| node1 | node2 | node1 accession | node2 accession | node1 annotation | node2 annotation | score |
| CKO_01004 | CKO_02896 | CKO_01004 | CKO_02896 | Hypothetical protein; FliG is one of three proteins (FliG, FliN, FliM) that forms the rotor-mounted switch complex (C ring), located at the base of the basal body. This complex interacts with the CheY and CheZ chemotaxis proteins, in addition to contacting components of the motor that determine the direction of flagellar rotation. | Hypothetical protein; COG: COG1536 Flagellar motor switch protein; Psort location: Cytoplasmic, score:9.12. | 0.922 |
| CKO_01004 | CKO_04200 | CKO_01004 | CKO_04200 | Hypothetical protein; FliG is one of three proteins (FliG, FliN, FliM) that forms the rotor-mounted switch complex (C ring), located at the base of the basal body. This complex interacts with the CheY and CheZ chemotaxis proteins, in addition to contacting components of the motor that determine the direction of flagellar rotation. | Hypothetical protein; Accelerates the degradation of transcripts by removing pyrophosphate from the 5'-end of triphosphorylated RNA, leading to a more labile monophosphorylated state that can stimulate subsequent ribonuclease cleavage; Belongs to the Nudix hydrolase family. | 0.535 |
| CKO_02526 | CKO_04200 | CKO_02526 | CKO_04200 | Hypothetical protein; KEGG: sec:SC0666 1.8e-212 dacA; D-alanyl-D-alanine carboxypeptidase, penicillin-binding protein 5 K07258; COG: COG1686 D-alanyl-D-alanine carboxypeptidase; Belongs to the peptidase S11 family. | Hypothetical protein; Accelerates the degradation of transcripts by removing pyrophosphate from the 5'-end of triphosphorylated RNA, leading to a more labile monophosphorylated state that can stimulate subsequent ribonuclease cleavage; Belongs to the Nudix hydrolase family. | 0.534 |
| CKO_02896 | CKO_01004 | CKO_02896 | CKO_01004 | Hypothetical protein; COG: COG1536 Flagellar motor switch protein; Psort location: Cytoplasmic, score:9.12. | Hypothetical protein; FliG is one of three proteins (FliG, FliN, FliM) that forms the rotor-mounted switch complex (C ring), located at the base of the basal body. This complex interacts with the CheY and CheZ chemotaxis proteins, in addition to contacting components of the motor that determine the direction of flagellar rotation. | 0.922 |
| CKO_02896 | CKO_04200 | CKO_02896 | CKO_04200 | Hypothetical protein; COG: COG1536 Flagellar motor switch protein; Psort location: Cytoplasmic, score:9.12. | Hypothetical protein; Accelerates the degradation of transcripts by removing pyrophosphate from the 5'-end of triphosphorylated RNA, leading to a more labile monophosphorylated state that can stimulate subsequent ribonuclease cleavage; Belongs to the Nudix hydrolase family. | 0.535 |
| CKO_04199 | CKO_04200 | CKO_04199 | CKO_04200 | Hypothetical protein; KEGG: spt:SPA2868 0. ptsP; phosphoenolpyruvate-protein phosphotransferase K08484; COG: COG3605 Signal transduction protein containing GAF and PtsI domains; Belongs to the PEP-utilizing enzyme family. | Hypothetical protein; Accelerates the degradation of transcripts by removing pyrophosphate from the 5'-end of triphosphorylated RNA, leading to a more labile monophosphorylated state that can stimulate subsequent ribonuclease cleavage; Belongs to the Nudix hydrolase family. | 0.801 |
| CKO_04200 | CKO_01004 | CKO_04200 | CKO_01004 | Hypothetical protein; Accelerates the degradation of transcripts by removing pyrophosphate from the 5'-end of triphosphorylated RNA, leading to a more labile monophosphorylated state that can stimulate subsequent ribonuclease cleavage; Belongs to the Nudix hydrolase family. | Hypothetical protein; FliG is one of three proteins (FliG, FliN, FliM) that forms the rotor-mounted switch complex (C ring), located at the base of the basal body. This complex interacts with the CheY and CheZ chemotaxis proteins, in addition to contacting components of the motor that determine the direction of flagellar rotation. | 0.535 |
| CKO_04200 | CKO_02526 | CKO_04200 | CKO_02526 | Hypothetical protein; Accelerates the degradation of transcripts by removing pyrophosphate from the 5'-end of triphosphorylated RNA, leading to a more labile monophosphorylated state that can stimulate subsequent ribonuclease cleavage; Belongs to the Nudix hydrolase family. | Hypothetical protein; KEGG: sec:SC0666 1.8e-212 dacA; D-alanyl-D-alanine carboxypeptidase, penicillin-binding protein 5 K07258; COG: COG1686 D-alanyl-D-alanine carboxypeptidase; Belongs to the peptidase S11 family. | 0.534 |
| CKO_04200 | CKO_02896 | CKO_04200 | CKO_02896 | Hypothetical protein; Accelerates the degradation of transcripts by removing pyrophosphate from the 5'-end of triphosphorylated RNA, leading to a more labile monophosphorylated state that can stimulate subsequent ribonuclease cleavage; Belongs to the Nudix hydrolase family. | Hypothetical protein; COG: COG1536 Flagellar motor switch protein; Psort location: Cytoplasmic, score:9.12. | 0.535 |
| CKO_04200 | CKO_04199 | CKO_04200 | CKO_04199 | Hypothetical protein; Accelerates the degradation of transcripts by removing pyrophosphate from the 5'-end of triphosphorylated RNA, leading to a more labile monophosphorylated state that can stimulate subsequent ribonuclease cleavage; Belongs to the Nudix hydrolase family. | Hypothetical protein; KEGG: spt:SPA2868 0. ptsP; phosphoenolpyruvate-protein phosphotransferase K08484; COG: COG3605 Signal transduction protein containing GAF and PtsI domains; Belongs to the PEP-utilizing enzyme family. | 0.801 |
| CKO_04200 | birA | CKO_04200 | CKO_03018 | Hypothetical protein; Accelerates the degradation of transcripts by removing pyrophosphate from the 5'-end of triphosphorylated RNA, leading to a more labile monophosphorylated state that can stimulate subsequent ribonuclease cleavage; Belongs to the Nudix hydrolase family. | Hypothetical protein; Acts both as a biotin--[acetyl-CoA-carboxylase] ligase and a biotin-operon repressor. In the presence of ATP, BirA activates biotin to form the BirA-biotinyl-5'-adenylate (BirA-bio-5'-AMP or holoBirA) complex. HoloBirA can either transfer the biotinyl moiety to the biotin carboxyl carrier protein (BCCP) subunit of acetyl-CoA carboxylase, or bind to the biotin operator site and inhibit transcription of the operon. | 0.731 |
| CKO_04200 | dapF | CKO_04200 | CKO_00151 | Hypothetical protein; Accelerates the degradation of transcripts by removing pyrophosphate from the 5'-end of triphosphorylated RNA, leading to a more labile monophosphorylated state that can stimulate subsequent ribonuclease cleavage; Belongs to the Nudix hydrolase family. | Hypothetical protein; Catalyzes the stereoinversion of LL-2,6-diaminoheptanedioate (L,L-DAP) to meso-diaminoheptanedioate (meso-DAP), a precursor of L- lysine and an essential component of the bacterial peptidoglycan. | 0.831 |
| CKO_04200 | hfq | CKO_04200 | CKO_03663 | Hypothetical protein; Accelerates the degradation of transcripts by removing pyrophosphate from the 5'-end of triphosphorylated RNA, leading to a more labile monophosphorylated state that can stimulate subsequent ribonuclease cleavage; Belongs to the Nudix hydrolase family. | Hypothetical protein; RNA chaperone that binds small regulatory RNA (sRNAs) and mRNAs to facilitate mRNA translational regulation in response to envelope stress, environmental stress and changes in metabolite concentrations. Also binds with high specificity to tRNAs. Belongs to the Hfq family. | 0.575 |
| CKO_04200 | nnrE | CKO_04200 | CKO_03669 | Hypothetical protein; Accelerates the degradation of transcripts by removing pyrophosphate from the 5'-end of triphosphorylated RNA, leading to a more labile monophosphorylated state that can stimulate subsequent ribonuclease cleavage; Belongs to the Nudix hydrolase family. | Hypothetical protein; Bifunctional enzyme that catalyzes the epimerization of the S- and R-forms of NAD(P)HX and the dehydration of the S-form of NAD(P)HX at the expense of ADP, which is converted to AMP. This allows the repair of both epimers of NAD(P)HX, a damaged form of NAD(P)H that is a result of enzymatic or heat-dependent hydration. Catalyzes the epimerization of the S- and R-forms of NAD(P)HX, a damaged form of NAD(P)H that is a result of enzymatic or heat-dependent hydration. This is a prerequisite for the S-specific NAD(P)H-hydrate dehydratase to allow the repair of both epi [...] | 0.838 |
| CKO_04200 | rnr | CKO_04200 | CKO_03653 | Hypothetical protein; Accelerates the degradation of transcripts by removing pyrophosphate from the 5'-end of triphosphorylated RNA, leading to a more labile monophosphorylated state that can stimulate subsequent ribonuclease cleavage; Belongs to the Nudix hydrolase family. | Hypothetical protein; 3'-5' exoribonuclease that releases 5'-nucleoside monophosphates and is involved in maturation of structured RNAs. Belongs to the RNR ribonuclease family. RNase R subfamily. | 0.648 |
| CKO_04200 | ybeY | CKO_04200 | CKO_02504 | Hypothetical protein; Accelerates the degradation of transcripts by removing pyrophosphate from the 5'-end of triphosphorylated RNA, leading to a more labile monophosphorylated state that can stimulate subsequent ribonuclease cleavage; Belongs to the Nudix hydrolase family. | Hypothetical protein; Single strand-specific metallo-endoribonuclease involved in late-stage 70S ribosome quality control and in maturation of the 3' terminus of the 16S rRNA. | 0.601 |
| birA | CKO_04200 | CKO_03018 | CKO_04200 | Hypothetical protein; Acts both as a biotin--[acetyl-CoA-carboxylase] ligase and a biotin-operon repressor. In the presence of ATP, BirA activates biotin to form the BirA-biotinyl-5'-adenylate (BirA-bio-5'-AMP or holoBirA) complex. HoloBirA can either transfer the biotinyl moiety to the biotin carboxyl carrier protein (BCCP) subunit of acetyl-CoA carboxylase, or bind to the biotin operator site and inhibit transcription of the operon. | Hypothetical protein; Accelerates the degradation of transcripts by removing pyrophosphate from the 5'-end of triphosphorylated RNA, leading to a more labile monophosphorylated state that can stimulate subsequent ribonuclease cleavage; Belongs to the Nudix hydrolase family. | 0.731 |
| birA | dapF | CKO_03018 | CKO_00151 | Hypothetical protein; Acts both as a biotin--[acetyl-CoA-carboxylase] ligase and a biotin-operon repressor. In the presence of ATP, BirA activates biotin to form the BirA-biotinyl-5'-adenylate (BirA-bio-5'-AMP or holoBirA) complex. HoloBirA can either transfer the biotinyl moiety to the biotin carboxyl carrier protein (BCCP) subunit of acetyl-CoA carboxylase, or bind to the biotin operator site and inhibit transcription of the operon. | Hypothetical protein; Catalyzes the stereoinversion of LL-2,6-diaminoheptanedioate (L,L-DAP) to meso-diaminoheptanedioate (meso-DAP), a precursor of L- lysine and an essential component of the bacterial peptidoglycan. | 0.520 |
| birA | hfq | CKO_03018 | CKO_03663 | Hypothetical protein; Acts both as a biotin--[acetyl-CoA-carboxylase] ligase and a biotin-operon repressor. In the presence of ATP, BirA activates biotin to form the BirA-biotinyl-5'-adenylate (BirA-bio-5'-AMP or holoBirA) complex. HoloBirA can either transfer the biotinyl moiety to the biotin carboxyl carrier protein (BCCP) subunit of acetyl-CoA carboxylase, or bind to the biotin operator site and inhibit transcription of the operon. | Hypothetical protein; RNA chaperone that binds small regulatory RNA (sRNAs) and mRNAs to facilitate mRNA translational regulation in response to envelope stress, environmental stress and changes in metabolite concentrations. Also binds with high specificity to tRNAs. Belongs to the Hfq family. | 0.416 |
| birA | nnrE | CKO_03018 | CKO_03669 | Hypothetical protein; Acts both as a biotin--[acetyl-CoA-carboxylase] ligase and a biotin-operon repressor. In the presence of ATP, BirA activates biotin to form the BirA-biotinyl-5'-adenylate (BirA-bio-5'-AMP or holoBirA) complex. HoloBirA can either transfer the biotinyl moiety to the biotin carboxyl carrier protein (BCCP) subunit of acetyl-CoA carboxylase, or bind to the biotin operator site and inhibit transcription of the operon. | Hypothetical protein; Bifunctional enzyme that catalyzes the epimerization of the S- and R-forms of NAD(P)HX and the dehydration of the S-form of NAD(P)HX at the expense of ADP, which is converted to AMP. This allows the repair of both epimers of NAD(P)HX, a damaged form of NAD(P)H that is a result of enzymatic or heat-dependent hydration. Catalyzes the epimerization of the S- and R-forms of NAD(P)HX, a damaged form of NAD(P)H that is a result of enzymatic or heat-dependent hydration. This is a prerequisite for the S-specific NAD(P)H-hydrate dehydratase to allow the repair of both epi [...] | 0.440 |
STRING v12.5 is now available!
