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Protein

Methionine aminopeptidase

Gene

map

Organism
Chlamydia muridarum (strain MoPn / Nigg)
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 sitei118 – 1181SubstrateUniRule annotation
Metal bindingi135 – 1351Divalent metal cation 1UniRule annotation
Metal bindingi146 – 1461Divalent metal cation 1UniRule annotation
Metal bindingi146 – 1461Divalent metal cation 2; catalyticUniRule annotation
Metal bindingi209 – 2091Divalent metal cation 2; catalytic; via tele nitrogenUniRule annotation
Binding sitei216 – 2161SubstrateUniRule annotation
Metal bindingi241 – 2411Divalent metal cation 2; catalyticUniRule annotation
Metal bindingi273 – 2731Divalent metal cation 1UniRule annotation
Metal bindingi273 – 2731Divalent 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

BioCyciCMUR243161:GHYU-253-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:TC_0240
OrganismiChlamydia muridarum (strain MoPn / Nigg)
Taxonomic identifieri243161 [NCBI]
Taxonomic lineageiBacteriaChlamydiaeChlamydialesChlamydiaceaeChlamydia/Chlamydophila groupChlamydia
ProteomesiUP000000800 Componenti: Chromosome

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 291291Methionine aminopeptidasePRO_0000148932Add
BLAST

Interactioni

Subunit structurei

Monomer.UniRule annotation

Protein-protein interaction databases

STRINGi243161.CmurN_010100001203.

Structurei

3D structure databases

ProteinModelPortaliQ9PL68.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

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

Phylogenomic databases

eggNOGiCOG0024.
KOiK01265.
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.
IPR004027. SEC_C_motif.
[Graphical view]
PfamiPF00557. Peptidase_M24. 1 hit.
PF02810. SEC-C. 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.

Q9PL68-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MKRNDPCWCG SQKKWKHCHY PTKPERPSDN LRQLYASRYD IIIKTPDQIE
60 70 80 90 100
KIRKACQVTA RILDALCKAA KEGVTTNELD QLSCNLHKQY NAIPAPLNYG
110 120 130 140 150
QPPFPKTICT SLNEVICHGI PNDTPLQNGD IMNIDVSCIV DGFYGDCSRM
160 170 180 190 200
VMIGEVPEIK KKVCEASLEA LNAAIAILEP NLPLYEIGEV IENCAARYGF
210 220 230 240 250
SVVDQFVGHG VGVRFHENPY VAHHRNSCKI PLAPGMTFTI EPMINVGKKE
260 270 280 290
GFIDPTNHWE ARTCDHQPSA QWEHTVLITD SGYEILTLLD N
Length:291
Mass (Da):32,646
Last modified:April 27, 2001 - v2
Checksum:iBAA33E190FC6160E
GO

Sequence cautioni

The sequence AAF39111.1 differs from that shown. Reason: Erroneous initiation. Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AE002160 Genomic DNA. Translation: AAF39111.1. Different initiation.
PIRiG81724.
RefSeqiWP_010229916.1. NZ_ACOV01000003.1.

Genome annotation databases

EnsemblBacteriaiAAF39111; AAF39111; TC_0240.
GeneIDi1246409.
KEGGicmu:TC_0240.
PATRICi20371872. VBIChlMur19118_0263.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AE002160 Genomic DNA. Translation: AAF39111.1. Different initiation.
PIRiG81724.
RefSeqiWP_010229916.1. NZ_ACOV01000003.1.

3D structure databases

ProteinModelPortaliQ9PL68.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi243161.CmurN_010100001203.

Protein family/group databases

MEROPSiM24.001.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAF39111; AAF39111; TC_0240.
GeneIDi1246409.
KEGGicmu:TC_0240.
PATRICi20371872. VBIChlMur19118_0263.

Phylogenomic databases

eggNOGiCOG0024.
KOiK01265.
OrthoDBiEOG6MWNDS.

Enzyme and pathway databases

BioCyciCMUR243161:GHYU-253-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.
IPR004027. SEC_C_motif.
[Graphical view]
PfamiPF00557. Peptidase_M24. 1 hit.
PF02810. SEC-C. 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: MoPn / Nigg.

Entry informationi

Entry nameiMAP1_CHLMU
AccessioniPrimary (citable) accession number: Q9PL68
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 27, 2001
Last sequence update: April 27, 2001
Last modified: July 22, 2015
This is version 100 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

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.