Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

Methionine aminopeptidase 2

Gene

mapB

Organism
Bacillus subtilis (strain 168)
Status
Reviewed-Annotation score: -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.UniRule annotation1 Publication

Catalytic activityi

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

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 keyPosition(s)DescriptionActionsGraphical viewLength
Binding sitei76SubstrateUniRule annotation1
Metal bindingi94Divalent metal cation 1UniRule annotation1
Metal bindingi105Divalent metal cation 1UniRule annotation1
Metal bindingi105Divalent metal cation 2; catalyticUniRule annotation1
Metal bindingi168Divalent metal cation 2; catalytic; via tele nitrogenUniRule annotation1
Binding sitei175SubstrateUniRule annotation1
Metal bindingi202Divalent metal cation 2; catalyticUniRule annotation1
Metal bindingi233Divalent metal cation 1UniRule annotation1
Metal bindingi233Divalent metal cation 2; catalyticUniRule annotation1

GO - Molecular functioni

Keywordsi

Molecular functionAminopeptidase, Hydrolase, Protease
LigandMetal-binding

Enzyme and pathway databases

BioCyciBSUB:BSU07690-MONOMER

Protein family/group databases

MEROPSiM24.036

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
OrganismiBacillus subtilis (strain 168)
Taxonomic identifieri224308 [NCBI]
Taxonomic lineageiBacteriaFirmicutesBacilliBacillalesBacillaceaeBacillus
Proteomesi
  • UP000001570 Componenti: Chromosome

Subcellular locationi

GO - Cellular componenti

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00003612751 – 249Methionine aminopeptidase 2Add BLAST249

Proteomic databases

PaxDbiO34484
PRIDEiO34484

Expressioni

Inductioni

Expressed at very low levels throughout growth.1 Publication

Interactioni

Subunit structurei

Monomer.UniRule annotation

Protein-protein interaction databases

STRINGi224308.Bsubs1_010100004293

Structurei

3D structure databases

ProteinModelPortaliO34484
SMRiO34484
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the peptidase M24A family. Methionine aminopeptidase type 1 subfamily.UniRule annotation

Phylogenomic databases

eggNOGiENOG4106A4F Bacteria
COG0024 LUCA
HOGENOMiHOG000030426
InParanoidiO34484
KOiK01265
OMAiESMWAGI
PhylomeDBiO34484

Family and domain databases

CDDicd01086 MetAP1, 1 hit
HAMAPiMF_01974 MetAP_1, 1 hit
InterProiView protein in InterPro
IPR036005 Creatinase/aminopeptidase-like
IPR000994 Pept_M24
IPR001714 Pept_M24_MAP
IPR002467 Pept_M24A_MAP1
PfamiView protein in Pfam
PF00557 Peptidase_M24, 1 hit
PRINTSiPR00599 MAPEPTIDASE
SUPFAMiSSF55920 SSF55920, 1 hit
TIGRFAMsiTIGR00500 met_pdase_I, 1 hit

Sequencei

Sequence statusi: Complete.

O34484-1 [UniParc]FASTAAdd to basket

« Hide

        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
Length:249
Mass (Da):27,211
Last modified:January 1, 1998 - v1
Checksum:iC3C36DE944528E3E
GO

Mass spectrometryi

Molecular mass is 27209.35±2.14 Da from positions 1 - 249. 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
PIRiE69810
RefSeqiNP_388650.1, NC_000964.3
WP_003233698.1, NZ_JNCM01000032.1

Genome annotation databases

EnsemblBacteriaiCAB12598; CAB12598; BSU07690
GeneIDi936121
KEGGibsu:BSU07690
PATRICifig|224308.179.peg.835

Similar proteinsi

Entry informationi

Entry nameiMAP12_BACSU
AccessioniPrimary (citable) accession number: O34484
Secondary accession number(s): Q79ET8
Entry historyiIntegrated into UniProtKB/Swiss-Prot: January 20, 2009
Last sequence update: January 1, 1998
Last modified: March 28, 2018
This is version 119 of the entry and version 1 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Cookie policy

We would like to use anonymized google analytics cookies to gather statistics on how uniprot.org is used in aggregate. Learn more

UniProt is an ELIXIR core data resource
Main funding by: National Institutes of Health