.1e-192 cysteine sulfinate desulfinase; COG: COG0520 Selenocysteine lyase; Psort location: Cytoplasmic, score:8.96.
  
 
 0.969
CKO_00253
Hypothetical protein; COG: COG0316 Uncharacterized conserved protein; Psort location: Cytoplasmic, score:8.96; Belongs to the HesB/IscA family.
 
  
 0.956
CKO_02607
Hypothetical protein; KEGG: dre:562769 1.9e-06 LOC562769; similar to Serine/threonine-protein kinase 10 (Lymphocyte-oriented kinase) K08837; COG: COG1076 DnaJ-domain-containing proteins 1; Psort location: Cytoplasmic, score:8.96.
  
 
 0.953
djlA
Hypothetical protein; Regulatory DnaK co-chaperone. Direct interaction between DnaK and DjlA is needed for the induction of the wcaABCDE operon, involved in the synthesis of a colanic acid polysaccharide capsule, possibly through activation of the RcsB/RcsC phosphotransfer signaling pathway. The colanic acid capsule may help the bacterium survive conditions outside the host.
  
 
 0.953
Your Current Organism:
Citrobacter koseri
NCBI taxonomy Id: 290338
Other names: C. koseri ATCC BAA-895, Citrobacter (diversus) koseri ATCC BAA-895, Citrobacter koseri ATCC BAA-895, Citrobacter koseri str. ATCC BAA-895, Citrobacter koseri strain ATCC BAA-895
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