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P0A1X6 (AMPM_SALTY) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 54. 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
Synonyms:pepM
Ordered Locus Names:STM0215
OrganismSalmonella typhimurium
Taxonomic identifier90371 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeSalmonella

Protein attributes

Sequence length264 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
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 By similarity.

Binds 1 sodium ion per subunit. The sodium ion has a structural role By similarity.

Sequence similarities

Belongs to the peptidase M24A family.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed Ref.3
Chain2 – 264263Methionine aminopeptidase
PRO_0000148952

Sites

Metal binding971Cobalt 1 By similarity
Metal binding1081Cobalt 1 By similarity
Metal binding1081Cobalt 2 By similarity
Metal binding1711Cobalt 2 By similarity
Metal binding2041Cobalt 2 By similarity
Metal binding2351Cobalt 1 By similarity
Metal binding2351Cobalt 2 By similarity
Binding site791Substrate By similarity
Binding site1781Substrate By similarity

Experimental info

Sequence conflict136 – 1383GIK → ALR AA sequence Ref.3
Sequence conflict1451R → N AA sequence Ref.3
Sequence conflict1481T → E AA sequence Ref.3
Sequence conflict1591G → A AA sequence Ref.3

Sequences

Sequence LengthMass (Da)Tools
P0A1X6 [UniParc].

Last modified January 23, 2007. Version 2.
Checksum: 8563A54BBE98A860

FASTA26429,292
        10         20         30         40         50         60 
MAISIKTSED IEKMRVAGRL AAEVLEMIEP YIKPGVTTGE LDRICNDYIV NEQHAISACL 

        70         80         90        100        110        120 
GYHGYPKSVC ISINEVVCHG IPDDAKHLKD GDIVNIDVTV IKDEFHGDTS KMFIVGKPTI 

       130        140        150        160        170        180 
LGERLCRVTQ ESLYLGIKMV KPGIRLRTIG AAIQKYAEGE GFSVVREYCG HGIGRGFHEE 

       190        200        210        220        230        240 
PQVLHYDADD GGVVLQPGMT FTIEPMLNAG DYRIRTMKDG WTVKTKDRSL SAQYEHTIVV 

       250        260 
TENGCEILTL RKDDTIPAII THDE 

« Hide

References

« Hide 'large scale' references
[1]"Cloning and nucleotide sequence of the Salmonella typhimurium pepM gene."
Movva N.R., Semon D., Meyer C., Kawashima E., Wingfield P., Miller J.L., Miller C.G.
Mol. Gen. Genet. 223:345-348(1990) [PubMed: 2250660] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: LT2.
[2]"Complete genome sequence of Salmonella enterica serovar Typhimurium LT2."
McClelland M., Sanderson K.E., Spieth J., Clifton S.W., Latreille P., Courtney L., Porwollik S., Ali J., Dante M., Du F., Hou S., Layman D., Leonard S., Nguyen C., Scott K., Holmes A., Grewal N., Mulvaney E. expand/collapse author list , Ryan E., Sun H., Florea L., Miller W., Stoneking T., Nhan M., Waterston R., Wilson R.K.
Nature 413:852-856(2001) [PubMed: 11677609] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: LT2 / SGSC1412 / ATCC 700720.
[3]"Purification and characterization of a methionine-specific aminopeptidase from Salmonella typhimurium."
Wingfield P., Graber P., Turcatti G., Movva N.R., Pelletier M., Craig S., Rose K., Miller C.G.
Eur. J. Biochem. 180:23-32(1989) [PubMed: 2651123] [Abstract]
Cited for: PROTEIN SEQUENCE OF 2-264.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
X55778 Genomic DNA. Translation: CAA39298.1.
AE006468 Genomic DNA. Translation: AAL19179.1.
PIRS12027.
RefSeqNP_459220.1. NC_003197.1.

3D structure databases

ProteinModelPortalP0A1X6.
SMRP0A1X6. Positions 2-264.
ModBaseSearch...

Protein family/group databases

MEROPSM24.001.

Proteomic databases

PRIDEP0A1X6.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID1251733.
GenomeReviewsGene locus STM0215 in contig AE006468_GR.
KEGGstm:STM0215.
PATRIC32378717. VBISalEnt20916_0228.

Phylogenomic databases

HOGENOMHBG299384.
OMAENGCEIM.
ProtClustDBPRK05716.

Enzyme and pathway databases

BioCycSTYP99287:STM0215-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.
PROSITEPS00680. MAP_1. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameAMPM_SALTY
AccessionPrimary (citable) accession number: P0A1X6
Secondary accession number(s): P10882
Entry history
Integrated into UniProtKB/Swiss-Prot: March 1, 2005
Last sequence update: January 23, 2007
Last modified: January 25, 2012
This is version 54 of the entry and version 2 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