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Protein

Methionine aminopeptidase

Gene

map

Organism
Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720)
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.1 PublicationUniRule annotation

Catalytic activityi

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

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)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei79 – 791SubstrateUniRule annotation
Metal bindingi97 – 971Divalent metal cation 1UniRule annotation
Metal bindingi108 – 1081Divalent metal cation 1UniRule annotation
Metal bindingi108 – 1081Divalent metal cation 2; catalyticUniRule annotation
Metal bindingi171 – 1711Divalent metal cation 2; catalytic; via tele nitrogenUniRule annotation
Binding sitei178 – 1781SubstrateUniRule annotation
Metal bindingi204 – 2041Divalent metal cation 2; catalyticUniRule annotation
Metal bindingi235 – 2351Divalent metal cation 1UniRule annotation
Metal bindingi235 – 2351Divalent metal cation 2; catalyticUniRule annotation

GO - Molecular functioni

  1. metal ion binding Source: UniProtKB-HAMAP
  2. metalloaminopeptidase activity Source: UniProtKB-HAMAP

GO - Biological processi

  1. protein initiator methionine removal Source: UniProtKB-HAMAP
Complete GO annotation...

Keywords - Molecular functioni

Aminopeptidase, Hydrolase, Protease

Keywords - Ligandi

Metal-binding

Enzyme and pathway databases

BioCyciSENT99287:GCTI-214-MONOMER.

Names & Taxonomyi

Protein namesi
Recommended name:
Methionine aminopeptidaseUniRule annotation (EC:3.4.11.18UniRule annotation)
Short name:
MAPUniRule annotation
Short name:
MetAPUniRule annotation
Alternative name(s):
Peptidase MUniRule annotation
Gene namesi
Name:mapUniRule annotation
Synonyms:pepM
Ordered Locus Names:STM0215
OrganismiSalmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720)
Taxonomic identifieri99287 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeSalmonella
ProteomesiUP000001014: Chromosome

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11Removed1 Publication
Chaini2 – 264263Methionine aminopeptidasePRO_0000148952Add
BLAST

Proteomic databases

PaxDbiP0A1X6.
PRIDEiP0A1X6.

Interactioni

Subunit structurei

Monomer.UniRule annotation

Protein-protein interaction databases

STRINGi99287.STM0215.

Structurei

3D structure databases

ProteinModelPortaliP0A1X6.
SMRiP0A1X6. Positions 2-264.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

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

Phylogenomic databases

eggNOGiCOG0024.
HOGENOMiHOG000030427.
KOiK01265.
OMAiPTIQGER.
OrthoDBiEOG6MWNDS.
PhylomeDBiP0A1X6.

Family and domain databases

Gene3Di3.90.230.10. 1 hit.
HAMAPiMF_01974. MetAP_1.
InterProiIPR001714. Pept_M24_MAP.
IPR000994. Pept_M24_structural-domain.
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.

Sequence processingi: The displayed sequence is further processed into a mature form.

P0A1X6-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MAISIKTSED IEKMRVAGRL AAEVLEMIEP YIKPGVTTGE LDRICNDYIV
60 70 80 90 100
NEQHAISACL GYHGYPKSVC ISINEVVCHG IPDDAKHLKD GDIVNIDVTV
110 120 130 140 150
IKDEFHGDTS KMFIVGKPTI LGERLCRVTQ ESLYLGIKMV KPGIRLRTIG
160 170 180 190 200
AAIQKYAEGE GFSVVREYCG HGIGRGFHEE PQVLHYDADD GGVVLQPGMT
210 220 230 240 250
FTIEPMLNAG DYRIRTMKDG WTVKTKDRSL SAQYEHTIVV TENGCEILTL
260
RKDDTIPAII THDE
Length:264
Mass (Da):29,292
Last modified:January 23, 2007 - v2
Checksum:i8563A54BBE98A860
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti136 – 1383GIK → ALR AA sequence (PubMed:2651123)Curated
Sequence conflicti145 – 1451R → N AA sequence (PubMed:2651123)Curated
Sequence conflicti148 – 1481T → E AA sequence (PubMed:2651123)Curated
Sequence conflicti159 – 1591G → A AA sequence (PubMed:2651123)Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X55778 Genomic DNA. Translation: CAA39298.1.
AE006468 Genomic DNA. Translation: AAL19179.1.
PIRiS12027.
RefSeqiNP_459220.1. NC_003197.1.

Genome annotation databases

EnsemblBacteriaiAAL19179; AAL19179; STM0215.
GeneIDi1251733.
KEGGistm:STM0215.
PATRICi32378717. VBISalEnt20916_0228.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X55778 Genomic DNA. Translation: CAA39298.1.
AE006468 Genomic DNA. Translation: AAL19179.1.
PIRiS12027.
RefSeqiNP_459220.1. NC_003197.1.

3D structure databases

ProteinModelPortaliP0A1X6.
SMRiP0A1X6. Positions 2-264.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi99287.STM0215.

Proteomic databases

PaxDbiP0A1X6.
PRIDEiP0A1X6.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAL19179; AAL19179; STM0215.
GeneIDi1251733.
KEGGistm:STM0215.
PATRICi32378717. VBISalEnt20916_0228.

Phylogenomic databases

eggNOGiCOG0024.
HOGENOMiHOG000030427.
KOiK01265.
OMAiPTIQGER.
OrthoDBiEOG6MWNDS.
PhylomeDBiP0A1X6.

Enzyme and pathway databases

BioCyciSENT99287:GCTI-214-MONOMER.

Family and domain databases

Gene3Di3.90.230.10. 1 hit.
HAMAPiMF_01974. MetAP_1.
InterProiIPR001714. Pept_M24_MAP.
IPR000994. Pept_M24_structural-domain.
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...

Publicationsi

« Hide 'large scale' publications
  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] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: LT2.
  2. 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] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 2-264, FUNCTION.

Entry informationi

Entry nameiMAP1_SALTY
AccessioniPrimary (citable) accession number: P0A1X6
Secondary accession number(s): P10882
Entry historyi
Integrated into UniProtKB/Swiss-Prot: March 1, 2005
Last sequence update: January 23, 2007
Last modified: January 7, 2015
This is version 77 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. Peptidase families
    Classification of peptidase families and list of entries
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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 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.