UniProtKB - P9WK19 (MAP12_MYCTU)
Protein
Methionine aminopeptidase 2
Gene
map
Organism
Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Status
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.UniRule annotation2 Publications
Catalytic activityi
- Release of N-terminal amino acids, preferentially methionine, from peptides and arylamides.UniRule annotation EC:3.4.11.18
Cofactori
Co2+UniRule annotation2 Publications, Zn2+UniRule annotation, Mn2+UniRule annotation2 Publications, Fe2+UniRule annotation1 PublicationNote: 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.UniRule annotation1 Publication
Activity regulationi
Inhibited by bengamide derivatives and by various metalloform-selective inhibitors.2 Publications
Kineticsi
- KM=58 µM for Met-Gly-Met-Met (at pH 7.5 and at 37 degrees Celsius)2 Publications
- KM=394 µM for Met-Ala-Ser (at pH 7.5 and at 37 degrees Celsius)2 Publications
Temperature dependencei
Optimum temperature is 37 degrees Celsius. It lost all its activities at 55 degrees Celsius.2 Publications
Sites
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Binding sitei | 114 | SubstrateUniRule annotation3 Publications | 1 | |
Metal bindingi | 131 | Divalent metal cation 1UniRule annotation3 Publications | 1 | |
Metal bindingi | 142 | Divalent metal cation 1UniRule annotation3 Publications | 1 | |
Metal bindingi | 142 | Divalent metal cation 2; catalyticUniRule annotation3 Publications | 1 | |
Metal bindingi | 205 | Divalent metal cation 2; catalytic; via tele nitrogenUniRule annotation3 Publications | 1 | |
Binding sitei | 212 | SubstrateUniRule annotation3 Publications | 1 | |
Metal bindingi | 238 | Divalent metal cation 2; catalyticUniRule annotation3 Publications | 1 | |
Metal bindingi | 269 | Divalent metal cation 1UniRule annotation3 Publications | 1 | |
Metal bindingi | 269 | Divalent metal cation 2; catalyticUniRule annotation3 Publications | 1 |
GO - Molecular functioni
- cobalt ion binding Source: MTBBASE
- iron ion binding Source: MTBBASE
- manganese ion binding Source: MTBBASE
- metalloaminopeptidase activity Source: MTBBASE
- nickel cation binding Source: MTBBASE
GO - Biological processi
- methionine metabolic process Source: MTBBASE
- protein initiator methionine removal involved in protein maturation Source: MTBBASE
Keywordsi
Molecular function | Aminopeptidase, Hydrolase, Protease |
Ligand | Metal-binding |
Enzyme and pathway databases
BioCyci | MTBH37RV:G185E-7112-MONOMER |
Names & Taxonomyi
Protein namesi | Recommended name: Methionine aminopeptidase 2UniRule annotation (EC:3.4.11.18UniRule annotation)Short name: MAP 2UniRule annotation Short name: MetAP 2UniRule annotation Alternative name(s): Peptidase MUniRule annotation |
Gene namesi | Name:mapUniRule annotation Synonyms:mapB Ordered Locus Names:Rv2861c ORF Names:MTV003.07c |
Organismi | Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv) |
Taxonomic identifieri | 83332 [NCBI] |
Taxonomic lineagei | Bacteria › Actinobacteria › Corynebacteriales › Mycobacteriaceae › Mycobacterium › Mycobacterium tuberculosis complex › |
Proteomesi |
|
Organism-specific databases
TubercuListi | Rv2861c |
PTM / Processingi
Molecule processing
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
ChainiPRO_0000148948 | 1 – 285 | Methionine aminopeptidase 2Add BLAST | 285 |
Proteomic databases
PaxDbi | P9WK19 |
Interactioni
Subunit structurei
Monomer.
UniRule annotationProtein-protein interaction databases
STRINGi | 83332.Rv2861c |
Structurei
Secondary structure
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details3D structure databases
SMRi | P9WK19 |
ModBasei | Search... |
PDBe-KBi | Search... |
Family & Domainsi
Sequence similaritiesi
Phylogenomic databases
eggNOGi | ENOG4105CA1 Bacteria COG0024 LUCA |
KOi | K01265 |
OMAi | GDHAYTF |
PhylomeDBi | P9WK19 |
Family and domain databases
CDDi | cd01086 MetAP1, 1 hit |
Gene3Di | 3.90.230.10, 1 hit |
HAMAPi | MF_01974 MetAP_1, 1 hit |
InterProi | View protein in InterPro IPR036005 Creatinase/aminopeptidase-like IPR000994 Pept_M24 IPR001714 Pept_M24_MAP IPR002467 Pept_M24A_MAP1 |
Pfami | View protein in Pfam PF00557 Peptidase_M24, 1 hit |
PRINTSi | PR00599 MAPEPTIDASE |
SUPFAMi | SSF55920 SSF55920, 1 hit |
TIGRFAMsi | TIGR00500 met_pdase_I, 1 hit |
PROSITEi | View protein in PROSITE PS00680 MAP_1, 1 hit |
i Sequence
Sequence statusi: Complete.
P9WK19-1 [UniParc]FASTAAdd to basket
10 20 30 40 50
MPSRTALSPG VLSPTRPVPN WIARPEYVGK PAAQEGSEPW VQTPEVIEKM
60 70 80 90 100
RVAGRIAAGA LAEAGKAVAP GVTTDELDRI AHEYLVDNGA YPSTLGYKGF
110 120 130 140 150
PKSCCTSLNE VICHGIPDST VITDGDIVNI DVTAYIGGVH GDTNATFPAG
160 170 180 190 200
DVADEHRLLV DRTREATMRA INTVKPGRAL SVIGRVIESY ANRFGYNVVR
210 220 230 240 250
DFTGHGIGTT FHNGLVVLHY DQPAVETIMQ PGMTFTIEPM INLGALDYEI
260 270 280
WDDGWTVVTK DRKWTAQFEH TLLVTDTGVE ILTCL
Mass spectrometryi
Sequence databases
Select the link destinations: EMBLi GenBanki DDBJi Links Updated | AL123456 Genomic DNA Translation: CCP45662.1 |
PIRi | G70885 |
RefSeqi | WP_003899513.1, NZ_NVQJ01000006.1 YP_177911.1, NC_000962.3 |
Genome annotation databases
EnsemblBacteriai | CCP45662; CCP45662; Rv2861c |
GeneIDi | 888596 |
KEGGi | mtu:Rv2861c mtv:RVBD_2861c |
Similar proteinsi
Cross-referencesi
Sequence databases
Select the link destinations: EMBLi GenBanki DDBJi Links Updated | AL123456 Genomic DNA Translation: CCP45662.1 |
PIRi | G70885 |
RefSeqi | WP_003899513.1, NZ_NVQJ01000006.1 YP_177911.1, NC_000962.3 |
3D structure databases
Select the link destinations: PDBei RCSB PDBi PDBji Links Updated | PDB 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 | [»] | |
4OOK | X-ray | 1.90 | A | 1-283 | [»] | |
SMRi | P9WK19 | |||||
ModBasei | Search... | |||||
PDBe-KBi | Search... |
Protein-protein interaction databases
STRINGi | 83332.Rv2861c |
Chemistry databases
DrugBanki | DB02909 5-(2-Chlorophenyl)Furan-2-Carboxylic Acid |
Proteomic databases
PaxDbi | P9WK19 |
Genome annotation databases
EnsemblBacteriai | CCP45662; CCP45662; Rv2861c |
GeneIDi | 888596 |
KEGGi | mtu:Rv2861c mtv:RVBD_2861c |
Organism-specific databases
TubercuListi | Rv2861c |
Phylogenomic databases
eggNOGi | ENOG4105CA1 Bacteria COG0024 LUCA |
KOi | K01265 |
OMAi | GDHAYTF |
PhylomeDBi | P9WK19 |
Enzyme and pathway databases
BioCyci | MTBH37RV:G185E-7112-MONOMER |
Miscellaneous databases
PROi | PR:P9WK19 |
Family and domain databases
CDDi | cd01086 MetAP1, 1 hit |
Gene3Di | 3.90.230.10, 1 hit |
HAMAPi | MF_01974 MetAP_1, 1 hit |
InterProi | View protein in InterPro IPR036005 Creatinase/aminopeptidase-like IPR000994 Pept_M24 IPR001714 Pept_M24_MAP IPR002467 Pept_M24A_MAP1 |
Pfami | View protein in Pfam PF00557 Peptidase_M24, 1 hit |
PRINTSi | PR00599 MAPEPTIDASE |
SUPFAMi | SSF55920 SSF55920, 1 hit |
TIGRFAMsi | TIGR00500 met_pdase_I, 1 hit |
PROSITEi | View protein in PROSITE PS00680 MAP_1, 1 hit |
ProtoNeti | Search... |
MobiDBi | Search... |
Entry informationi
Entry namei | MAP12_MYCTU | |
Accessioni | P9WK19Primary (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: | November 13, 2019 | |
This is version 33 of the entry and version 1 of the sequence. See complete history. | ||
Entry statusi | Reviewed (UniProtKB/Swiss-Prot) | |
Annotation program | Prokaryotic Protein Annotation Program |
Miscellaneousi
Keywords - Technical termi
3D-structure, Complete proteome, Reference proteomeDocuments
- Peptidase families
Classification of peptidase families and list of entries - SIMILARITY comments
Index of protein domains and families - Mycobacterium tuberculosis strains ATCC 25618 / H37Rv and CDC 1551 / Oshkosh
Mycobacterium tuberculosis strains ATCC 25618 / H37Rv and CDC 1551 / Oshkosh: entries and gene names - PDB cross-references
Index of Protein Data Bank (PDB) cross-references