Methionine aminopeptidase 2 - Mycobacterium tuberculosis

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P0A5J2 (AMPM2_MYCTU) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 52. History...

Clusters with 100%, 90%, 50% identity |

Documents (3) |

Third-party data

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Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents Customize order

Names and origin

Protein names

Recommended name:
Methionine aminopeptidase 2
Short name=MAP
EC=3.4.11.18

Alternative name(s):
Peptidase M

Gene names

Name:	map
Synonyms:	mapB
Ordered Locus Names:	Rv2861c, MT2929
ORF Names:	MTV003.07c

Organism

Mycobacterium tuberculosis

Taxonomic identifier

1773 [NCBI]

Taxonomic lineage

Bacteria › Actinobacteria › Actinobacteridae › Actinomycetales › Corynebacterineae › Mycobacteriaceae › Mycobacterium › Mycobacterium tuberculosis complex

Protein attributes

Sequence length	285 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Removes the N-terminal methionine from nascent proteins, when the penultimate amino acid is alanine or proline, but enzyme activity is remarkably low when the second residue is phenylalanine or leucine. With glycine at the second position, Map is more active with a tetrapeptide than with a tripeptide. Ref.3 Ref.5
Catalytic activity	Release of N-terminal amino acids, preferentially methionine, from peptides and arylamides.
Cofactor	Binds 2 divalent cations per subunit. The enzyme is active with manganese, magnesium, iron and nickel ions. Ref.3 Ref.5 Ref.6
Enzyme regulation	Inhibited by bengamide derivatives and by various metalloform-selective inhibitors. Ref.5 Ref.6
Sequence similarities	Belongs to the peptidase M24A family.
Biophysicochemical properties	Kinetic parameters: K_M=58 µM for Met-Gly-Met-Met (at pH 7.5 and at 37 degrees Celsius) Ref.3 Ref.5 K_M=394 µM for Met-Ala-Ser (at pH 7.5 and at 37 degrees Celsius) K_M=141 µM for nickel ions K_M=192 µM for manganese ions K_M=349 µM for cobalt ions K_M=349 µM for iron ions Temperature dependence: Optimum temperature is 37 degrees Celsius. It lost all its activities at 55 degrees Celsius.
Mass spectrometry	Molecular mass is 32516 Da from positions 1 - 285. Determined by MALDI. Ref.3

Ontologies

Keywords
Ligand	Cobalt Metal-binding
Molecular function	Aminopeptidase Hydrolase Protease
Technical term	3D-structure Complete proteome Reference proteome
Gene Ontology (GO)
Biological process	methionine metabolic process Inferred from direct assay Ref.5. Source: MTBBASE protein initiator methionine removal involved in protein maturation Inferred from direct assay Ref.5. Source: MTBBASE proteolysis Inferred from electronic annotation. Source: UniProtKB-KW
Molecular function	cobalt ion binding Inferred from direct assay Ref.5. Source: MTBBASE iron ion binding Inferred from direct assay Ref.5. Source: MTBBASE manganese ion binding Inferred from direct assay Ref.5. Source: MTBBASE metalloaminopeptidase activity Inferred from direct assay Ref.3 Ref.5. Source: MTBBASE nickel cation binding Inferred from direct assay Ref.5. Source: MTBBASE
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 285

285

Methionine aminopeptidase 2

PRO_0000148948

Regions

Region

131 – 133

Substrate binding

Region

203 – 205

Substrate binding

Sites

Metal binding

131

Divalent cations 1

Metal binding

142

Divalent cations 1

Metal binding

142

Divalent cations 2

Metal binding

205

Divalent cations 2

Metal binding

238

Divalent cations 2

Metal binding

269

Divalent cations 1

Metal binding

269

Divalent cations 2

Binding site

114

Substrate

Binding site

142

Substrate

Binding site

212

Substrate

Binding site

238

Substrate

Binding site

269

Substrate

Secondary structure

285

Helix Strand Turn

Details...

Sequences

Sequence

Length

Mass (Da)

Tools

P0A5J2 [UniParc].

Last modified March 15, 2005. Version 1.
Checksum: E69831250E6C6130
Show »

FASTA

285

30,891

        10         20         30         40         50         60 
MPSRTALSPG VLSPTRPVPN WIARPEYVGK PAAQEGSEPW VQTPEVIEKM RVAGRIAAGA 

        70         80         90        100        110        120 
LAEAGKAVAP GVTTDELDRI AHEYLVDNGA YPSTLGYKGF PKSCCTSLNE VICHGIPDST 

       130        140        150        160        170        180 
VITDGDIVNI DVTAYIGGVH GDTNATFPAG DVADEHRLLV DRTREATMRA INTVKPGRAL 

       190        200        210        220        230        240 
SVIGRVIESY ANRFGYNVVR DFTGHGIGTT FHNGLVVLHY DQPAVETIMQ PGMTFTIEPM 

       250        260        270        280 
INLGALDYEI WDDGWTVVTK DRKWTAQFEH TLLVTDTGVE ILTCL

« Hide

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Deciphering the biology of Mycobacterium tuberculosis from the complete genome sequence." Cole S.T., Brosch R., Parkhill J., Garnier T., Churcher C.M., Harris D.E., Gordon S.V., Eiglmeier K., Gas S., Barry C.E. III, Tekaia F., Badcock K., Basham D., Brown D., Chillingworth T., Connor R., Davies R.M., Devlin K. Barrell B.G. Nature 393:537-544(1998) [PubMed: 9634230] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 25618 / H37Rv.
[2]	"Whole-genome comparison of Mycobacterium tuberculosis clinical and laboratory strains." Fleischmann R.D., Alland D., Eisen J.A., Carpenter L., White O., Peterson J.D., DeBoy R.T., Dodson R.J., Gwinn M.L., Haft D.H., Hickey E.K., Kolonay J.F., Nelson W.C., Umayam L.A., Ermolaeva M.D., Salzberg S.L., Delcher A., Utterback T.R. Fraser C.M. J. Bacteriol. 184:5479-5490(2002) [PubMed: 12218036] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: CDC 1551 / Oshkosh.
[3]	"Expression and characterization of two functional methionine aminopeptidases from Mycobacterium tuberculosis H37Rv." Zhang X., Chen S., Hu Z., Zhang L., Wang H. Curr. Microbiol. 59:520-525(2009) [PubMed: 19688379] [Abstract] Cited for: FUNCTION AS A METHIONINE AMINOPEPTIDASE, SUBSTRATES SPECIFICITY, BIOPHYSICOCHEMICAL PROPERTIES, COFACTOR, MASS SPECTROMETRY.
[4]	"Identification of an SH3-binding motif in a new class of methionine aminopeptidases from Mycobacterium tuberculosis suggests a mode of interaction with the ribosome." Addlagatta A., Quillin M.L., Omotoso O., Liu J.O., Matthews B.W. Biochemistry 44:7166-7174(2005) [PubMed: 15882055] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (1.51 ANGSTROMS) IN COMPLEXES WITH COBALT IONS AND METHIONINE.
[5]	"Catalysis and inhibition of Mycobacterium tuberculosis methionine aminopeptidase." Lu J.P., Chai S.C., Ye Q.Z. J. Med. Chem. 53:1329-1337(2010) [PubMed: 20038112] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (1.4 ANGSTROMS) IN COMPLEX WITH ANALOGS SUBSTRATE AND DIVALENT CATIONS, FUNCTION AS A METHIONINE AMINOPEPTIDASE, BIOPHYSICOCHEMICAL PROPERTIES, ENZYME REGULATION, COFACTOR.
[6]	"Inhibition of Mycobacterium tuberculosis methionine aminopeptidases by bengamide derivatives." Lu J.P., Yuan X.H., Yuan H., Wang W.L., Wan B., Franzblau S.G., Ye Q.Z. ChemMedChem 6:1041-1048(2011) [PubMed: 21465667] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (1.25 ANGSTROMS) IN COMPLEX WITH ANALOGS SUBSTRATE AND MANGANESE IONS, COFACTOR, ENZYME REGULATION.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

BX842581 Genomic DNA. Translation: CAE55527.1.
AE000516 Genomic DNA. Translation: AAK47254.1.

PIR

G70885.

RefSeq

NP_337440.1. NC_002755.2.
YP_177911.1. NC_000962.2.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1Y1N	X-ray	1.51	A	1-285	[»]
1YJ3	X-ray	1.60	A	1-285	[»]
3IU7	X-ray	1.40	A	1-285	[»]
3IU8	X-ray	1.85	A	1-285	[»]
3IU9	X-ray	1.75	A	1-285	[»]
3PKA	X-ray	1.25	A	1-285	[»]
3PKB	X-ray	1.25	A	1-285	[»]
3PKC	X-ray	1.47	A	1-285	[»]
3PKD	X-ray	1.47	A	1-285	[»]
3PKE	X-ray	1.60	A	1-285	[»]

ProteinModelPortal

P0A5J2.

SMR

P0A5J2. Positions 4-285.

ModBase

Search...

Protein family/group databases

MEROPS

M24.001.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

EnsemblBacteria

EBMYCT00000000789; EBMYCP00000000789; EBMYCG00000000789.
EBMYCT00000070136; EBMYCP00000068195; EBMYCG00000070131.

GeneID

888596.
925347.

GenomeReviews

Gene locus MT2929 in contig AE000516_GR.
Gene locus Rv2861c in contig AL123456_GR.

KEGG

mtc:MT2929.
mtu:Rv2861c.

PATRIC

18128212. VBIMycTub22151_3205.

TIGR

MT2929.

Organism-specific databases

TubercuList

Rv2861c.

Phylogenomic databases

GeneTree

EBGT00050000016752.

HOGENOM

HBG299384.

OMA

IEPMISE.

PhylomeDB

P0A5J2.

ProtClustDB

PRK12896.

Family and domain databases

InterPro

IPR001714. Pept_M24_MAP.
IPR000994. Pept_M24_structural-domain.
IPR002467. Pept_M24A_MAP1.
[Graphical view]

Gene3D

G3DSA:3.90.230.10. Peptidase_M24_cat_core. 1 hit.

K01265.

Pfam

PF00557. Peptidase_M24. 1 hit.
[Graphical view]

PRINTS

PR00599. MAPEPTIDASE.

SUPFAM

SSF55920. Peptidase_M24_cat_core. 1 hit.

TIGRFAMs

TIGR00500. Met_pdase_I. 1 hit.

PROSITE

PS00680. MAP_1. 1 hit.
[Graphical view]

ProtoNet

Search...

Entry information

Entry name

AMPM2_MYCTU

Accession

Primary (citable) accession number: P0A5J2
Secondary accession number(s): O33343

Entry history

Integrated into UniProtKB/Swiss-Prot:	March 15, 2005
Last sequence update:	March 15, 2005
Last modified:	January 25, 2012
This is version 52 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program

Relevant documents

Peptidase families

Classification of peptidase families and list of entries

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families

Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents

Preferred order of sections

Names and origin

Protein attributes

General annotation (Comments)

Ontologies

Sequence annotation (Features)

Molecule processing

Regions

Sites

Secondary structure

Sequences

References

Cross-references

Sequence databases

3D structure databases

Protein family/group databases

Protocols and materials databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Family and domain databases

Entry information

Relevant documents