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UniProtKB - O34484 (MAP12_BACSU)
Protein
Methionine aminopeptidase 2
Gene
mapB
Organism
Bacillus subtilis (strain 168)
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 annotation1 PublicationCatalytic activityi
- Release of N-terminal amino acids, preferentially methionine, from peptides and arylamides.UniRule annotation EC:3.4.11.18
Cofactori
Co2+UniRule annotation, Zn2+UniRule annotation, Mn2+UniRule annotation, Fe2+UniRule annotationNote: 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 annotation
Sites
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Binding sitei | 76 | SubstrateUniRule annotation | 1 | |
Metal bindingi | 94 | Divalent metal cation 1UniRule annotation | 1 | |
Metal bindingi | 105 | Divalent metal cation 1UniRule annotation | 1 | |
Metal bindingi | 105 | Divalent metal cation 2; catalyticUniRule annotation | 1 | |
Metal bindingi | 168 | Divalent metal cation 2; catalytic; via tele nitrogenUniRule annotation | 1 | |
Binding sitei | 175 | SubstrateUniRule annotation | 1 | |
Metal bindingi | 202 | Divalent metal cation 2; catalyticUniRule annotation | 1 | |
Metal bindingi | 233 | Divalent metal cation 1UniRule annotation | 1 | |
Metal bindingi | 233 | Divalent metal cation 2; catalyticUniRule annotation | 1 |
GO - Molecular functioni
- metal ion binding Source: UniProtKB-UniRule
- metalloaminopeptidase activity Source: UniProtKB-UniRule
GO - Biological processi
- protein initiator methionine removal Source: UniProtKB-UniRule
Keywordsi
Molecular function | Aminopeptidase, Hydrolase, Protease |
Ligand | Metal-binding |
Enzyme and pathway databases
BioCyci | BSUB:BSU07690-MONOMER |
Protein family/group databases
MEROPSi | M24.036 |
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 |
Gene namesi | Name:mapBUniRule annotation Synonyms:yflG Ordered Locus Names:BSU07690 |
Organismi | Bacillus subtilis (strain 168) |
Taxonomic identifieri | 224308 [NCBI] |
Taxonomic lineagei | Bacteria › Firmicutes › Bacilli › Bacillales › Bacillaceae › Bacillus › |
Proteomesi |
|
Subcellular locationi
Cytoplasm and Cytosol
- Cytoplasm 1 Publication
Other locations
- cytoplasm Source: UniProtKB-SubCell
Keywords - Cellular componenti
CytoplasmPTM / Processingi
Molecule processing
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
ChainiPRO_0000361275 | 1 – 249 | Methionine aminopeptidase 2Add BLAST | 249 |
Proteomic databases
PaxDbi | O34484 |
PRIDEi | O34484 |
Expressioni
Inductioni
Expressed at very low levels throughout growth.1 Publication
Interactioni
Subunit structurei
Monomer.
UniRule annotationProtein-protein interaction databases
STRINGi | 224308.BSU07690 |
Family & Domainsi
Sequence similaritiesi
Phylogenomic databases
eggNOGi | COG0024, Bacteria |
InParanoidi | O34484 |
OMAi | HWEHSVA |
PhylomeDBi | O34484 |
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 |
i Sequence
Sequence statusi: Complete.
O34484-1 [UniParc]FASTAAdd to basket
10 20 30 40 50
MIVTNDQELE GLKKIGRIVA LAREEMKRKA EPGMSTKDLD LIGKAVLDEH
60 70 80 90 100
GAVSAPEKEY DFPGVTCISV NDEVAHGIPS TSKILKAGDL VNIDISAEFG
110 120 130 140 150
GFYSDTGISF VLGEGEERLH KLCQCAENAF QKGLQQAKAG KRQNQIGRAV
160 170 180 190 200
YHEARSQGFT VIKTLTGHGI GRSLHEAPNH IMNYYDPFDN ALFKNGTVIA
210 220 230 240
LEPFISTKAE TIVEAGDGWT FKTPDKSMVA QVEHTIVITK DEPIILTKL
Mass spectrometryi
Molecular mass is 27209.35±2.14 Da. 1 Publication
Sequence databases
Select the link destinations: EMBLi GenBanki DDBJi Links Updated | D86417 Genomic DNA Translation: BAA22300.1 AL009126 Genomic DNA Translation: CAB12598.1 |
PIRi | E69810 |
RefSeqi | NP_388650.1, NC_000964.3 WP_003233698.1, NZ_JNCM01000032.1 |
Genome annotation databases
EnsemblBacteriai | CAB12598; CAB12598; BSU_07690 |
GeneIDi | 936121 |
KEGGi | bsu:BSU07690 |
PATRICi | fig|224308.179.peg.835 |
Similar proteinsi
Cross-referencesi
Sequence databases
Select the link destinations: EMBLi GenBanki DDBJi Links Updated | D86417 Genomic DNA Translation: BAA22300.1 AL009126 Genomic DNA Translation: CAB12598.1 |
PIRi | E69810 |
RefSeqi | NP_388650.1, NC_000964.3 WP_003233698.1, NZ_JNCM01000032.1 |
3D structure databases
AlphaFoldDBi | O34484 |
SMRi | O34484 |
ModBasei | Search... |
Protein-protein interaction databases
STRINGi | 224308.BSU07690 |
Protein family/group databases
MEROPSi | M24.036 |
Proteomic databases
PaxDbi | O34484 |
PRIDEi | O34484 |
Genome annotation databases
EnsemblBacteriai | CAB12598; CAB12598; BSU_07690 |
GeneIDi | 936121 |
KEGGi | bsu:BSU07690 |
PATRICi | fig|224308.179.peg.835 |
Phylogenomic databases
eggNOGi | COG0024, Bacteria |
InParanoidi | O34484 |
OMAi | HWEHSVA |
PhylomeDBi | O34484 |
Enzyme and pathway databases
BioCyci | BSUB:BSU07690-MONOMER |
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 |
MobiDBi | Search... |
Entry informationi
Entry namei | MAP12_BACSU | |
Accessioni | O34484Primary (citable) accession number: O34484 Secondary accession number(s): Q79ET8 | |
Entry historyi | Integrated into UniProtKB/Swiss-Prot: | January 20, 2009 |
Last sequence update: | January 1, 1998 | |
Last modified: | May 25, 2022 | |
This is version 133 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
Reference proteomeDocuments
- Peptidase families
Classification of peptidase families and list of entries - SIMILARITY comments
Index of protein domains and families