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Protein

Methionine aminopeptidase

Gene

map

Organism
Staphylococcus aureus (strain Mu50 / ATCC 700699)
Status
Reviewed-Annotation score: Annotation score: 3 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.UniRule annotation

Catalytic activityi

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

Cofactori

Co2+UniRule annotation1 Publication, 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 annotation1 Publication

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei76 – 761SubstrateUniRule annotation1 Publication
Metal bindingi93 – 931Divalent metal cation 1UniRule annotation1 Publication
Metal bindingi104 – 1041Divalent metal cation 1UniRule annotation1 Publication
Metal bindingi104 – 1041Divalent metal cation 2; catalyticUniRule annotation1 Publication
Metal bindingi168 – 1681Divalent metal cation 2; catalytic; via tele nitrogenUniRule annotation1 Publication
Binding sitei175 – 1751SubstrateUniRule annotation1 Publication
Metal bindingi202 – 2021Divalent metal cation 2; catalyticUniRule annotation1 Publication
Metal bindingi233 – 2331Divalent metal cation 1UniRule annotation1 Publication
Metal bindingi233 – 2331Divalent metal cation 2; catalyticUniRule annotation1 Publication

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Aminopeptidase, Hydrolase, Protease

Keywords - Ligandi

Metal-binding

Enzyme and pathway databases

BioCyciSAUR158878:GJJ5-1943-MONOMER.

Protein family/group databases

MEROPSiM24.036.

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
Ordered Locus Names:SAV1888
OrganismiStaphylococcus aureus (strain Mu50 / ATCC 700699)
Taxonomic identifieri158878 [NCBI]
Taxonomic lineageiBacteriaFirmicutesBacilliBacillalesStaphylococcaceaeStaphylococcus
Proteomesi
  • UP000002481 Componenti: Chromosome

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 252252Methionine aminopeptidasePRO_0000148955Add
BLAST

Proteomic databases

PaxDbiP0A078.

2D gel databases

World-2DPAGE0002:P0A078.

Interactioni

Subunit structurei

Monomer.UniRule annotation

Protein-protein interaction databases

STRINGi158878.SAV1888.

Structurei

Secondary structure

1
252
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi6 – 2924Combined sources
Helixi36 – 5015Combined sources
Helixi55 – 606Combined sources
Beta strandi63 – 708Combined sources
Beta strandi73 – 753Combined sources
Beta strandi89 – 9810Combined sources
Beta strandi101 – 11010Combined sources
Helixi118 – 13417Combined sources
Helixi144 – 15613Combined sources
Beta strandi167 – 1693Combined sources
Beta strandi171 – 18111Combined sources
Beta strandi197 – 2015Combined sources
Beta strandi204 – 2085Combined sources
Beta strandi216 – 2194Combined sources
Beta strandi229 – 2379Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1QXWX-ray1.67A1-252[»]
1QXYX-ray1.04A1-252[»]
1QXZX-ray1.68A1-252[»]
ProteinModelPortaliP0A078.
SMRiP0A078. Positions 1-249.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP0A078.

Family & Domainsi

Sequence similaritiesi

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

Phylogenomic databases

eggNOGiENOG4105CA1. Bacteria.
COG0024. LUCA.
HOGENOMiHOG000030426.
KOiK01265.
OMAiVIKDEYH.
PhylomeDBiP0A078.

Family and domain databases

Gene3Di3.90.230.10. 1 hit.
HAMAPiMF_01974. MetAP_1. 1 hit.
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.

Sequencei

Sequence statusi: Complete.

P0A078-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MIVKTEEELQ ALKEIGYICA KVRNTMQAAT KPGITTKELD NIAKELFEEY
60 70 80 90 100
GAISAPIHDE NFPGQTCISV NEEVAHGIPS KRVIREGDLV NIDVSALKNG
110 120 130 140 150
YYADTGISFV VGESDDPMKQ KVCDVATMAF ENAIAKVKPG TKLSNIGKAV
160 170 180 190 200
HNTARQNDLK VIKNLTGHGV GLSLHEAPAH VLNYFDPKDK TLLTEGMVLA
210 220 230 240 250
IEPFISSNAS FVTEGKNEWA FETSDKSFVA QIEHTVIVTK DGPILTTKIE

EE
Length:252
Mass (Da):27,502
Last modified:March 1, 2005 - v1
Checksum:i3E42E623286B537B
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
BA000017 Genomic DNA. Translation: BAB58050.1.
RefSeqiWP_000636142.1. NC_002758.2.

Genome annotation databases

EnsemblBacteriaiBAB58050; BAB58050; SAV1888.
KEGGisav:SAV1888.
PATRICi19564622. VBIStaAur52173_1950.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
BA000017 Genomic DNA. Translation: BAB58050.1.
RefSeqiWP_000636142.1. NC_002758.2.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1QXWX-ray1.67A1-252[»]
1QXYX-ray1.04A1-252[»]
1QXZX-ray1.68A1-252[»]
ProteinModelPortaliP0A078.
SMRiP0A078. Positions 1-249.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi158878.SAV1888.

Protein family/group databases

MEROPSiM24.036.

2D gel databases

World-2DPAGE0002:P0A078.

Proteomic databases

PaxDbiP0A078.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiBAB58050; BAB58050; SAV1888.
KEGGisav:SAV1888.
PATRICi19564622. VBIStaAur52173_1950.

Phylogenomic databases

eggNOGiENOG4105CA1. Bacteria.
COG0024. LUCA.
HOGENOMiHOG000030426.
KOiK01265.
OMAiVIKDEYH.
PhylomeDBiP0A078.

Enzyme and pathway databases

BioCyciSAUR158878:GJJ5-1943-MONOMER.

Miscellaneous databases

EvolutionaryTraceiP0A078.
PROiP0A078.

Family and domain databases

Gene3Di3.90.230.10. 1 hit.
HAMAPiMF_01974. MetAP_1. 1 hit.
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.
ProtoNetiSearch...

Entry informationi

Entry nameiMAP1_STAAM
AccessioniPrimary (citable) accession number: P0A078
Secondary accession number(s): Q9KWL1
Entry historyi
Integrated into UniProtKB/Swiss-Prot: March 1, 2005
Last sequence update: March 1, 2005
Last modified: September 7, 2016
This is version 91 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. Peptidase families
    Classification of peptidase families and list of entries
  3. SIMILARITY comments
    Index of protein domains and families

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 one 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.