Proteasome subunit beta
Details
- Name
- Proteasome subunit beta
- Kind
- protein
- Synonyms
- 20S proteasome beta subunit
- 3.4.25.1
- Proteasome core protein PrcB
- Gene Name
- prcB
- UniProtKB Entry
- P9WHT9Swiss-Prot
- Organism
- Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
- NCBI Taxonomy ID
- 83332
- Amino acid sequence
>lcl|BSEQ0051259|Proteasome subunit beta MTWPLPDRLSINSLSGTPAVDLSSFTDFLRRQAPELLPASISGGAPLAGGDAQLPHGTTI VALKYPGGVVMAGDRRSTQGNMISGRDVRKVYITDDYTATGIAGTAAVAVEFARLYAVEL EHYEKLEGVPLTFAGKINRLAIMVRGNLAAAMQGLLALPLLAGYDIHASDPQSAGRIVSF DAAGGWNIEEEGYQAVGSGSLFAKSSMKKLYSQVTDGDSGLRVAVEALYDAADDDSATGG PDLVRGIFPTAVIIDADGAVDVPESRIAELARAIIESRSGADTFGSDGGEK
- Number of residues
- 291
- Molecular Weight
- 30304.72
- Theoretical pI
- Not Available
- GO Classification
- Functionsthreonine-type endopeptidase activity / zymogen bindingProcessesgrowth / modification-dependent protein catabolic process / pathogenesis / proteasomal protein catabolic process / proteolysis involved in cellular protein catabolic processComponentscytoplasm / extracellular region / plasma membrane / proteasome core complex, beta-subunit complex
- General Function
- Component of the proteasome core, a large protease complex with broad specificity involved in protein degradation. The M.tuberculosis proteasome is able to cleave oligopeptides not only after hydrophobic but also after basic, acidic and small neutral residues (PubMed:16468985). In complex with the ATPase Mpa, degrades protein targets conjugated to a prokaryotic ubiquitin-like protein (Pup). Among the identified substrates of the M.tuberculosis proteasome are the pupylated FabD, PanB and Mpa proteins (PubMed:17082771). One function of the proteasome is to contribute to M.tuberculosis ability to resist killing by host macrophages, since the core proteasome is essential for persistence of the pathogen during the chronic phase of infection in mice (PubMed:18059281). Likely functions to recycle amino acids under nutrient starvation, thereby enabling the cell to maintain basal metabolic activities (By similarity) (PubMed:20711362). The mechanism of protection against bactericidal chemistries of the host's immune response probably involves the degradation of proteins that are irreversibly oxidized, nitrated, or nitrosated. A proteolysis-independent activity of the proteasome core is required for optimal growth of M.tuberculosis in mouse lungs and for RNI resistance; in contrast, long-term survival of M.tuberculosis in stationary phase and during starvation in vitro and in the chronic phase of mouse infection required a proteolytically active proteasome (PubMed:20711362).
- Specific Function
- threonine-type endopeptidase activity
- Pfam Domain Function
- Proteasome (PF00227)
- Signal Regions
- Not Available
- Transmembrane Regions
- Not Available
- Cellular Location
- Cytoplasm
- Gene sequence
>lcl|BSEQ0051260|Proteasome subunit beta (prcB) GTGACCTGGCCGTTGCCCGATCGCCTGTCCATTAATTCACTCTCTGGAACACCCGCTGTA GACCTATCTTCTTTCACTGACTTCCTGCGCCGCCAGGCGCCGGAGTTGCTGCCGGCAAGC ATCAGCGGCGGTGCGCCACTCGCAGGCGGCGATGCGCAACTGCCGCACGGCACCACCATT GTCGCGCTGAAATACCCCGGCGGTGTTGTCATGGCGGGTGACCGGCGTTCGACGCAGGGC AACATGATTTCTGGGCGTGATGTGCGCAAGGTGTATATCACCGATGACTACACCGCTACC GGCATCGCTGGCACGGCTGCGGTCGCGGTTGAGTTTGCCCGGCTGTATGCCGTGGAACTT GAGCACTACGAGAAGCTCGAGGGTGTGCCGCTGACGTTTGCCGGCAAAATCAACCGGCTG GCGATTATGGTGCGTGGCAATCTGGCGGCCGCGATGCAGGGTCTGCTGGCGTTGCCGTTG CTGGCGGGCTACGACATTCATGCGTCTGACCCGCAGAGCGCGGGTCGTATCGTTTCGTTC GACGCCGCCGGCGGTTGGAACATCGAGGAAGAGGGCTATCAGGCGGTGGGCTCGGGTTCG CTGTTCGCGAAGTCGTCGATGAAGAAGTTGTATTCGCAGGTTACCGACGGTGATTCGGGG CTGCGGGTGGCGGTCGAGGCGCTCTACGACGCCGCCGACGACGACTCCGCCACCGGCGGT CCGGACCTGGTGCGGGGCATCTTTCCGACGGCGGTGATCATCGACGCCGACGGGGCGGTT GACGTGCCGGAGAGCCGGATTGCCGAATTGGCCCGCGCGATCATCGAAAGCCGTTCGGGT GCGGATACTTTCGGCTCCGATGGCGGTGAGAAGTGA
- Chromosome Location
- Not Available
- Locus
- Not Available
- External Identifiers
Resource Link UniProtKB ID P9WHT9 UniProtKB Entry Name PSB_MYCTU PDB ID(s) 2FHG, 2FHH, 2JAY, 3H6F, 3H6I, 3HF9, 3HFA, 3KRD, 3MFE, 3MI0, 3MKA, 5LZP, 5THO, 5TRG, 5TRR, 5TRS, 5TRY, 5TS0 KEGG ID mtu:Rv2110c NCBI Gene ID 887508 - General References
- Cole ST, Brosch R, Parkhill J, Garnier T, Churcher C, Harris D, Gordon SV, Eiglmeier K, Gas S, Barry CE 3rd, Tekaia F, Badcock K, Basham D, Brown D, Chillingworth T, Connor R, Davies R, Devlin K, Feltwell T, Gentles S, Hamlin N, Holroyd S, Hornsby T, Jagels K, Krogh A, McLean J, Moule S, Murphy L, Oliver K, Osborne J, Quail MA, Rajandream MA, Rogers J, Rutter S, Seeger K, Skelton J, Squares R, Squares S, Sulston JE, Taylor K, Whitehead S, Barrell BG: Deciphering the biology of Mycobacterium tuberculosis from the complete genome sequence. Nature. 1998 Jun 11;393(6685):537-44. [Article]
- Lin G, Hu G, Tsu C, Kunes YZ, Li H, Dick L, Parsons T, Li P, Chen Z, Zwickl P, Weich N, Nathan C: Mycobacterium tuberculosis prcBA genes encode a gated proteasome with broad oligopeptide specificity. Mol Microbiol. 2006 Mar;59(5):1405-16. [Article]
- Pearce MJ, Arora P, Festa RA, Butler-Wu SM, Gokhale RS, Darwin KH: Identification of substrates of the Mycobacterium tuberculosis proteasome. EMBO J. 2006 Nov 15;25(22):5423-32. Epub 2006 Nov 2. [Article]
- Gandotra S, Schnappinger D, Monteleone M, Hillen W, Ehrt S: In vivo gene silencing identifies the Mycobacterium tuberculosis proteasome as essential for the bacteria to persist in mice. Nat Med. 2007 Dec;13(12):1515-20. Epub 2007 Dec 2. [Article]
- Kelkar DS, Kumar D, Kumar P, Balakrishnan L, Muthusamy B, Yadav AK, Shrivastava P, Marimuthu A, Anand S, Sundaram H, Kingsbury R, Harsha HC, Nair B, Prasad TS, Chauhan DS, Katoch K, Katoch VM, Kumar P, Chaerkady R, Ramachandran S, Dash D, Pandey A: 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. [Article]
- Poulsen C, Holton S, Geerlof A, Wilmanns M, Song YH: Stoichiometric protein complex formation and over-expression using the prokaryotic native operon structure. FEBS Lett. 2010 Feb 19;584(4):669-74. doi: 10.1016/j.febslet.2009.12.057. Epub 2010 Jan 18. [Article]
- Gandotra S, Lebron MB, Ehrt S: The Mycobacterium tuberculosis proteasome active site threonine is essential for persistence yet dispensable for replication and resistance to nitric oxide. PLoS Pathog. 2010 Aug 12;6(8):e1001040. doi: 10.1371/journal.ppat.1001040. [Article]
- Anandan T, Han J, Baun H, Nyayapathy S, Brown JT, Dial RL, Moltalvo JA, Kim MS, Yang SH, Ronning DR, Husson RN, Suh J, Kang CM: Phosphorylation regulates mycobacterial proteasome. J Microbiol. 2014 Sep;52(9):743-54. doi: 10.1007/s12275-014-4416-2. Epub 2014 Sep 2. [Article]
- Hu G, Lin G, Wang M, Dick L, Xu RM, Nathan C, Li H: Structure of the Mycobacterium tuberculosis proteasome and mechanism of inhibition by a peptidyl boronate. Mol Microbiol. 2006 Mar;59(5):1417-28. [Article]
- Lin G, Li D, de Carvalho LP, Deng H, Tao H, Vogt G, Wu K, Schneider J, Chidawanyika T, Warren JD, Li H, Nathan C: Inhibitors selective for mycobacterial versus human proteasomes. Nature. 2009 Oct 1;461(7264):621-6. doi: 10.1038/nature08357. Epub 2009 Sep 16. [Article]
- Lin G, Li D, Chidawanyika T, Nathan C, Li H: Fellutamide B is a potent inhibitor of the Mycobacterium tuberculosis proteasome. Arch Biochem Biophys. 2010 Sep 15;501(2):214-20. doi: 10.1016/j.abb.2010.06.009. Epub 2010 Jun 15. [Article]
- Li D, Li H, Wang T, Pan H, Lin G, Li H: Structural basis for the assembly and gate closure mechanisms of the Mycobacterium tuberculosis 20S proteasome. EMBO J. 2010 Jun 16;29(12):2037-47. doi: 10.1038/emboj.2010.95. Epub 2010 May 11. [Article]
Associated Data
- Drug Relations
Drug Drug group Pharmacological action? Type Actions Details N-(4-MORPHOLINE)CARBONYL-B-(1-NAPHTHYL)-L-ALANINE-L-LEUCINE BORONIC ACID experimental unknown target Details