node1 | node2 | node1 accession | node2 accession | node1 annotation | node2 annotation | score |
creD | pbpC | b4400 | b2519 | Inner membrane protein; Tolerance to colicin E2. | Penicillin-insensitive murein repair transglycosylase; Cell wall formation. The enzyme has a penicillin-insensitive transglycosylase N-terminal domain (formation of linear glycan strands) and a transpeptidase C-terminal domain which may not be functional. | 0.570 |
creD | yfhM | b4400 | b2520 | Inner membrane protein; Tolerance to colicin E2. | Bacterial alpha2-macroglobulin colonization factor ECAM; Protects the bacterial cell from host peptidases. Acts by a 'trapping' mechanism. Cleavage of the bait-region domain by host peptidases leads to a global conformational change, which results in entrapment of the host peptidase and activation of the thioester bond that covalently binds the attacking host peptidase. Trapped peptidases are still active except against very large substrates. May protect the entire periplam, including the lipoproteins anchored to the periplasmic side of the outer membrane, against intruding endopeptidases. | 0.546 |
nrdR | yfhM | b0413 | b2520 | Nrd regulon repressor; Represses transcription of the class Ib RNR genes nrdHIEF but has much smaller effect on transcription of the class Ia RNR genes nrdAB and class III RNR genes nrdDG. By binding to nrdR boxes in the promoter regions to alter promoter activity, nrdR differentially regulates nrdAB, nrdHIEF and nrdD transcription in aerobic growth. | Bacterial alpha2-macroglobulin colonization factor ECAM; Protects the bacterial cell from host peptidases. Acts by a 'trapping' mechanism. Cleavage of the bait-region domain by host peptidases leads to a global conformational change, which results in entrapment of the host peptidase and activation of the thioester bond that covalently binds the attacking host peptidase. Trapped peptidases are still active except against very large substrates. May protect the entire periplam, including the lipoproteins anchored to the periplasmic side of the outer membrane, against intruding endopeptidases. | 0.778 |
pbpC | creD | b2519 | b4400 | Penicillin-insensitive murein repair transglycosylase; Cell wall formation. The enzyme has a penicillin-insensitive transglycosylase N-terminal domain (formation of linear glycan strands) and a transpeptidase C-terminal domain which may not be functional. | Inner membrane protein; Tolerance to colicin E2. | 0.570 |
pbpC | sseA | b2519 | b2521 | Penicillin-insensitive murein repair transglycosylase; Cell wall formation. The enzyme has a penicillin-insensitive transglycosylase N-terminal domain (formation of linear glycan strands) and a transpeptidase C-terminal domain which may not be functional. | 3-mercaptopyruvate sulfurtransferase; Transfers a sulfur ion to cyanide or to other thiol compounds. Also has weak rhodanese activity (130-fold lower). Its participation in detoxification of cyanide may be small. May be involved in the enhancement of serine sensitivity. | 0.489 |
pbpC | yfhM | b2519 | b2520 | Penicillin-insensitive murein repair transglycosylase; Cell wall formation. The enzyme has a penicillin-insensitive transglycosylase N-terminal domain (formation of linear glycan strands) and a transpeptidase C-terminal domain which may not be functional. | Bacterial alpha2-macroglobulin colonization factor ECAM; Protects the bacterial cell from host peptidases. Acts by a 'trapping' mechanism. Cleavage of the bait-region domain by host peptidases leads to a global conformational change, which results in entrapment of the host peptidase and activation of the thioester bond that covalently binds the attacking host peptidase. Trapped peptidases are still active except against very large substrates. May protect the entire periplam, including the lipoproteins anchored to the periplasmic side of the outer membrane, against intruding endopeptidases. | 0.997 |
sseA | pbpC | b2521 | b2519 | 3-mercaptopyruvate sulfurtransferase; Transfers a sulfur ion to cyanide or to other thiol compounds. Also has weak rhodanese activity (130-fold lower). Its participation in detoxification of cyanide may be small. May be involved in the enhancement of serine sensitivity. | Penicillin-insensitive murein repair transglycosylase; Cell wall formation. The enzyme has a penicillin-insensitive transglycosylase N-terminal domain (formation of linear glycan strands) and a transpeptidase C-terminal domain which may not be functional. | 0.489 |
sseA | yfhM | b2521 | b2520 | 3-mercaptopyruvate sulfurtransferase; Transfers a sulfur ion to cyanide or to other thiol compounds. Also has weak rhodanese activity (130-fold lower). Its participation in detoxification of cyanide may be small. May be involved in the enhancement of serine sensitivity. | Bacterial alpha2-macroglobulin colonization factor ECAM; Protects the bacterial cell from host peptidases. Acts by a 'trapping' mechanism. Cleavage of the bait-region domain by host peptidases leads to a global conformational change, which results in entrapment of the host peptidase and activation of the thioester bond that covalently binds the attacking host peptidase. Trapped peptidases are still active except against very large substrates. May protect the entire periplam, including the lipoproteins anchored to the periplasmic side of the outer membrane, against intruding endopeptidases. | 0.505 |
ulaR | yfhM | b4191 | b2520 | Transcriptional repressor for the L-ascorbate utilization divergent operon; Represses ulaG and the ulaABCDEF operon. Two ulaR binding sites have been identified in each promoter. Full activity requires simultaneous interaction of UlaR with both divergent promoters and seems to be dependent on repressor-mediated DNA loop formation, which is helped by the action of integration host factor. | Bacterial alpha2-macroglobulin colonization factor ECAM; Protects the bacterial cell from host peptidases. Acts by a 'trapping' mechanism. Cleavage of the bait-region domain by host peptidases leads to a global conformational change, which results in entrapment of the host peptidase and activation of the thioester bond that covalently binds the attacking host peptidase. Trapped peptidases are still active except against very large substrates. May protect the entire periplam, including the lipoproteins anchored to the periplasmic side of the outer membrane, against intruding endopeptidases. | 0.532 |
yfaA | yfaP | b2230 | b2225 | DUF2138 family protein, putative host defense protein. | DUF2135 family protein, putative host defense protein. | 0.956 |
yfaA | yfaQ | b2230 | b2226 | DUF2138 family protein, putative host defense protein. | Tandem DUF2300 domain protein, putative host defense protein. | 0.935 |
yfaA | yfaT | b2230 | b2229 | DUF2138 family protein, putative host defense protein. | Uncharacterized protein YfaT; Pseudogene, bacterial alpha2-macroglobulin YfaS variant family; putative membrane protein; To P.aeruginosa PA4490 and T.maritima TM0986. | 0.986 |
yfaA | yfhM | b2230 | b2520 | DUF2138 family protein, putative host defense protein. | Bacterial alpha2-macroglobulin colonization factor ECAM; Protects the bacterial cell from host peptidases. Acts by a 'trapping' mechanism. Cleavage of the bait-region domain by host peptidases leads to a global conformational change, which results in entrapment of the host peptidase and activation of the thioester bond that covalently binds the attacking host peptidase. Trapped peptidases are still active except against very large substrates. May protect the entire periplam, including the lipoproteins anchored to the periplasmic side of the outer membrane, against intruding endopeptidases. | 0.695 |
yfaP | yfaA | b2225 | b2230 | DUF2135 family protein, putative host defense protein. | DUF2138 family protein, putative host defense protein. | 0.956 |
yfaP | yfaQ | b2225 | b2226 | DUF2135 family protein, putative host defense protein. | Tandem DUF2300 domain protein, putative host defense protein. | 0.987 |
yfaP | yfaT | b2225 | b2229 | DUF2135 family protein, putative host defense protein. | Uncharacterized protein YfaT; Pseudogene, bacterial alpha2-macroglobulin YfaS variant family; putative membrane protein; To P.aeruginosa PA4490 and T.maritima TM0986. | 0.882 |
yfaP | yfhM | b2225 | b2520 | DUF2135 family protein, putative host defense protein. | Bacterial alpha2-macroglobulin colonization factor ECAM; Protects the bacterial cell from host peptidases. Acts by a 'trapping' mechanism. Cleavage of the bait-region domain by host peptidases leads to a global conformational change, which results in entrapment of the host peptidase and activation of the thioester bond that covalently binds the attacking host peptidase. Trapped peptidases are still active except against very large substrates. May protect the entire periplam, including the lipoproteins anchored to the periplasmic side of the outer membrane, against intruding endopeptidases. | 0.679 |
yfaQ | yfaA | b2226 | b2230 | Tandem DUF2300 domain protein, putative host defense protein. | DUF2138 family protein, putative host defense protein. | 0.935 |
yfaQ | yfaP | b2226 | b2225 | Tandem DUF2300 domain protein, putative host defense protein. | DUF2135 family protein, putative host defense protein. | 0.987 |
yfaQ | yfaT | b2226 | b2229 | Tandem DUF2300 domain protein, putative host defense protein. | Uncharacterized protein YfaT; Pseudogene, bacterial alpha2-macroglobulin YfaS variant family; putative membrane protein; To P.aeruginosa PA4490 and T.maritima TM0986. | 0.922 |