STRINGSTRING
cspI cspI rnhB rnhB rnhA rnhA tig tig ppiB ppiB cspE cspE cspD cspD cspH cspH cspG cspG cspB cspB cspF cspF cspC cspC amyA amyA bglX bglX fkpA fkpA slyD slyD ppiA ppiA cspA cspA malS malS cutA cutA groL groL fklB fklB
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:
cspIQin prophage; Cold shock-like protein. (70 aa)
rnhBRibonuclease HII, degrades RNA of DNA-RNA hybrids; Endonuclease that specifically degrades the RNA of RNA-DNA hybrids; Belongs to the RNase HII family. (198 aa)
rnhARibonuclease HI, degrades RNA of DNA-RNA hybrids; Endonuclease that specifically degrades the RNA of RNA-DNA hybrids. RNase H participates in DNA replication; it helps to specify the origin of genomic replication by suppressing initiation at origins other than the oriC locus; along with the 5'-3' exonuclease of pol1, it removes RNA primers from the Okazaki fragments of lagging strand synthesis; and it defines the origin of replication for ColE1-type plasmids by specific cleavage of an RNA preprimer. (155 aa)
tigPeptidyl-prolyl cis/trans isomerase (trigger factor); Involved in protein export. Acts as a chaperone by maintaining the newly synthesized secretory and non-secretory proteins in an open conformation. Binds to 3 regions of unfolded substrate PhoA, preferring aromatic and hydrophobic residues, keeping it stretched out and unable to form aggregates. Binds to nascent polypeptide chains via ribosomal protein L23. Functions as a peptidyl-prolyl cis-trans isomerase in vitro, this activity is dispensible in vivo for chaperone activity. Belongs to the FKBP-type PPIase family. Tig subfamily. (432 aa)
ppiBPeptidyl-prolyl cis-trans isomerase B (rotamase B); PPIases accelerate the folding of proteins. It catalyzes the cis-trans isomerization of proline imidic peptide bonds in oligopeptides. (164 aa)
cspECold shock protein; Protein involved in transcription activator activity, transcription and response to temperature stimulus. (69 aa)
cspDInhibitor of DNA replication, cold shock protein homolog; Inhibits DNA replication at both initiation and elongation steps, most probably by binding to the opened, single-stranded regions at replication forks. Plays a regulatory role in chromosomal replication in nutrient-depleted cells. (74 aa)
cspHStress protein, member of the CspA-family; Cold shock-like protein; Protein involved in response to temperature stimulus. (70 aa)
cspGHomolog of Salmonella cold shock protein; Protein involved in response to temperature stimulus. (70 aa)
cspBQin prophage; cold shock protein. (71 aa)
cspFQin prophage; cold shock protein. (70 aa)
cspCStress protein, member of the CspA-family; Cold shock protein; Protein involved in transcription activator activity, transcription and response to temperature stimulus. (69 aa)
amyACytoplasmic alpha-amylase; Protein involved in carbohydrate catabolic process and polysaccharide catabolic process; Belongs to the glycosyl hydrolase 13 family. (495 aa)
bglXbeta-D-glucoside glucohydrolase, periplasmic; Protein involved in carbohydrate catabolic process; Belongs to the glycosyl hydrolase 3 family. (765 aa)
fkpAFKBP-type peptidyl-prolyl cis-trans isomerase (rotamase); PPIases accelerate the folding of proteins. It catalyzes the cis-trans isomerization of proline imidic peptide bonds in oligopeptides. (270 aa)
slyDFKBP-type peptidyl prolyl cis-trans isomerase (rotamase); Folding helper with both chaperone and peptidyl-prolyl cis- trans isomerase (PPIase) activities. Chaperone activity prevents aggregation of unfolded or partially folded proteins and promotes their correct folding. PPIases catalyze the cis-trans isomerization of Xaa- Pro bonds of peptides, which accelerates slow steps of protein folding and thus shortens the lifetime of intermediates. Both strategies lower the concentration of intermediates and increase the productivity and yield of the folding reaction. SlyD could be involved in [...] (196 aa)
ppiAPeptidyl-prolyl cis-trans isomerase A (rotamase A); PPIases accelerate the folding of proteins. It catalyzes the cis-trans isomerization of proline imidic peptide bonds in oligopeptides; Belongs to the cyclophilin-type PPIase family. (190 aa)
cspARNA chaperone and antiterminator, cold-inducible; Binds to and stimulates the transcription of the CCAAT- containing, cold-shock-inducible promoters of the H-NS and GyrA proteins. Binds also to the inverted repeat 5'-ATTGG-3'. (70 aa)
malSAlpha-amylase; Since only maltooligosaccharides up to a chain length of 6 glucose units are actively transported through the cytoplasmic membrane via the membrane-bound complex of three proteins, MalF, MalG, and MalK, longer maltooligosaccharides must first be degraded by the periplasmic alpha-amylase, the MalS protein; Belongs to the glycosyl hydrolase 13 family. (676 aa)
cutADivalent-cation tolerance protein, copper sensitivity; Involved in resistance toward heavy metals. Belongs to the CutA family. (112 aa)
groLCpn60 chaperonin GroEL, large subunit of GroESL; Prevents misfolding and promotes the refolding and proper assembly of unfolded polypeptides generated under stress conditions. (548 aa)
fklBFKBP-type peptidyl-prolyl cis-trans isomerase (rotamase); PPIases accelerate the folding of proteins. It catalyzes the cis-trans isomerization of proline imidic peptide bonds in oligopeptides. (206 aa)
Your Current Organism:
Escherichia coli K12
NCBI taxonomy Id: 511145
Other names: E. coli str. K-12 substr. MG1655, Escherichia coli MG1655, Escherichia coli str. K-12 substr. MG1655, Escherichia coli str. K12 substr. MG1655, Escherichia coli str. MG1655, Escherichia coli strain MG1655
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