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P0A078 (AMPM_STAAM) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 53. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | 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
Ordered Locus Names:SAV1888
OrganismStaphylococcus aureus (strain Mu50 / ATCC 700699) [Complete proteome] [HAMAP]
Taxonomic identifier158878 [NCBI]
Taxonomic lineageBacteria › Firmicutes › Bacillales › Staphylococcus

Protein attributes

Sequence length252 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

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.

Sequence similarities

Belongs to the peptidase M24A family.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 252252Methionine aminopeptidase
PRO_0000148955

Sites

Metal binding931Cobalt 1
Metal binding1041Cobalt 1
Metal binding1041Cobalt 2
Metal binding1681Cobalt 2
Metal binding2021Cobalt 2
Metal binding2331Cobalt 1
Metal binding2331Cobalt 2
Binding site761Substrate
Binding site1751Substrate

Secondary structure

1 ............................... 252
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P0A078 [UniParc].

Last modified March 1, 2005. Version 1.
Checksum: 3E42E623286B537B

FASTA25227,502
        10         20         30         40         50         60 
MIVKTEEELQ ALKEIGYICA KVRNTMQAAT KPGITTKELD NIAKELFEEY GAISAPIHDE 

        70         80         90        100        110        120 
NFPGQTCISV NEEVAHGIPS KRVIREGDLV NIDVSALKNG YYADTGISFV VGESDDPMKQ 

       130        140        150        160        170        180 
KVCDVATMAF ENAIAKVKPG TKLSNIGKAV HNTARQNDLK VIKNLTGHGV GLSLHEAPAH 

       190        200        210        220        230        240 
VLNYFDPKDK TLLTEGMVLA IEPFISSNAS FVTEGKNEWA FETSDKSFVA QIEHTVIVTK 

       250 
DGPILTTKIE EE

« Hide

References

« Hide 'large scale' references
[1]"Whole genome sequencing of meticillin-resistant Staphylococcus aureus."
Kuroda M., Ohta T., Uchiyama I., Baba T., Yuzawa H., Kobayashi I., Cui L., Oguchi A., Aoki K., Nagai Y., Lian J.-Q., Ito T., Kanamori M., Matsumaru H., Maruyama A., Murakami H., Hosoyama A., Mizutani-Ui Y. expand/collapse author list , Takahashi N.K., Sawano T., Inoue R., Kaito C., Sekimizu K., Hirakawa H., Kuhara S., Goto S., Yabuzaki J., Kanehisa M., Yamashita A., Oshima K., Furuya K., Yoshino C., Shiba T., Hattori M., Ogasawara N., Hayashi H., Hiramatsu K.
Lancet 357:1225-1240(2001) [PubMed: 11418146] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: Mu50 / ATCC 700699.
[2]"Crystal structures of Staphylococcusaureus methionine aminopeptidase complexed with keto heterocycle and aminoketone inhibitors reveal the formation of a tetrahedral intermediate."
Douangamath A., Dale G.E., D'Arcy A., Almstetter M., Eckl R., Frutos-Hoener A., Henkel B., Illgen K., Nerdinger S., Schulz H., Mac Sweeney A., Thormann M., Treml A., Pierau S., Wadman S., Oefner C.
J. Med. Chem. 47:1325-1328(2004) [PubMed: 14998322] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.04 ANGSTROMS) IN COMPLEXES WITH COBALT IONS AND INHIBITOR.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		BA000017 Genomic DNA. Translation: BAB58050.1.
RefSeqNP_372412.1. NC_002758.2.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1QXWX-ray1.67A1-252[»]
1QXYX-ray1.04A1-252[»]
1QXZX-ray1.68A1-252[»]
ProteinModelPortalP0A078.
SMRP0A078. Positions 1-249.
ModBaseSearch...

Protein-protein interaction databases

STRINGP0A078.

2D gel databases

World-2DPAGE0002:P0A078.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaEBSTAT00000005509; EBSTAP00000005327; EBSTAG00000005508.
GeneID1121901.
GenomeReviewsGene locus SAV1888 in contig BA000017_GR.
KEGGsav:SAV1888.
PATRIC19564622. VBIStaAur52173_1950.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0024.
GeneTreeEBGT00050000023792.
HOGENOMHBG299384.
OMAVFTVEPF.
ProtClustDBPRK05716.

Enzyme and pathway databases

BioCycSAUR158878:SAV1888-MONOMER.

Family and domain databases

InterProIPR001714. Pept_M24_MAP.
IPR000994. Pept_M24_structural-domain.
IPR002467. Pept_M24A_MAP1.
[Graphical view]
Gene3DG3DSA:3.90.230.10. Peptidase_M24_cat_core. 1 hit.
KOK01265.
PfamPF00557. Peptidase_M24. 1 hit.
[Graphical view]
PRINTSPR00599. MAPEPTIDASE.
SUPFAMSSF55920. Peptidase_M24_cat_core. 1 hit.
TIGRFAMsTIGR00500. Met_pdase_I. 1 hit.
ProtoNetSearch...

Other

BindingDBP0A078.

Entry information

Entry nameAMPM_STAAM
AccessionPrimary (citable) accession number: P0A078
Secondary accession number(s): Q9KWL1
Entry history
Integrated into UniProtKB/Swiss-Prot: March 1, 2005
Last sequence update: March 1, 2005
Last modified: January 25, 2012
This is version 53 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

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families

to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents