node1 | node2 | node1 accession | node2 accession | node1 annotation | node2 annotation | score |
CLPP | DEF | WS2210 | WS2212 | 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. | POLYPEPTIDE DEFORMYLASE PDF FORMYLMETHIONINEDEFORMYLASE; 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. | 0.909 |
CLPP | FLII | WS2210 | WS2207 | 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. | FLAGELLUM-SPECIFIC ATP SYNTHASE. | 0.610 |
CLPP | TIG | WS2210 | WS2209 | 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. | PUTATIVE TRIGGER FACTOR PROTEIN; Involved in protein export. Acts as a chaperone by maintaining the newly synthesized protein in an open conformation. Functions as a peptidyl-prolyl cis-trans isomerase; Belongs to the FKBP-type PPIase family. Tig subfamily. | 0.939 |
CLPP | WS0850 | WS2210 | WS0850 | 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. | SENSORY TRANSDUCTION HISTIDINE KINASE. | 0.477 |
CLPP | WS2211 | WS2210 | WS2211 | 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. | Hypothetical protein. | 0.772 |
CLPP | WS2213 | WS2210 | WS2213 | 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. | SIGMA-54 INTERACTING PROTEIN. | 0.760 |
DEF | CLPP | WS2212 | WS2210 | POLYPEPTIDE DEFORMYLASE PDF FORMYLMETHIONINEDEFORMYLASE; 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. | 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. | 0.909 |
DEF | FLII | WS2212 | WS2207 | POLYPEPTIDE DEFORMYLASE PDF FORMYLMETHIONINEDEFORMYLASE; 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. | FLAGELLUM-SPECIFIC ATP SYNTHASE. | 0.571 |
DEF | RUVC | WS2212 | WS2229 | POLYPEPTIDE DEFORMYLASE PDF FORMYLMETHIONINEDEFORMYLASE; 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. | CROSSOVER JUNCTION ENDODEOXYRIBONUCLEASE; Nuclease that resolves Holliday junction intermediates in genetic recombination. Cleaves the cruciform structure in supercoiled DNA by nicking to strands with the same polarity at sites symmetrically opposed at the junction in the homologous arms and leaves a 5'-terminal phosphate and a 3'-terminal hydroxyl group. | 0.408 |
DEF | TIG | WS2212 | WS2209 | POLYPEPTIDE DEFORMYLASE PDF FORMYLMETHIONINEDEFORMYLASE; 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. | PUTATIVE TRIGGER FACTOR PROTEIN; Involved in protein export. Acts as a chaperone by maintaining the newly synthesized protein in an open conformation. Functions as a peptidyl-prolyl cis-trans isomerase; Belongs to the FKBP-type PPIase family. Tig subfamily. | 0.962 |
DEF | WS2211 | WS2212 | WS2211 | POLYPEPTIDE DEFORMYLASE PDF FORMYLMETHIONINEDEFORMYLASE; 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. | Hypothetical protein. | 0.794 |
DEF | WS2213 | WS2212 | WS2213 | POLYPEPTIDE DEFORMYLASE PDF FORMYLMETHIONINEDEFORMYLASE; 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. | SIGMA-54 INTERACTING PROTEIN. | 0.942 |
FLII | CLPP | WS2207 | WS2210 | FLAGELLUM-SPECIFIC ATP SYNTHASE. | 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. | 0.610 |
FLII | DEF | WS2207 | WS2212 | FLAGELLUM-SPECIFIC ATP SYNTHASE. | POLYPEPTIDE DEFORMYLASE PDF FORMYLMETHIONINEDEFORMYLASE; 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. | 0.571 |
FLII | TIG | WS2207 | WS2209 | FLAGELLUM-SPECIFIC ATP SYNTHASE. | PUTATIVE TRIGGER FACTOR PROTEIN; Involved in protein export. Acts as a chaperone by maintaining the newly synthesized protein in an open conformation. Functions as a peptidyl-prolyl cis-trans isomerase; Belongs to the FKBP-type PPIase family. Tig subfamily. | 0.610 |
FLII | WS0850 | WS2207 | WS0850 | FLAGELLUM-SPECIFIC ATP SYNTHASE. | SENSORY TRANSDUCTION HISTIDINE KINASE. | 0.677 |
FLII | WS1801 | WS2207 | WS1801 | FLAGELLUM-SPECIFIC ATP SYNTHASE. | FLAGELLAR BASAL-BODY ROD PROTEIN FLGG. | 0.895 |
FLII | WS2211 | WS2207 | WS2211 | FLAGELLUM-SPECIFIC ATP SYNTHASE. | Hypothetical protein. | 0.678 |
FLII | WS2213 | WS2207 | WS2213 | FLAGELLUM-SPECIFIC ATP SYNTHASE. | SIGMA-54 INTERACTING PROTEIN. | 0.579 |
RUVC | DEF | WS2229 | WS2212 | CROSSOVER JUNCTION ENDODEOXYRIBONUCLEASE; Nuclease that resolves Holliday junction intermediates in genetic recombination. Cleaves the cruciform structure in supercoiled DNA by nicking to strands with the same polarity at sites symmetrically opposed at the junction in the homologous arms and leaves a 5'-terminal phosphate and a 3'-terminal hydroxyl group. | POLYPEPTIDE DEFORMYLASE PDF FORMYLMETHIONINEDEFORMYLASE; 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. | 0.408 |