IED ID |
IndEnz0002001950 |
Enzyme Type ID |
protease001950 |
Protein Name |
SecB-like chaperone Rv1957
|
Gene Name |
secBL Rv1957 |
Organism |
Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv) |
Taxonomic Lineage |
cellular organisms
Bacteria
Terrabacteria group
Actinobacteria
Actinomycetia (high G+C Gram-positive bacteria)
Corynebacteriales
Mycobacteriaceae
Mycobacterium
Mycobacterium tuberculosis complex
Mycobacterium tuberculosis
Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
|
Enzyme Sequence |
MTDRTDADDLDLQRVGARLAARAQIRDIRLLRTQAAVHRAPKPAQGLTYDLEFEPAVDADPATISAFVVRISCHLRIQNQAADDDVKEGDTKDETQDVATADFEFAALFDYHLQEGEDDPTEEELTAYAATTGRFALYPYIREYVYDLTGRLALPPLTLEILSRPMPVSPGAQWPATRGTP |
Enzyme Length |
181 |
Uniprot Accession Number |
P95257 |
Absorption |
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Active Site |
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Activity Regulation |
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Binding Site |
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Calcium Binding |
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catalytic Activity |
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DNA Binding |
|
EC Number |
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Enzyme Function |
FUNCTION: 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. {ECO:0000269|PubMed:21536872}. |
Temperature Dependency |
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PH Dependency |
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Pathway |
|
nucleotide Binding |
|
Features |
Beta strand (4); Chain (1); Helix (2); Initiator methionine (1); Modified residue (1); Turn (2) |
Keywords |
3D-structure;Acetylation;Chaperone;Reference proteome |
Interact With |
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Induction |
INDUCTION: Probably induced by the DNA damaging agent mitomycin C. Part of the Rv1954A-higB1-higA1-Rv1957 operon, as well as the higB1-higA1-Rv1957 operon, which is probably the mitomycin-induced operon; the former but not latter operon is autorepressed by HigA1 (PubMed:20585061). {ECO:0000269|PubMed:19118359, ECO:0000269|PubMed:20585061}. |
Subcellular Location |
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Modified Residue |
MOD_RES 2; /note=N-acetylthreonine; /evidence=ECO:0007744|PubMed:21969609 |
Post Translational Modification |
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Signal Peptide |
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Structure 3D |
X-ray crystallography (1) |
Cross Reference PDB |
5MTW;
|
Mapped Pubmed ID |
27827369;
30770830;
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Motif |
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Gene Encoded By |
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Mass |
20,106 |
Kinetics |
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Metal Binding |
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Rhea ID |
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Cross Reference Brenda |
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