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Reviewed, UniProtKB/Swiss-Prot P0A078 (AMPM_STAAM)

Last modified July 22, 2008. Version 29. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (4) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

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 lineageBacteriaFirmicutesBacillalesStaphylococcus

Protein attributes

Sequence length252 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is not processed.
Protein existenceEvidence at protein level.

General annotation (Comments)

Function

Removes the amino-terminal methionine from nascent proteins By similarity.

Catalytic activity

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

Cofactor

Binds 2 cobalt ions per subunit By similarity.

Sequence similarities

Belongs to the peptidase M24A family.

Ontologies

Keywords

   LigandCobalt
Metal-binding
   Molecular functionAminopeptidase
Hydrolase
Protease
   Technical term3D-structure
Complete proteome

Gene Ontology (GO)

None. [Check GOA]

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical view

Molecule processing

Chain1 – 252252Methionine aminopeptidase

Sites

Metal binding931Cobalt 2 By similarity
Metal binding1041Cobalt 1 By similarity
Metal binding1041Cobalt 2 By similarity
Metal binding1681Cobalt 1 By similarity
Metal binding2021Cobalt 1 By similarity
Metal binding2331Cobalt 1 By similarity
Metal binding2331Cobalt 2 By similarity

Secondary structure

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

Details...

Sequences

Sequence LengthMass (Da)Tools
P0A078-1 [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].
[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).

Cross-references

Sequence databases

BA000017 Genomic DNA. Translation: BAB58050.1.
RefSeqNP_372412.1.

3D structure databases

EntryMethodResolution (Å)ChainPositionsPDBsum
1QXWX-ray1.67A1-252[»]
1QXYX-ray1.04A1-252[»]
1QXZX-ray1.68A1-252[»]
ModBaseSearch...

2-D gel databases

World-2DPAGE0002:P0A078.

Genome annotation databases

GeneID1121901.
GenomeReviewsGene locus SAV1888 in contig BA000017_GR.
KEGGsav:SAV1888.

Organism-specific databases

CMRSearch...

Phylogenomic databases

HOGENOMP0A078.

Enzyme and pathway databases

BioCycSAUR158878:SAV1888-MON.

Family and domain databases

InterProIPR001714. Pept_M24_MAP.
IPR002467. Pept_M24A_MAP1.
IPR000994. Peptidase_M24_cat_core.
[Graphical view]
Gene3DG3DSA:3.90.230.10. Peptidase_M24_cat_core. 1 hit.
PANTHERPTHR10804:SF13. Pept_M24A_MAP1. 1 hit.
PTHR10804. Peptidase_M24_cat_core. 1 hit.
PfamPF00557. Peptidase_M24. 1 hit.
[Graphical view]
PRINTSPR00599. MAPEPTIDASE.
TIGRFAMsTIGR00500. met_pdase_I. 1 hit.
ProDomP0A078.
[Graphical view] [Entries sharing at least one domain]
BLOCKSSearch...

Other Resources

BindingDBP0A078.
ProtoNetSearch...

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: July 22, 2008
This is version 29 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHAMAP (High-quality Automated and Manual Annotation of microbial Proteomes)

Relevant documents

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

Peptidase families

Classification of peptidase families and list of entries

UniProtKB secondary accession numbers

Index of UniProtKB secondary accession numbers

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents