groEL2 molecular chaperone GroEL [Mycobacterium tuberculosis H37Rv] - Gene

Summary

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Gene symbol: groEL2
Gene description: molecular chaperone GroEL
Locus tag: Rv0440
Gene type: protein coding
RefSeq status: PROVISIONAL
Organism: Mycobacterium tuberculosis H37Rv (strain: H37Rv, type-material: type strain of Mycobacterium tuberculosis)
Lineage: Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae; Mycobacterium; Mycobacterium tuberculosis complex
Also known as: groEL-2; groL2; hsp60; hsp65
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Genomic context

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Sequence:: NC_000962.3 (528608..530230)

NC_000962.3 Genomic Context describing neighboring genes

Genomic regions, transcripts, and products

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Genomic Sequence:: NC_000962.3

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Bibliography

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GeneRIFs: Gene References Into Functions

What's a GeneRIF?

Interaction mechanism of Mycobacterium tuberculosis GroEL2 protein with macrophage Lectin-like, oxidized low-density lipoprotein receptor-1: An integrated computational and experimental study.
Title: Interaction mechanism of Mycobacterium tuberculosis GroEL2 protein with macrophage Lectin-like, oxidized low-density lipoprotein receptor-1: An integrated computational and experimental study.
Here the authors present data showing that GroEL2, a substrate of Hip1, modulates dendritic cell functions. The full-length GroEL2 protein elicited robust proinflammatory responses from dendritic cells and promoted their maturation and antigen presentation to T cells. In contrast, the cleaved form of GroEL2, which predominates in Mycobacterium tuberculosis, was poorly immunostimulatory.
Title: Mycobacterium tuberculosis GroEL2 Modulates Dendritic Cell Responses.
hsp65 Nested PCR-PRA was shown to be a fast and reliable assay for diagnosing tuberculosis
Title: Evaluation of hsp65 nested PCR-restriction analysis (PRA) for diagnosing tuberculosis in a high burden country.
Data suggest that cleavage of HSP65 by matrix metalloproteinases, including MMP-9, to create immunogenic peptides contributes to complex immunomodulatory interplay in course of TB infection. [HSP65]
Title: Matrix metalloproteinase proteolysis of the mycobacterial HSP65 protein as a potential source of immunogenic peptides in human tuberculosis.
Findings reveal a unique role of the Mycobacterium tuberculosis heat shock protein 60 favouring development of Th2 type response by upregulating surface expression of TLR2 on macrophages which could be a survival strategy adopted by the bacilli.
Title: Mycobacterium tuberculosis heat shock protein 60 modulates immune response to PPD by manipulating the surface expression of TLR2 on macrophages.
GroELs play a role in the protein folding process of HspR.
Title: Modulation of DNA-binding activity of Mycobacterium tuberculosis HspR by chaperones.
HSP65 and HSP70 from Mycobacterium tuberculosis signal via TLR4
Title: Mycobacterium tuberculosis heat shock proteins use diverse Toll-like receptor pathways to activate pro-inflammatory signals.

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General gene information

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Homology

Orthologs from OrthoDB

General protein information

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Preferred Names: molecular chaperone GroEL

NP_214954.1

60 kDa chaperonin 2 GroEL2 (protein CPN60-2) (GroEL protein 2) (65 kDa antigen) (heat shock protein 65) (cell wall protein A) (antigen A). Purified 65 kDa antigen can elicit a strong delayed-type hypersensitivity reaction in experimental animals infected with M. tuberculosis. This protein is one of the major immunoreactive proteins of the mycobacteria. This antigen contains epitopes that are common to various species of mycobacteria.

NCBI Reference Sequences (RefSeq)

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Genome Annotation

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Reference assembly

Genomic

NC_000962.3 Reference assembly

Range

528608..530230

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GenBank, FASTA, Sequence Viewer (Graphics)

mRNA and Protein(s)

NP_214954.1 molecular chaperone GroEL [Mycobacterium tuberculosis H37Rv]

See identical proteins and their annotated locations for NP_214954.1

Status: PROVISIONAL

UniProtKB/TrEMBL

R4LUN2

Conserved Domains (1) summary

PRK00013
Location:1 → 530

groEL; chaperonin GroEL; Reviewed