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There are several matches for 'Rv1957'.
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organism
protein
1)
Mycobacterium tuberculosis H37Rv
secBL - 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 [...]
[a.k.a.
Rv1957
, CCP44725.1, RVBD_1957]
2)
Mycobacterium tuberculosis H37Rv
higB - 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 [...]
[a.k.a. Rv1955, CCP44723.1, RVBD_1955]
3)
Mycobacterium tuberculosis H37Rv
higA - 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.
[a.k.a. Rv1956, CCP44724.1, mtv:RVBD_1956]
4)
Mycolicibacterium smegmatis
secBL - Hypothetical protein; Chaperone component of an orphan antitoxin chaperone (AC) system; there is no toxin gene in close genomic proximity. When expressed in E.coli complements the cold-sensitive phenotype of a secB deletion, suggesting it may have a generic chaperone function. Does not however complement the toxin-neutralizing effect of its M.tuberculosis paralog
Rv1957
(AC P95257) in E.coli, probably because the antitoxin genes are not from the same family.
[a.k.a. MSMEG_2143, ABK76162.1, NZ_SIJM01000021.1]