JG24_30345 protein (Klebsiella pneumoniae) - STRING interaction network
"JG24_30345" - Periplasmic serine endoprotease DegP-like in Klebsiella pneumoniae
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second shell of interactors
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proteins of unknown 3D structure
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some 3D structure is known or predicted
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Known Interactions
from curated databases
experimentally determined
Predicted Interactions
gene neighborhood
gene fusions
gene co-occurrence
protein homology
Your Input:
Gene Fusion
JG24_30345Periplasmic serine endoprotease DegP-like; Protease Do; required at high temperature; degrades damaged proteins; Derived by automated computational analysis using gene prediction method- Protein Homology; Belongs to the peptidase S1C family (477 aa)    
Predicted Functional Partners:
ATP-dependent Clp protease ATP-binding 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 (424 aa)
ATP-dependent Clp protease proteolytic subunit; 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 (207 aa)
Anti-sigma-E factor RseA; An anti-sigma factor for extracytoplasmic function (ECF) sigma factor sigma-E (RpoE). ECF sigma factors are held in an inactive form by an anti-sigma factor until released by regulated intramembrane proteolysis (RIP). RIP occurs when an extracytoplasmic signal triggers a concerted proteolytic cascade to transmit information and elicit cellular responses. The membrane-spanning regulatory substrate protein is first cut periplasmically (site-1 protease, S1P, DegS), then within the membrane itself (site-2 protease, S2P, RseP), while cytoplasmic proteases finish de [...] (216 aa)
Outer membrane protein A; OmpA is believed to be a porin, involved in diffusion of nonspecific small solutes across the outer membrane. It is the most abundant integral protein of the outer membrane of E. coli, and it is known to play a role as a phage receptor, a mediator of F-factor dependent conjugation, and in maintaining the structural shape of the outer membrane; 3a; II*; G; d; Derived by automated computational analysis using gene prediction method- Protein Homology (358 aa)
Peptide deformylase; Removes the formyl group from the N-terminal Met of newly synthesized proteins. Requires at least a dipeptide for an efficient rate of reaction. N-terminal L-methionine is a prerequisite for activity but the enzyme has broad specificity at other positions (169 aa)
Membrane protein insertase YidC; Required for the insertion and/or proper folding and/or complex formation of integral membrane proteins into the membrane. Involved in integration of membrane proteins that insert both dependently and independently of the Sec translocase complex, as well as at least some lipoproteins. Aids folding of multispanning membrane proteins (548 aa)
60 kDa chaperonin; Prevents misfolding and promotes the refolding and proper assembly of unfolded polypeptides generated under stress conditions (548 aa)
dGTPase; dGTPase preferentially hydrolyzes dGTP over the other canonical NTPs (504 aa)
Signal peptidase I; Catalyzes the cleavage of the amino-terminal leader peptide from secretory proteins; Derived by automated computational analysis using gene prediction method- Protein Homology; Belongs to the peptidase S26 family (324 aa)
Multimodular transpeptidase-transglycosylase; Penicillin-binding protein 1b; contains transglycosylase and transpeptidase activity; major enzyme for peptidoglycan biosynthesis in Escherichia coli; transmembrane protein; forms dimers; three variants, one of which may be a degradation product, while the other appears to result from an alternative initiation site, are found within the cell; Derived by automated computational analysis using gene prediction method- Protein Homology (854 aa)
Your Current Organism:
Klebsiella pneumoniae
NCBI taxonomy Id: 573
Other names: ATCC 13883, Bacillus pneumoniae, Bacterium pneumoniae crouposae, CCUG 225, CIP 82.91, DSM 30104, HAMBI 450, Hyalococcus pneumoniae, IFO 14940, K. pneumoniae, Klebsiella pneumoniae, Klebsiella sp. M-AI-2, Klebsiella sp. PB12, Klebsiella sp. RCE-7, LMG 2095, NBRC 14940, NCTC 9633
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