node1 | node2 | node1 accession | node2 accession | node1 annotation | node2 annotation | score |
Rv1954A | higA | Rv1954A | Rv1956 | Rv1954A, len: 100 aa. Hypothetical unknown protein. | Possible antitoxin HigA; Antitoxin component of an atypical, type II toxin-antitoxin chaperone (TAC) system. Upon expression in M.smegmatis neutralizes the effect of cognate toxin HigB1. Neutralization of HigB1 toxin in E.coli or M.marinum also requires SecB-like chaperone Rv1957, making this the first toxin-antitoxin chaperone (TAC) system. Antitoxin aggregation and degradation are prevented by the chaperone. | 0.554 |
Rv1954A | higB | Rv1954A | Rv1955 | Rv1954A, len: 100 aa. Hypothetical unknown protein. | Possible toxin HigB; Toxic component of an atypical, type II toxin-antitoxin chaperone (TAC) system. Upon expression in M.smegmatis inhibits colony formation and cell growth. Ectopic expression in wild-type M.tuberculosis has no effect on cell growth; ectopic expression in a triple higB1-higA1-Rv1957 (delta TAC) disruption mutant causes growth arrest, killing a considerable proportion of the cells. Increased ectopic expression leads to decreased levels of IdeR- and Zur-regulated genes as well as cleavage within the mRNA region of tmRNA (transfer-mRNA), strongly suggesting it is an endo [...] | 0.618 |
Rv1954A | secBL | Rv1954A | Rv1957 | Rv1954A, len: 100 aa. Hypothetical unknown protein. | Hypothetical protein; Chaperone component of an atypical, type II toxin-antitoxin chaperone (TAC) system. Prevents antitoxin HigA1 aggregation in vitro at a 1:3 chaperone:antitoxin ratio, probably also protects antitoxin HigA1 from protease. Required for neutralization of toxin HigB1 upon ectopic expression in Mycobacterium marinum or E.coli. When expressed in E.coli complements a secB deletion, restores export of OmpA and MBP and inhibits aggregation of proOmpC although it is less efficient than endogenous SecB. Complements the general chaperone function of E.coli SecB less well; Belo [...] | 0.661 |
higA | Rv1954A | Rv1956 | Rv1954A | Possible antitoxin HigA; Antitoxin component of an atypical, type II toxin-antitoxin chaperone (TAC) system. Upon expression in M.smegmatis neutralizes the effect of cognate toxin HigB1. Neutralization of HigB1 toxin in E.coli or M.marinum also requires SecB-like chaperone Rv1957, making this the first toxin-antitoxin chaperone (TAC) system. Antitoxin aggregation and degradation are prevented by the chaperone. | Rv1954A, len: 100 aa. Hypothetical unknown protein. | 0.554 |
higA | higA2 | Rv1956 | Rv2021c | Possible antitoxin HigA; Antitoxin component of an atypical, type II toxin-antitoxin chaperone (TAC) system. Upon expression in M.smegmatis neutralizes the effect of cognate toxin HigB1. Neutralization of HigB1 toxin in E.coli or M.marinum also requires SecB-like chaperone Rv1957, making this the first toxin-antitoxin chaperone (TAC) system. Antitoxin aggregation and degradation are prevented by the chaperone. | Transcriptional regulatory protein; Putative antitoxin component of a type II toxin-antitoxin (TA) system. Its cognate toxin would be HigB2. | 0.839 |
higA | higB | Rv1956 | Rv1955 | Possible antitoxin HigA; Antitoxin component of an atypical, type II toxin-antitoxin chaperone (TAC) system. Upon expression in M.smegmatis neutralizes the effect of cognate toxin HigB1. Neutralization of HigB1 toxin in E.coli or M.marinum also requires SecB-like chaperone Rv1957, making this the first toxin-antitoxin chaperone (TAC) system. Antitoxin aggregation and degradation are prevented by the chaperone. | Possible toxin HigB; Toxic component of an atypical, type II toxin-antitoxin chaperone (TAC) system. Upon expression in M.smegmatis inhibits colony formation and cell growth. Ectopic expression in wild-type M.tuberculosis has no effect on cell growth; ectopic expression in a triple higB1-higA1-Rv1957 (delta TAC) disruption mutant causes growth arrest, killing a considerable proportion of the cells. Increased ectopic expression leads to decreased levels of IdeR- and Zur-regulated genes as well as cleavage within the mRNA region of tmRNA (transfer-mRNA), strongly suggesting it is an endo [...] | 0.993 |
higA | higB2 | Rv1956 | Rv2022c | Possible antitoxin HigA; Antitoxin component of an atypical, type II toxin-antitoxin chaperone (TAC) system. Upon expression in M.smegmatis neutralizes the effect of cognate toxin HigB1. Neutralization of HigB1 toxin in E.coli or M.marinum also requires SecB-like chaperone Rv1957, making this the first toxin-antitoxin chaperone (TAC) system. Antitoxin aggregation and degradation are prevented by the chaperone. | Conserved protein; Putative toxic component of a type II toxin-antitoxin (TA) system. Its cognate antitoxin would be HigA2. Belongs to the mycobacterial HigB family. | 0.784 |
higA | higB3 | Rv1956 | Rv3182 | Possible antitoxin HigA; Antitoxin component of an atypical, type II toxin-antitoxin chaperone (TAC) system. Upon expression in M.smegmatis neutralizes the effect of cognate toxin HigB1. Neutralization of HigB1 toxin in E.coli or M.marinum also requires SecB-like chaperone Rv1957, making this the first toxin-antitoxin chaperone (TAC) system. Antitoxin aggregation and degradation are prevented by the chaperone. | Conserved hypothetical protein; Putative toxic component of a type II toxin-antitoxin (TA) system. Its cognate antitoxin would be HigA3. Not toxic upon expression in M.smegmatis. | 0.568 |
higA | relE | Rv1956 | Rv1246c | Possible antitoxin HigA; Antitoxin component of an atypical, type II toxin-antitoxin chaperone (TAC) system. Upon expression in M.smegmatis neutralizes the effect of cognate toxin HigB1. Neutralization of HigB1 toxin in E.coli or M.marinum also requires SecB-like chaperone Rv1957, making this the first toxin-antitoxin chaperone (TAC) system. Antitoxin aggregation and degradation are prevented by the chaperone. | Toxin RelE; Toxic component of a type II toxin-antitoxin (TA) system. Has RNase activity (By similarity). Overexpression in M.tuberculosis or M.smegmatis inhibits colony formation in a bacteriostatic rather than bacteriocidal fashion. Its toxic effect is neutralized by coexpression with cognate antitoxin RelB (shown only for M.smegmatis). | 0.587 |
higA | secBL | Rv1956 | Rv1957 | Possible antitoxin HigA; Antitoxin component of an atypical, type II toxin-antitoxin chaperone (TAC) system. Upon expression in M.smegmatis neutralizes the effect of cognate toxin HigB1. Neutralization of HigB1 toxin in E.coli or M.marinum also requires SecB-like chaperone Rv1957, making this the first toxin-antitoxin chaperone (TAC) system. Antitoxin aggregation and degradation are prevented by the chaperone. | Hypothetical protein; Chaperone component of an atypical, type II toxin-antitoxin chaperone (TAC) system. Prevents antitoxin HigA1 aggregation in vitro at a 1:3 chaperone:antitoxin ratio, probably also protects antitoxin HigA1 from protease. Required for neutralization of toxin HigB1 upon ectopic expression in Mycobacterium marinum or E.coli. When expressed in E.coli complements a secB deletion, restores export of OmpA and MBP and inhibits aggregation of proOmpC although it is less efficient than endogenous SecB. Complements the general chaperone function of E.coli SecB less well; Belo [...] | 0.999 |
higA2 | higA | Rv2021c | Rv1956 | Transcriptional regulatory protein; Putative antitoxin component of a type II toxin-antitoxin (TA) system. Its cognate toxin would be HigB2. | Possible antitoxin HigA; Antitoxin component of an atypical, type II toxin-antitoxin chaperone (TAC) system. Upon expression in M.smegmatis neutralizes the effect of cognate toxin HigB1. Neutralization of HigB1 toxin in E.coli or M.marinum also requires SecB-like chaperone Rv1957, making this the first toxin-antitoxin chaperone (TAC) system. Antitoxin aggregation and degradation are prevented by the chaperone. | 0.839 |
higA2 | higB | Rv2021c | Rv1955 | Transcriptional regulatory protein; Putative antitoxin component of a type II toxin-antitoxin (TA) system. Its cognate toxin would be HigB2. | Possible toxin HigB; Toxic component of an atypical, type II toxin-antitoxin chaperone (TAC) system. Upon expression in M.smegmatis inhibits colony formation and cell growth. Ectopic expression in wild-type M.tuberculosis has no effect on cell growth; ectopic expression in a triple higB1-higA1-Rv1957 (delta TAC) disruption mutant causes growth arrest, killing a considerable proportion of the cells. Increased ectopic expression leads to decreased levels of IdeR- and Zur-regulated genes as well as cleavage within the mRNA region of tmRNA (transfer-mRNA), strongly suggesting it is an endo [...] | 0.684 |
higA2 | higB2 | Rv2021c | Rv2022c | Transcriptional regulatory protein; Putative antitoxin component of a type II toxin-antitoxin (TA) system. Its cognate toxin would be HigB2. | Conserved protein; Putative toxic component of a type II toxin-antitoxin (TA) system. Its cognate antitoxin would be HigA2. Belongs to the mycobacterial HigB family. | 0.998 |
higA2 | higB3 | Rv2021c | Rv3182 | Transcriptional regulatory protein; Putative antitoxin component of a type II toxin-antitoxin (TA) system. Its cognate toxin would be HigB2. | Conserved hypothetical protein; Putative toxic component of a type II toxin-antitoxin (TA) system. Its cognate antitoxin would be HigA3. Not toxic upon expression in M.smegmatis. | 0.954 |
higA2 | relE | Rv2021c | Rv1246c | Transcriptional regulatory protein; Putative antitoxin component of a type II toxin-antitoxin (TA) system. Its cognate toxin would be HigB2. | Toxin RelE; Toxic component of a type II toxin-antitoxin (TA) system. Has RNase activity (By similarity). Overexpression in M.tuberculosis or M.smegmatis inhibits colony formation in a bacteriostatic rather than bacteriocidal fashion. Its toxic effect is neutralized by coexpression with cognate antitoxin RelB (shown only for M.smegmatis). | 0.474 |
higA2 | relK | Rv2021c | Rv3358 | Transcriptional regulatory protein; Putative antitoxin component of a type II toxin-antitoxin (TA) system. Its cognate toxin would be HigB2. | Toxin RelK; Toxic component of a type II toxin-antitoxin (TA) system. Has RNase activity and preferentially cleaves at the 3'-end of purine ribonucleotides (By similarity). Overexpression in M.tuberculosis or M.smegmatis inhibits colony formation in a bacteriostatic rather than bacteriocidal fashion. Its toxic effect is neutralized by coexpression with antitoxin RelJ (shown only for M.smegmatis). Overexpression also increases the number of rifampcin-tolerant persister cells. Belongs to the YoeB family. | 0.540 |
higA2 | secBL | Rv2021c | Rv1957 | Transcriptional regulatory protein; Putative antitoxin component of a type II toxin-antitoxin (TA) system. Its cognate toxin would be HigB2. | Hypothetical protein; Chaperone component of an atypical, type II toxin-antitoxin chaperone (TAC) system. Prevents antitoxin HigA1 aggregation in vitro at a 1:3 chaperone:antitoxin ratio, probably also protects antitoxin HigA1 from protease. Required for neutralization of toxin HigB1 upon ectopic expression in Mycobacterium marinum or E.coli. When expressed in E.coli complements a secB deletion, restores export of OmpA and MBP and inhibits aggregation of proOmpC although it is less efficient than endogenous SecB. Complements the general chaperone function of E.coli SecB less well; Belo [...] | 0.536 |
higB | Rv1954A | Rv1955 | Rv1954A | Possible toxin HigB; Toxic component of an atypical, type II toxin-antitoxin chaperone (TAC) system. Upon expression in M.smegmatis inhibits colony formation and cell growth. Ectopic expression in wild-type M.tuberculosis has no effect on cell growth; ectopic expression in a triple higB1-higA1-Rv1957 (delta TAC) disruption mutant causes growth arrest, killing a considerable proportion of the cells. Increased ectopic expression leads to decreased levels of IdeR- and Zur-regulated genes as well as cleavage within the mRNA region of tmRNA (transfer-mRNA), strongly suggesting it is an endo [...] | Rv1954A, len: 100 aa. Hypothetical unknown protein. | 0.618 |
higB | higA | Rv1955 | Rv1956 | Possible toxin HigB; Toxic component of an atypical, type II toxin-antitoxin chaperone (TAC) system. Upon expression in M.smegmatis inhibits colony formation and cell growth. Ectopic expression in wild-type M.tuberculosis has no effect on cell growth; ectopic expression in a triple higB1-higA1-Rv1957 (delta TAC) disruption mutant causes growth arrest, killing a considerable proportion of the cells. Increased ectopic expression leads to decreased levels of IdeR- and Zur-regulated genes as well as cleavage within the mRNA region of tmRNA (transfer-mRNA), strongly suggesting it is an endo [...] | Possible antitoxin HigA; Antitoxin component of an atypical, type II toxin-antitoxin chaperone (TAC) system. Upon expression in M.smegmatis neutralizes the effect of cognate toxin HigB1. Neutralization of HigB1 toxin in E.coli or M.marinum also requires SecB-like chaperone Rv1957, making this the first toxin-antitoxin chaperone (TAC) system. Antitoxin aggregation and degradation are prevented by the chaperone. | 0.993 |
higB | higA2 | Rv1955 | Rv2021c | Possible toxin HigB; Toxic component of an atypical, type II toxin-antitoxin chaperone (TAC) system. Upon expression in M.smegmatis inhibits colony formation and cell growth. Ectopic expression in wild-type M.tuberculosis has no effect on cell growth; ectopic expression in a triple higB1-higA1-Rv1957 (delta TAC) disruption mutant causes growth arrest, killing a considerable proportion of the cells. Increased ectopic expression leads to decreased levels of IdeR- and Zur-regulated genes as well as cleavage within the mRNA region of tmRNA (transfer-mRNA), strongly suggesting it is an endo [...] | Transcriptional regulatory protein; Putative antitoxin component of a type II toxin-antitoxin (TA) system. Its cognate toxin would be HigB2. | 0.684 |