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P28617 (AMPM_GEOSE) Reviewed, UniProtKB/Swiss-Prot

Last modified November 16, 2011. Version 63. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
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Names and origin

Protein namesRecommended name:
Methionine aminopeptidase

Short name=MAP
EC=3.4.11.18
Alternative name(s):
Peptidase M
Gene names
Name:map
OrganismGeobacillus stearothermophilus (Bacillus stearothermophilus)
Taxonomic identifier1422 [NCBI]
Taxonomic lineageBacteriaFirmicutesBacillalesBacillaceaeGeobacillus

Protein attributes

Sequence length51 AA.
Sequence statusFragment.
Protein existenceInferred from homology

General annotation (Comments)

Function

Removes the amino-terminal methionine from nascent proteins.

Catalytic activity

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

Cofactor

Binds 2 cobalt ions per subunit. The true nature of the physiological cofactor is under debate. The enzyme is also active with zinc, manganese or divalent iron ions Potential.

Sequence similarities

Belongs to the peptidase M24A family.

Ontologies

Keywords
   LigandCobalt
   Molecular functionAminopeptidase
Hydrolase
Protease
Gene Ontology (GO)
   Biological processcellular process

Inferred from electronic annotation. Source: InterPro

proteolysis

Inferred from electronic annotation. Source: UniProtKB-KW

   Molecular functionaminopeptidase activity

Inferred from electronic annotation. Source: UniProtKB-KW

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – ›51›51Methionine aminopeptidase
PRO_0000148926

Experimental info

Non-terminal residue511

Sequences

Sequence LengthMass (Da)Tools
P28617 [UniParc].

Last modified December 1, 1992. Version 1.
Checksum: 1E270FB8C42489D8

FASTA515,698
        10         20         30         40         50 
MIICKTAHEI TLMREAGKIV SATLEELKNH IRPGVTTKEL DAIAEEVIRS H 

« Hide

References

[1]"Zinc, a novel structural element found in the family of bacterial adenylate kinases."
Glaser P., Presecan E., Delepierre M., Surewicz W.K., Mantsch H.H., Barzu O., Gilles A.M.
Biochemistry 31:3038-3043(1992) [PubMed: 1554691] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
M88104 Genomic DNA. Translation: AAA22206.1.
PIRC42196.

3D structure databases

ProteinModelPortalP28617.
ModBaseSearch...

Protein family/group databases

MEROPSM24.001.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Family and domain databases

InterProIPR000994. Pept_M24_structural-domain.
[Graphical view]
Gene3DG3DSA:3.90.230.10. Peptidase_M24_cat_core. 1 hit.
PfamPF00557. Peptidase_M24. 1 hit.
[Graphical view]
SUPFAMSSF55920. Peptidase_M24_cat_core. 1 hit.
PROSITEPS00680. MAP_1. Partial match.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameAMPM_GEOSE
AccessionPrimary (citable) accession number: P28617
Entry history
Integrated into UniProtKB/Swiss-Prot: December 1, 1992
Last sequence update: December 1, 1992
Last modified: November 16, 2011
This is version 63 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

Peptidase families

Classification of peptidase families and list of entries

SIMILARITY comments

Index of protein domains and families