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P9WK19

- MAP12_MYCTU

UniProt

P9WK19 - MAP12_MYCTU

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Protein
Methionine aminopeptidase 2
Gene
map, mapB, Rv2861c, MTV003.07c
Organism
Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

Functioni

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.2 Publications

Catalytic activityi

Release of N-terminal amino acids, preferentially methionine, from peptides and arylamides.UniRule annotation

Cofactori

Binds 2 divalent metal cations per subunit. Has a high-affinity and a low affinity metal-binding site. The true nature of the physiological cofactor is under debate. The enzyme is active with cobalt, zinc, manganese or divalent iron ions. Most likely, methionine aminopeptidases function as mononuclear Fe2+-metalloproteases under physiological conditions, and the catalytically relevant metal-binding site has been assigned to the histidine-containing high-affinity site By similarity.3 Publications

Enzyme regulationi

Inhibited by bengamide derivatives and by various metalloform-selective inhibitors.2 Publications

Kineticsi

  1. KM=58 µM for Met-Gly-Met-Met (at pH 7.5 and at 37 degrees Celsius)2 Publications
  2. KM=394 µM for Met-Ala-Ser (at pH 7.5 and at 37 degrees Celsius)

Temperature dependencei

Optimum temperature is 37 degrees Celsius. It lost all its activities at 55 degrees Celsius.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei114 – 1141Substrate
Metal bindingi131 – 1311Divalent metal cation 1
Metal bindingi142 – 1421Divalent metal cation 1
Metal bindingi142 – 1421Divalent metal cation 2; catalytic
Metal bindingi205 – 2051Divalent metal cation 2; catalytic; via tele nitrogen
Binding sitei212 – 2121Substrate
Metal bindingi238 – 2381Divalent metal cation 2; catalytic
Metal bindingi269 – 2691Divalent metal cation 1
Metal bindingi269 – 2691Divalent metal cation 2; catalytic

GO - Molecular functioni

  1. metal ion binding Source: UniProtKB-HAMAP
  2. metalloaminopeptidase activity Source: UniProtKB-HAMAP
Complete GO annotation...

GO - Biological processi

  1. protein initiator methionine removal Source: UniProtKB-HAMAP
Complete GO annotation...

Keywords - Molecular functioni

Aminopeptidase, Hydrolase, Protease

Keywords - Ligandi

Metal-binding

Names & Taxonomyi

Protein namesi
Recommended name:
Methionine aminopeptidase 2 (EC:3.4.11.18)
Short name:
MAP 2
Short name:
MetAP 2
Alternative name(s):
Peptidase M
Gene namesi
Name:map
Synonyms:mapB
Ordered Locus Names:Rv2861c
ORF Names:MTV003.07c
OrganismiMycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Taxonomic identifieri83332 [NCBI]
Taxonomic lineageiBacteriaActinobacteriaActinobacteridaeActinomycetalesCorynebacterineaeMycobacteriaceaeMycobacteriumMycobacterium tuberculosis complex
ProteomesiUP000001584: Chromosome

Organism-specific databases

TubercuListiRv2861c.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 285285Methionine aminopeptidase 2UniRule annotation
PRO_0000148948Add
BLAST

Interactioni

Subunit structurei

Monomer By similarity.UniRule annotation

Structurei

Secondary structure

Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Turni26 – 294
Beta strandi30 – 323
Beta strandi36 – 383
Helixi44 – 6623
Helixi74 – 8714
Turni93 – 964
Helixi97 – 993
Beta strandi102 – 1087
Beta strandi111 – 1133
Beta strandi127 – 13610
Beta strandi139 – 14810
Helixi154 – 17219
Helixi182 – 19211
Turni193 – 1953
Beta strandi200 – 2023
Beta strandi204 – 2063
Beta strandi208 – 2125
Beta strandi233 – 2375
Beta strandi240 – 2445
Beta strandi248 – 2503
Beta strandi257 – 2593
Beta strandi265 – 2673
Beta strandi269 – 2746
Beta strandi276 – 2838

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1Y1NX-ray1.51A1-285[»]
1YJ3X-ray1.60A1-285[»]
3IU7X-ray1.40A1-285[»]
3IU8X-ray1.85A1-285[»]
3IU9X-ray1.75A1-285[»]
3PKAX-ray1.25A1-285[»]
3PKBX-ray1.25A1-285[»]
3PKCX-ray1.47A1-285[»]
3PKDX-ray1.47A1-285[»]
3PKEX-ray1.60A1-285[»]
3RORX-ray2.00A1-285[»]
4IDYX-ray2.00A1-285[»]
4IECX-ray2.00A1-285[»]
4IF7X-ray2.00A1-285[»]
ProteinModelPortaliP9WK19.

Family & Domainsi

Sequence similaritiesi

Phylogenomic databases

KOiK01265.
PhylomeDBiP9WK19.

Family and domain databases

Gene3Di3.90.230.10. 1 hit.
HAMAPiMF_01974. MetAP_1.
InterProiIPR001714. Pept_M24_MAP.
IPR000994. Pept_M24_structural-domain.
IPR002467. Pept_M24A_MAP1.
[Graphical view]
PfamiPF00557. Peptidase_M24. 1 hit.
[Graphical view]
PRINTSiPR00599. MAPEPTIDASE.
SUPFAMiSSF55920. SSF55920. 1 hit.
TIGRFAMsiTIGR00500. met_pdase_I. 1 hit.
PROSITEiPS00680. MAP_1. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P9WK19-1 [UniParc]FASTAAdd to Basket

« Hide

MPSRTALSPG VLSPTRPVPN WIARPEYVGK PAAQEGSEPW VQTPEVIEKM    50
RVAGRIAAGA LAEAGKAVAP GVTTDELDRI AHEYLVDNGA YPSTLGYKGF 100
PKSCCTSLNE VICHGIPDST VITDGDIVNI DVTAYIGGVH GDTNATFPAG 150
DVADEHRLLV DRTREATMRA INTVKPGRAL SVIGRVIESY ANRFGYNVVR 200
DFTGHGIGTT FHNGLVVLHY DQPAVETIMQ PGMTFTIEPM INLGALDYEI 250
WDDGWTVVTK DRKWTAQFEH TLLVTDTGVE ILTCL 285
Length:285
Mass (Da):30,891
Last modified:April 16, 2014 - v1
Checksum:iE69831250E6C6130
GO

Mass spectrometryi

Molecular mass is 32516 Da from positions 1 - 285. Determined by MALDI. 1 Publication

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AL123456 Genomic DNA. Translation: CCP45662.1.
PIRiG70885.
RefSeqiYP_006516313.1. NC_018143.2.
YP_177911.1. NC_000962.3.

Genome annotation databases

GeneIDi13317652.
888596.
KEGGimtu:Rv2861c.
mtv:RVBD_2861c.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AL123456 Genomic DNA. Translation: CCP45662.1 .
PIRi G70885.
RefSeqi YP_006516313.1. NC_018143.2.
YP_177911.1. NC_000962.3.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
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 [» ]
3ROR X-ray 2.00 A 1-285 [» ]
4IDY X-ray 2.00 A 1-285 [» ]
4IEC X-ray 2.00 A 1-285 [» ]
4IF7 X-ray 2.00 A 1-285 [» ]
ProteinModelPortali P9WK19.
ModBasei Search...

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

GeneIDi 13317652.
888596.
KEGGi mtu:Rv2861c.
mtv:RVBD_2861c.

Organism-specific databases

TubercuListi Rv2861c.

Phylogenomic databases

KOi K01265.
PhylomeDBi P9WK19.

Family and domain databases

Gene3Di 3.90.230.10. 1 hit.
HAMAPi MF_01974. MetAP_1.
InterProi IPR001714. Pept_M24_MAP.
IPR000994. Pept_M24_structural-domain.
IPR002467. Pept_M24A_MAP1.
[Graphical view ]
Pfami PF00557. Peptidase_M24. 1 hit.
[Graphical view ]
PRINTSi PR00599. MAPEPTIDASE.
SUPFAMi SSF55920. SSF55920. 1 hit.
TIGRFAMsi TIGR00500. met_pdase_I. 1 hit.
PROSITEi PS00680. MAP_1. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: ATCC 25618 / H37Rv.
  2. "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] [Europe PMC] [Abstract]
    Cited for: FUNCTION AS A METHIONINE AMINOPEPTIDASE, SUBSTRATE SPECIFICITY, BIOPHYSICOCHEMICAL PROPERTIES, COFACTOR, MASS SPECTROMETRY.
  3. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Strain: ATCC 25618 / H37Rv.
  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] [Europe PMC] [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] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.4 ANGSTROMS) IN COMPLEX WITH SUBSTRATE ANALOGS 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] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.25 ANGSTROMS) IN COMPLEX WITH SUBSTRATE ANALOGS AND MANGANESE IONS, COFACTOR, ENZYME REGULATION.

Entry informationi

Entry nameiMAP12_MYCTU
AccessioniPrimary (citable) accession number: P9WK19
Secondary accession number(s): L0TDS5, O33343, P0A5J2
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 16, 2014
Last sequence update: April 16, 2014
Last modified: September 3, 2014
This is version 5 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. Mycobacterium tuberculosis strains ATCC 25618 / H37Rv and CDC 1551 / Oshkosh
    Mycobacterium tuberculosis strains ATCC 25618 / H37Rv and CDC 1551 / Oshkosh: entries and gene names
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. Peptidase families
    Classification of peptidase families and list of entries
  4. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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