Methionine aminopeptidase 2
Details
- Name
- Methionine aminopeptidase 2
- Synonyms
- 3.4.11.18
- MAP 2
- mapB
- Peptidase M
- Gene Name
- map
- Organism
- Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
- Amino acid sequence
>lcl|BSEQ0051235|Methionine aminopeptidase 2 MPSRTALSPGVLSPTRPVPNWIARPEYVGKPAAQEGSEPWVQTPEVIEKMRVAGRIAAGA LAEAGKAVAPGVTTDELDRIAHEYLVDNGAYPSTLGYKGFPKSCCTSLNEVICHGIPDST VITDGDIVNIDVTAYIGGVHGDTNATFPAGDVADEHRLLVDRTREATMRAINTVKPGRAL SVIGRVIESYANRFGYNVVRDFTGHGIGTTFHNGLVVLHYDQPAVETIMQPGMTFTIEPM INLGALDYEIWDDGWTVVTKDRKWTAQFEHTLLVTDTGVEILTCL
- Number of residues
- 285
- Molecular Weight
- 30890.78
- Theoretical pI
- Not Available
- GO Classification
- Functionscobalt ion binding / iron ion binding / manganese ion binding / metalloaminopeptidase activity / nickel cation bindingProcessesmethionine metabolic process / protein initiator methionine removal involved in protein maturation
- General Function
- Removes the N-terminal methionine from nascent proteins. The N-terminal methionine is often cleaved when the second residue in the primary sequence is small and uncharged (Met-Ala-, Cys, Gly, Pro, Ser, Thr, or Val). Requires deformylation of the N(alpha)-formylated initiator methionine before it can be hydrolyzed.
- Specific Function
- Cobalt ion binding
- Pfam Domain Function
- Peptidase_M24 (PF00557)
- Transmembrane Regions
- Not Available
- Cellular Location
- Not Available
- Gene sequence
>lcl|BSEQ0051236|Methionine aminopeptidase 2 (map) ATGCCTAGTCGTACCGCGCTCTCCCCCGGCGTGCTGTCCCCGACACGGCCGGTGCCCAAC TGGATCGCGCGCCCCGAATACGTCGGCAAACCGGCCGCCCAAGAGGGCAGCGAGCCGTGG GTGCAGACACCTGAGGTCATCGAGAAGATGCGCGTGGCAGGCCGGATCGCCGCAGGTGCG TTGGCCGAGGCGGGCAAGGCGGTCGCGCCCGGGGTAACCACCGACGAACTCGACCGGATC GCGCACGAATACCTGGTCGACAACGGCGCCTACCCATCAACGCTGGGCTACAAGGGATTC CCGAAGTCGTGCTGCACGTCCCTCAACGAGGTCATCTGCCATGGAATCCCCGACTCGACG GTGATCACCGACGGCGACATCGTCAACATCGACGTCACCGCCTACATCGGTGGGGTGCAC GGTGACACCAACGCGACGTTTCCGGCCGGCGATGTCGCAGACGAACACCGGTTGCTCGTT GACCGGACCCGCGAAGCGACCATGCGTGCGATCAACACCGTCAAGCCCGGGCGGGCGTTG TCCGTTATCGGTCGTGTCATCGAGTCGTATGCAAATCGGTTCGGGTACAACGTGGTTCGA GACTTCACTGGTCATGGCATCGGCACGACGTTCCACAACGGGCTGGTCGTCTTGCACTAC GACCAGCCCGCTGTCGAGACCATCATGCAGCCGGGGATGACCTTCACCATCGAGCCGATG ATCAACTTGGGCGCACTGGACTACGAAATCTGGGACGACGGTTGGACGGTGGTCACCAAG GACCGCAAGTGGACCGCACAGTTCGAACACACCCTGCTGGTTACCGATACCGGCGTCGAG ATCCTGACCTGTCTGTAG
- Chromosome Location
- Not Available
- Locus
- Not Available
- External Identifiers
Resource Link UniProtKB ID P9WK19 UniProtKB Entry Name MAP12_MYCTU - 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]
- Zhang X, Chen S, Hu Z, Zhang L, Wang H: Expression and characterization of two functional methionine aminopeptidases from Mycobacterium tuberculosis H37Rv. Curr Microbiol. 2009 Nov;59(5):520-5. doi: 10.1007/s00284-009-9470-3. Epub 2009 Aug 18. [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]
- Addlagatta A, Quillin ML, Omotoso O, Liu JO, Matthews BW: Identification of an SH3-binding motif in a new class of methionine aminopeptidases from Mycobacterium tuberculosis suggests a mode of interaction with the ribosome. Biochemistry. 2005 May 17;44(19):7166-74. [Article]
- Lu JP, Chai SC, Ye QZ: Catalysis and inhibition of Mycobacterium tuberculosis methionine aminopeptidase. J Med Chem. 2010 Feb 11;53(3):1329-37. doi: 10.1021/jm901624n. [Article]
- Lu JP, Yuan XH, Yuan H, Wang WL, Wan B, Franzblau SG, Ye QZ: Inhibition of Mycobacterium tuberculosis methionine aminopeptidases by bengamide derivatives. ChemMedChem. 2011 Jun 6;6(6):1041-8. doi: 10.1002/cmdc.201100003. Epub 2011 Apr 4. [Article]