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Protein

Methionine aminopeptidase 1

Gene

map

Organism
Bacillus subtilis (strain 168)
Status
Reviewed-Annotation score: Annotation score: 4 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.UniRule annotation1 Publication

Catalytic activityi

Release of N-terminal amino acids, preferentially methionine, from peptides and arylamides.UniRule annotation1 Publication

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 sitei77SubstrateUniRule 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 bindingi201Divalent metal cation 2; catalyticUniRule annotation1
Metal bindingi232Divalent metal cation 1UniRule annotation1
Metal bindingi232Divalent metal cation 2; catalyticUniRule annotation1

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Aminopeptidase, Hydrolase, Protease

Keywords - Ligandi

Metal-binding

Enzyme and pathway databases

BioCyciBSUB:BSU01380-MONOMER.

Names & Taxonomyi

Protein namesi
Recommended name:
Methionine aminopeptidase 1UniRule annotation (EC:3.4.11.18UniRule annotation)
Short name:
MAP 1UniRule annotation
Short name:
MetAP 1UniRule annotation
Alternative name(s):
Peptidase MUniRule annotation
Gene namesi
Name:mapUniRule annotation
Ordered Locus Names:BSU01380
OrganismiBacillus subtilis (strain 168)
Taxonomic identifieri224308 [NCBI]
Taxonomic lineageiBacteriaFirmicutesBacilliBacillalesBacillaceaeBacillus
Proteomesi
  • UP000001570 Componenti: Chromosome

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00001489271 – 248Methionine aminopeptidase 1Add BLAST248

Proteomic databases

PaxDbiP19994.
PRIDEiP19994.

Expressioni

Inductioni

Expression increases gradually during the log phase of growth.1 Publication

Interactioni

Subunit structurei

Monomer.UniRule annotation

Protein-protein interaction databases

STRINGi224308.Bsubs1_010100000710.

Structurei

3D structure databases

ProteinModelPortaliP19994.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

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

Phylogenomic databases

eggNOGiENOG4105CA1. Bacteria.
COG0024. LUCA.
HOGENOMiHOG000030426.
InParanoidiP19994.
KOiK01265.
OMAiIGQNLHE.
PhylomeDBiP19994.

Family and domain databases

CDDicd01086. MetAP1. 1 hit.
Gene3Di3.90.230.10. 1 hit.
HAMAPiMF_01974. MetAP_1. 1 hit.
InterProiIPR000994. Pept_M24.
IPR001714. Pept_M24_MAP.
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.

P19994-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MIICKTPREL GIMREAGRIV ALTHEELKKH IKPGISTKEL DQIAERFIKK
60 70 80 90 100
QGAIPSFKGY NGFRGSICVS VNEELVHGIP GSRVLKDGDI ISIDIGAKLN
110 120 130 140 150
GYHGDSAWTY PVGNISDDDK KLLEVTEESL YKGLQEAKPG ERLSNISHAI
160 170 180 190 200
QTYVENEQFS VVREYVGHGV GQDLHEDPQI PHYGPPNKGP RLKPGMVLAI
210 220 230 240
EPMVNAGSRY VKTLADNWTV VTVDGKKCAH FEHTIAITET GFDILTRV
Length:248
Mass (Da):27,409
Last modified:February 1, 1991 - v1
Checksum:i6D6F7A593D84A761
GO

Mass spectrometryi

Molecular mass is 27409.17±0.92 Da from positions 1 - 248. 1 Publication

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
D00619 Genomic DNA. Translation: BAA00497.1.
L47971 Genomic DNA. Translation: AAB06821.1.
AL009126 Genomic DNA. Translation: CAB11914.1.
PIRiJS0493.
RefSeqiNP_388019.1. NC_000964.3.
WP_003225828.1. NZ_JNCM01000029.1.

Genome annotation databases

EnsemblBacteriaiCAB11914; CAB11914; BSU01380.
GeneIDi11237902.
938929.
KEGGibsu:BSU01380.
PATRICi18971785. VBIBacSub10457_0141.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
D00619 Genomic DNA. Translation: BAA00497.1.
L47971 Genomic DNA. Translation: AAB06821.1.
AL009126 Genomic DNA. Translation: CAB11914.1.
PIRiJS0493.
RefSeqiNP_388019.1. NC_000964.3.
WP_003225828.1. NZ_JNCM01000029.1.

3D structure databases

ProteinModelPortaliP19994.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi224308.Bsubs1_010100000710.

Proteomic databases

PaxDbiP19994.
PRIDEiP19994.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiCAB11914; CAB11914; BSU01380.
GeneIDi11237902.
938929.
KEGGibsu:BSU01380.
PATRICi18971785. VBIBacSub10457_0141.

Phylogenomic databases

eggNOGiENOG4105CA1. Bacteria.
COG0024. LUCA.
HOGENOMiHOG000030426.
InParanoidiP19994.
KOiK01265.
OMAiIGQNLHE.
PhylomeDBiP19994.

Enzyme and pathway databases

BioCyciBSUB:BSU01380-MONOMER.

Family and domain databases

CDDicd01086. MetAP1. 1 hit.
Gene3Di3.90.230.10. 1 hit.
HAMAPiMF_01974. MetAP_1. 1 hit.
InterProiIPR000994. Pept_M24.
IPR001714. Pept_M24_MAP.
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]
ProtoNetiSearch...

Entry informationi

Entry nameiMAP11_BACSU
AccessioniPrimary (citable) accession number: P19994
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 1, 1991
Last sequence update: February 1, 1991
Last modified: November 30, 2016
This is version 134 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

Complete proteome, Reference proteome

Documents

  1. Bacillus subtilis
    Bacillus subtilis (strain 168): entries, gene names and cross-references to SubtiList
  2. Peptidase families
    Classification of peptidase families and list of entries
  3. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.