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Protein

Methionine aminopeptidase

Gene

map

Organism
Treponema pallidum (strain Nichols)
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Protein inferred from homologyi

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 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 sitei76 – 761SubstrateUniRule annotation
Metal bindingi93 – 931Divalent metal cation 1UniRule annotation
Metal bindingi104 – 1041Divalent metal cation 1UniRule annotation
Metal bindingi104 – 1041Divalent metal cation 2; catalyticUniRule annotation
Metal bindingi167 – 1671Divalent metal cation 2; catalytic; via tele nitrogenUniRule annotation
Binding sitei174 – 1741SubstrateUniRule annotation
Metal bindingi201 – 2011Divalent metal cation 2; catalyticUniRule annotation
Metal bindingi232 – 2321Divalent metal cation 1UniRule annotation
Metal bindingi232 – 2321Divalent metal cation 2; catalyticUniRule annotation

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Aminopeptidase, Hydrolase, Protease

Keywords - Ligandi

Metal-binding

Enzyme and pathway databases

BioCyciTPAL243276:GC1H-890-MONOMER.

Protein family/group databases

MEROPSiM24.001.

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:TP_0842
OrganismiTreponema pallidum (strain Nichols)
Taxonomic identifieri243276 [NCBI]
Taxonomic lineageiBacteriaSpirochaetesSpirochaetalesSpirochaetaceaeTreponema
ProteomesiUP000000811 Componenti: Chromosome

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 255255Methionine aminopeptidasePRO_0000148966Add
BLAST

Interactioni

Subunit structurei

Monomer.UniRule annotation

Protein-protein interaction databases

IntActiO83814. 7 interactions.
STRINGi243276.TP0842.

Structurei

3D structure databases

ProteinModelPortaliO83814.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

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

Phylogenomic databases

eggNOGiCOG0024.
KOiK01265.
OMAiLGYHGFT.
OrthoDBiEOG6MWNDS.

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.

O83814-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MIRIKTPEQI DGIRASCKAL ARLFDVLIPL VKPGVQTQEL DAFCQRFIRS
60 70 80 90 100
VGGVPAWFSE GFPAAACISI NEEVIHGLPS ARVIQDGDLV SLDVGINLNG
110 120 130 140 150
YISDACRTVP VGGVAHERLE LLRVTTECLR AGIKACRAGA RVRAVSRAVY
160 170 180 190 200
AVAARHRFGV VYEYCGHGVG LAVHEEPNIP NVPGLEGPNP RFLPGMVVAI
210 220 230 240 250
EPMLTLGTDE VRTSADGWTV VTADGSCACH VEHTVAVFAD HTEVLTEPTE

VERTG
Length:255
Mass (Da):27,316
Last modified:November 1, 1998 - v1
Checksum:i4EDE582C67F3526A
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AE000520 Genomic DNA. Translation: AAC65810.1.
PIRiB71273.
RefSeqiNP_219278.1. NC_000919.1.
WP_010882286.1. NC_021490.2.
YP_008091667.1. NC_021490.2.

Genome annotation databases

EnsemblBacteriaiAAC65810; AAC65810; TP_0842.
GeneIDi2611002.
KEGGitpa:TP0842.
tpw:TPANIC_0842.
PATRICi20531791. VBITrePal57110_0893.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AE000520 Genomic DNA. Translation: AAC65810.1.
PIRiB71273.
RefSeqiNP_219278.1. NC_000919.1.
WP_010882286.1. NC_021490.2.
YP_008091667.1. NC_021490.2.

3D structure databases

ProteinModelPortaliO83814.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

IntActiO83814. 7 interactions.
STRINGi243276.TP0842.

Protein family/group databases

MEROPSiM24.001.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAC65810; AAC65810; TP_0842.
GeneIDi2611002.
KEGGitpa:TP0842.
tpw:TPANIC_0842.
PATRICi20531791. VBITrePal57110_0893.

Phylogenomic databases

eggNOGiCOG0024.
KOiK01265.
OMAiLGYHGFT.
OrthoDBiEOG6MWNDS.

Enzyme and pathway databases

BioCyciTPAL243276:GC1H-890-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

  1. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: Nichols.

Entry informationi

Entry nameiMAP1_TREPA
AccessioniPrimary (citable) accession number: O83814
Entry historyi
Integrated into UniProtKB/Swiss-Prot: December 15, 1998
Last sequence update: November 1, 1998
Last modified: May 27, 2015
This is version 103 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

Complete proteome, 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.