STRINGSTRING
ftsH ftsH AEV66909.1 AEV66909.1 AEV66920.1 AEV66920.1 AEV66921.1 AEV66921.1 AEV66968.1 AEV66968.1 AEV66971.1 AEV66971.1 AEV67109.1 AEV67109.1 clpB clpB AEV67125.1 AEV67125.1 AEV67259.1 AEV67259.1 AEV67260.1 AEV67260.1 mcsB mcsB AEV67262.1 AEV67262.1 AEV67313.1 AEV67313.1 AEV67314.1 AEV67314.1 AEV67315.1 AEV67315.1 AEV67316.1 AEV67316.1 clpP clpP clpX clpX AEV67553.1 AEV67553.1 AEV67554.1 AEV67554.1 AEV67562.1 AEV67562.1 AEV67735.1 AEV67735.1 lon lon AEV67784.1 AEV67784.1 AEV68103.1 AEV68103.1 AEV68104.1 AEV68104.1 AEV68292.1 AEV68292.1 AEV68429.1 AEV68429.1 AEV68495.1 AEV68495.1 AEV68845.1 AEV68845.1 AEV69161.1 AEV69161.1 dnaJ dnaJ dnaK dnaK grpE grpE hrcA hrcA AEV69450.1 AEV69450.1 AEV69451.1 AEV69451.1 AEV69452.1 AEV69452.1 AEV69623.1 AEV69623.1 AEV69654.1 AEV69654.1 AEV69667.1 AEV69667.1 msrB msrB AEV69928.1 AEV69928.1 AEV70294.1 AEV70294.1 groL groL groS groS AEV70579.1 AEV70579.1
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:
ftsHATP-dependent metalloprotease FtsH; Acts as a processive, ATP-dependent zinc metallopeptidase for both cytoplasmic and membrane proteins. Plays a role in the quality control of integral membrane proteins; Belongs to the AAA ATPase family. In the central section; belongs to the AAA ATPase family. (603 aa)
AEV66909.1TIGRFAM: small redox-active disulfide protein 2. (75 aa)
AEV66920.1Actin-like ATPase involved in cell division; PFAM: StbA protein. (302 aa)
AEV66921.1Hypothetical protein. (96 aa)
AEV66968.1Protein-tyrosine-phosphatase; PFAM: Low molecular weight phosphotyrosine protein phosphatase; TIGRFAM: arsenate reductase, glutathione/glutaredoxin type. (133 aa)
AEV66971.1TIGRFAM: small redox-active disulfide protein 2. (75 aa)
AEV67109.1DnaJ-class molecular chaperone with C-terminal Zn finger domain; PFAM: DnaJ domain; DnaJ C terminal region. (312 aa)
clpBATP-dependent chaperone ClpB; Part of a stress-induced multi-chaperone system, it is involved in the recovery of the cell from heat-induced damage, in cooperation with DnaK, DnaJ and GrpE; Belongs to the ClpA/ClpB family. (864 aa)
AEV67125.1Molecular chaperone (small heat shock protein); PFAM: Hsp20/alpha crystallin family; Belongs to the small heat shock protein (HSP20) family. (151 aa)
AEV67259.1PFAM: Firmicute transcriptional repressor of class III stress genes (CtsR); Belongs to the CtsR family. (153 aa)
AEV67260.1Uncharacterized protein with conserved CXXC pairs; PFAM: UvrB/uvrC motif. (165 aa)
mcsBArginine kinase; Catalyzes the specific phosphorylation of arginine residues in proteins. (342 aa)
AEV67262.1ATPase with chaperone activity, ATP-binding subunit; PFAM: AAA domain (Cdc48 subfamily); C-terminal, D2-small domain, of ClpB protein; Clp amino terminal domain; ATPase family associated with various cellular activities (AAA); Belongs to the ClpA/ClpB family. (810 aa)
AEV67313.1PFAM: Cytochrome C biogenesis protein transmembrane region. (222 aa)
AEV67314.1Peroxiredoxin; PFAM: AhpC/TSA family. (199 aa)
AEV67315.1Thioredoxin-disulfide reductase; PFAM: Thioredoxin; Pyridine nucleotide-disulphide oxidoreductase; TIGRFAM: thioredoxin-disulfide reductase. (426 aa)
AEV67316.1Thioredoxin reductase; PFAM: Pyridine nucleotide-disulphide oxidoreductase. (298 aa)
clpPATP-dependent Clp protease, proteolytic subunit ClpP; Cleaves peptides in various proteins in a process that requires ATP hydrolysis. Has a chymotrypsin-like activity. Plays a major role in the degradation of misfolded proteins. Belongs to the peptidase S14 family. (194 aa)
clpXEndopeptidase Clp ATP-binding regulatory subunit ClpX; ATP-dependent specificity component of the Clp protease. It directs the protease to specific substrates. Can perform chaperone functions in the absence of ClpP. (431 aa)
AEV67553.1Peroxiredoxin; Thiol-specific peroxidase that catalyzes the reduction of hydrogen peroxide and organic hydroperoxides to water and alcohols, respectively. Plays a role in cell protection against oxidative stress by detoxifying peroxides; Belongs to the peroxiredoxin family. AhpC/Prx1 subfamily. (187 aa)
AEV67554.1Alkyl hydroperoxide reductase, F subunit; PFAM: Pyridine nucleotide-disulphide oxidoreductase; TIGRFAM: alkyl hydroperoxide reductase, F subunit. (509 aa)
AEV67562.1Peroxiredoxin; Thiol-specific peroxidase that catalyzes the reduction of hydrogen peroxide and organic hydroperoxides to water and alcohols, respectively. Plays a role in cell protection against oxidative stress by detoxifying peroxides; Belongs to the peroxiredoxin family. AhpC/Prx1 subfamily. (187 aa)
AEV67735.1Peroxiredoxin; Thiol-specific peroxidase that catalyzes the reduction of hydrogen peroxide and organic hydroperoxides to water and alcohols, respectively. Plays a role in cell protection against oxidative stress by detoxifying peroxides. (219 aa)
lonATP-dependent protease La; ATP-dependent serine protease that mediates the selective degradation of mutant and abnormal proteins as well as certain short- lived regulatory proteins. Required for cellular homeostasis and for survival from DNA damage and developmental changes induced by stress. Degrades polypeptides processively to yield small peptide fragments that are 5 to 10 amino acids long. Binds to DNA in a double-stranded, site-specific manner. (811 aa)
AEV67784.1PFAM: Negative regulator of genetic competence (MecA). (208 aa)
AEV68103.1HflK protein; HflC and HflK could encode or regulate a protease. (321 aa)
AEV68104.1Membrane protease subunit, stomatin/prohibitin; HflC and HflK could regulate a protease. (287 aa)
AEV68292.1PFAM: Tetratricopeptide repeat. (331 aa)
AEV68429.1Molecular chaperone; PFAM: Hsp70 protein; Belongs to the heat shock protein 70 family. (566 aa)
AEV68495.1Trypsin-like serine protease with C-terminal PDZ domain; PFAM: Trypsin. (276 aa)
AEV68845.1Trypsin-like serine protease with C-terminal PDZ domain; PFAM: Trypsin; PDZ domain (Also known as DHR or GLGF). (482 aa)
AEV69161.1Molecular chaperone of HSP90 family; PFAM: Histidine kinase-, DNA gyrase B-, and HSP90-like ATPase; Hsp90 protein. (631 aa)
dnaJChaperone protein DnaJ; Participates actively in the response to hyperosmotic and heat shock by preventing the aggregation of stress-denatured proteins and by disaggregating proteins, also in an autonomous, DnaK-independent fashion. Unfolded proteins bind initially to DnaJ; upon interaction with the DnaJ-bound protein, DnaK hydrolyzes its bound ATP, resulting in the formation of a stable complex. GrpE releases ADP from DnaK; ATP binding to DnaK triggers the release of the substrate protein, thus completing the reaction cycle. Several rounds of ATP-dependent interactions between DnaJ, D [...] (383 aa)
dnaKChaperone protein DnaK; Acts as a chaperone; Belongs to the heat shock protein 70 family. (612 aa)
grpEMolecular chaperone GrpE (heat shock protein); Participates actively in the response to hyperosmotic and heat shock by preventing the aggregation of stress-denatured proteins, in association with DnaK and GrpE. It is the nucleotide exchange factor for DnaK and may function as a thermosensor. Unfolded proteins bind initially to DnaJ; upon interaction with the DnaJ-bound protein, DnaK hydrolyzes its bound ATP, resulting in the formation of a stable complex. GrpE releases ADP from DnaK; ATP binding to DnaK triggers the release of the substrate protein, thus completing the reaction cycle. [...] (218 aa)
hrcAHeat shock gene repressor HrcA; Negative regulator of class I heat shock genes (grpE-dnaK- dnaJ and groELS operons). Prevents heat-shock induction of these operons. (374 aa)
AEV69450.1PFAM: Protein of unknown function (DUF1266). (251 aa)
AEV69451.1DnaJ-class molecular chaperone with C-terminal Zn finger domain; PFAM: DnaJ domain; Tetratricopeptide repeat; manually curated. (433 aa)
AEV69452.1Molecular chaperone; PFAM: Hsp70 protein; Belongs to the heat shock protein 70 family. (565 aa)
AEV69623.1PFAM: Thioredoxin; TIGRFAM: thioredoxin; protein disulfide-isomerase domain; Belongs to the thioredoxin family. (110 aa)
AEV69654.1ATPase with chaperone activity, ATP-binding subunit; PFAM: AAA domain (Cdc48 subfamily); C-terminal, D2-small domain, of ClpB protein; ATPase family associated with various cellular activities (AAA); Belongs to the ClpA/ClpB family. (787 aa)
AEV69667.1PFAM: ATPase family associated with various cellular activities (AAA); Tetratricopeptide repeat; Belongs to the AAA ATPase family. (427 aa)
msrBmethionine-R-sulfoxide reductase/methionine-S-sulfoxide reductase; Has an important function as a repair enzyme for proteins that have been inactivated by oxidation. Catalyzes the reversible oxidation-reduction of methionine sulfoxide in proteins to methionine. (331 aa)
AEV69928.1Membrane protease subunit, stomatin/prohibitin; PFAM: SPFH domain / Band 7 family. (374 aa)
AEV70294.1ATP-dependent Zn protease; PFAM: FtsH Extracellular; ATPase family associated with various cellular activities (AAA); Belongs to the AAA ATPase family. (394 aa)
groLChaperonin GroL; Prevents misfolding and promotes the refolding and proper assembly of unfolded polypeptides generated under stress conditions. (545 aa)
groSCo-chaperonin GroES; Binds to Cpn60 in the presence of Mg-ATP and suppresses the ATPase activity of the latter. (94 aa)
AEV70579.1Trypsin-like serine protease with C-terminal PDZ domain; PFAM: Trypsin; PDZ domain (Also known as DHR or GLGF). (406 aa)
Your Current Organism:
Hungateiclostridium clariflavum
NCBI taxonomy Id: 720554
Other names: Clostridium clariflavum DSM 19732, Clostridium clariflavum EBR45, H. clariflavum DSM 19732, Hungateiclostridium clariflavum DSM 19732
Server load: low (14%) [HD]
STRING is a Core Data Resource as designated by Global Biodata Coalition and ELIXIR.