Detail Information for IndEnz0002001950
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
Active Site
Activity Regulation
Binding Site
Calcium Binding
catalytic Activity
DNA Binding
EC Number
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
PH Dependency
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
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
Modified Residue MOD_RES 2; /note=N-acetylthreonine; /evidence=ECO:0007744|PubMed:21969609
Post Translational Modification
Signal Peptide
Structure 3D X-ray crystallography (1)
Cross Reference PDB 5MTW;
Mapped Pubmed ID 27827369; 30770830;
Motif
Gene Encoded By
Mass 20,106
Kinetics
Metal Binding
Rhea ID
Cross Reference Brenda