groEL1
- Type
- protein_coding
- Name
- groEL1
- Locus Name
-
Rv3417c
- Product
-
60 kDa chaperonin 1 GroEL1 (protein CPN60-1) (GroEL protein 1)
- Functional Category
-
Virulence, detoxification, adaptation
- Location
- 3835272..3836891 (- strand)
- Gene Length
- 1619 bp
- Nucleotides
-
ATGAGCAAGCTGATCGAATACGACGAAACCGCGCGTCGCGCCATGGAGGTCGGCATGGACAAGCTGGCCGACACCGTGCGGGTGACGCTGGGGCCGCGCGGCCGGCATGTGGTGCTGGCCAAGGCGTTTGGCGGACCCACGGTTACCAACGACGGCGTCACGGTGGCACGTGAGATCGAGCTGGAAGATCCGTTTGAAGACTTGGGCGCCCAGCTGGTGAAGTCGGTGGCCACCAAGACCAACGATGTGGCCGGTGACGGCACCACCACCGCAACCATCTTGGCGCAGGCACTGATCAAGGGCGGCCTGAGGCTAGTGGCCGCCGGCGTCAACCCGATCGCGCTCGGCGTGGGAATCGGCAAGGCCGCCGACGCGGTATCCGAGGCGCTGCTGGCATCGGCCACGCCGGTGTCCGGCAAGACCGGCATCGCGCAGGTGGCGACGGTGTCCTCGCGCGACGAGCAGATCGGTGACCTGGTTGGCGAAGCGATGAGCAAGGTCGGCCACGACGGCGTGGTCAGCGTCGAAGAATCCTCGACGCTGGGCACCGAGTTGGAGTTCACCGAGGGTATCGGCTTCGACAAGGGCTTCTTGTCGGCATACTTCGTTACCGACTTCGATAACCAGCAGGCGGTGCTCGAGGACGCGTTGATCCTGCTGCACCAAGACAAGATCAGCTCGCTTCCCGATCTGTTGCCATTGCTGGAAAAGGTTGCAGGAACGGGTAAGCCACTACTGATCGTGGCTGAAGACGTGGAGGGCGAAGCGTTGGCGACGCTGGTCGTCAACGCGATTCGCAAGACGTTGAAAGCGGTCGCGGTCAAGGGGCCGTACTTCGGTGACCGCCGTAAGGCGTTCCTTGAGGACCTGGCGGTGGTGACGGGTGGCCAGGTGGTCAACCCCGACGCCGGCATGGTGCTGCGCGAGGTGGGCTTGGAGGTGCTGGGCTCGGCCCGACGCGTGGTGGTCAGCAAGGACGACACGGTCATTGTCGACGGCGGCGGCACCGCAGAAGCGGTGGCCAACCGGGCGAAGCACTTGCGTGCCGAGATCGACAAGAGCGATTCGGATTGGGATCGGGAAAAGCTTGGCGAGCGGCTGGCCAAACTGGCCGGCGGGGTTGCTGTCATCAAGGTGGGTGCCGCCACCGAGACCGCACTCAAGGAGCGCAAGGAAAGCGTCGAGGATGCGGTCGCGGCCGCCAAGGCCGCGGTCGAGGAGGGCATCGTCCCTGGTGGGGGAGCCTCGCTCATCCACCAGGCCCGCAAGGCGCTGACCGAACTGCGTGCGTCGCTGACCGGTGACGAGGTCCTCGGTGTCGACGTGTTCTCCGAAGCCCTTGCCGCGCCGTTGTTCTGGATCGCCGCCAACGCTGGCTTGGACGGCTCGGTGGTGGTCAACAAGGTCAGCGAGCTACCCGCCGGGCATGGGCTGAACGTGAACACCCTGAGCTATGGTGACTTGGCCGCTGACGGCGTCATCGACCCGGTCAAGGTGACTAGGTCGGCGGTGTTGAACGCGTCATCGGTTGCCCGGATGGTACTCACCACCGAGACGGTCGTGGTCGACAAGCCGGCCAAGGCAGAAGATCACGACCATCACCACGGGCACGCGCACTG
- Drug Resistance
- Mutations
- Function
- Prevents aggregation of substrate proteins and promotes their refolding (PubMed:15327959). Functions in the absence of co-chaperone CH10 and ATP. {ECO:0000269|PubMed:15327959, ECO:0000305|PubMed:21094166}.; FUNCTION: May mediate association of bacteria with macrophages; recombinant protein competitively inhibits the association of M.tuberculosis with mouse bone marrow-derived macrophages (PubMed:19470749). {ECO:0000269|PubMed:19470749}.
- Family
-
Chaperonin (HSP60) family
- GO
-
- cell surface GO:0009986 cellular_component
- response to heat GO:0009408 biological_process
- positive regulation of transcription regulatory region DNA binding GO:2000679 biological_process
- DNA protection GO:0042262 biological_process
- protein refolding GO:0042026 biological_process
- cell wall GO:0005618 cellular_component
- ATP binding GO:0005524 molecular_function
- single-stranded DNA binding GO:0003697 molecular_function
- GroEL-GroES complex GO:1990220 cellular_component
- plasma membrane GO:0005886 cellular_component
- 'de novo' protein folding GO:0006458 biological_process
- nucleoid organization GO:0090143 biological_process
- unfolded protein binding GO:0051082 molecular_function
- bacterial nucleoid GO:0043590 cellular_component
- InterPro
3M6C
- Name
- 60 kDa chaperonin 1 (GroEL protein 1) (Protein Cpn60-1)
- Family
- Chaperonin (HSP60) family
- Protein Sequence
-
MSKLIEYDETARRAMEVGMDKLADTVRVTLGPRGRHVVLAKAFGGPTVTNDGVTVAREIELEDPFEDLGAQLVKSVATKTNDVAGDGTTTATILAQALIKGGLRLVAAGVNPIALGVGIGKAADAVSEALLASATPVSGKTGIAQVATVSSRDEQIGDLVGEAMSKVGHDGVVSVEESSTLGTELEFTEGIGFDKGFLSAYFVTDFDNQQAVLEDALILLHQDKISSLPDLLPLLEKVAGTGKPLLIVAEDVEGEALATLVVNAIRKTLKAVAVKGPYFGDRRKAFLEDLAVVTGGQVVNPDAGMVLREVGLEVLGSARRVVVSKDDTVIVDGGGTAEAVANRAKHLRAEIDKSDSDWDREKLGERLAKLAGGVAVIKVGAATETALKERKESVEDAVAAAKAAVEEGIVPGGGASLIHQARKALTELRASLTGDEVLGVDVFSEALAAPLFWIAANAGLDGSVVVNKVSELPAGHGLNVNTLSYGDLAADGVIDPVKVTRSAVLNASSVARMVLTTETVVVDKPAKAEDHDHHHGHAH
- Mass
- 55,877 Da
- Length
- 539 Aa
Summary
Rv3417c doesn't seem to be a targeted by any drug.
-
-
Tuberculosis mtu05152
mtu05152Human Diseases; Infectious disease: bacterial
-
-
-
RNA degradation mtu03018
mtu03018Genetic Information Processing; Folding, sorting and degradation
-
- Biochemical evidence for relaxed substrate specificity of Nalpha-acetyltransferase (Rv3420c/rimI) of Mycobacterium tuberculosis.
- Sci Rep. 2016 Jun 29;6:28892. doi: 10.1038/srep28892.
- Structural and functional conservation of Mycobacterium tuberculosis GroEL paralogs suggests that GroEL1 Is a chaperonin.
- J Mol Biol. 2011 Jan 21;405(3):831-9. doi: 10.1016/j.jmb.2010.11.021. Epub 2010 Nov 19.
- Proteogenomic analysis of Mycobacterium tuberculosis by high resolution mass spectrometry.
- Mol Cell Proteomics. 2011 Dec;10(12):M111.011627. doi: 10.1074/mcp.M111.011445. Epub 2011 Oct 3.
- Facilitated oligomerization of mycobacterial GroEL: evidence for phosphorylation-mediated oligomerization.
- J Bacteriol. 2009 Nov;191(21):6525-38. doi: 10.1128/JB.00652-09. Epub 2009 Aug 28.
- Mycobacterium tuberculosis Cpn60.2 and DnaK are located on the bacterial surface, where Cpn60.2 facilitates efficient bacterial association with macrophages.
- Infect Immun. 2009 Aug;77(8):3389-401. doi: 10.1128/IAI.00143-09. Epub 2009 May 26.
- The Mycobacterium tuberculosis GroEL1 chaperone is a substrate of Ser/Thr protein kinases.
- J Bacteriol. 2009 Apr;191(8):2876-83. doi: 10.1128/JB.01569-08. Epub 2009 Feb 6.
- A Mycobacterium tuberculosis mutant lacking the groEL homologue cpn60.1 is viable but fails to induce an inflammatory response in animal models of infection.
- Infect Immun. 2008 Apr;76(4):1535-46. doi: 10.1128/IAI.01078-07. Epub 2008 Jan 28.
- Mycobacterium tuberculosis GroEL homologues unusually exist as lower oligomers and retain the ability to suppress aggregation of substrate proteins.
- J Mol Biol. 2004 Sep 10;342(2):605-17. doi: 10.1016/j.jmb.2004.07.066.
- Deciphering the biology of Mycobacterium tuberculosis from the complete genome sequence.
- Nature. 1998 Jun 11;393(6685):537-44. doi: 10.1038/31159.
- Mycobacterium tuberculosis expresses two chaperonin-60 homologs.
- Proc Natl Acad Sci U S A. 1993 Apr 1;90(7):2608-12. doi: 10.1073/pnas.90.7.2608.