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Protein

Methionine aminopeptidase

Gene

map

Organism
Chlamydia pneumoniae (Chlamydophila pneumoniae)
Status
Reviewed-Annotation score: -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)DescriptionActionsGraphical viewLength
Binding sitei118SubstrateUniRule annotation1
Metal bindingi135Divalent metal cation 1UniRule annotation1
Metal bindingi146Divalent metal cation 1UniRule annotation1
Metal bindingi146Divalent metal cation 2; catalyticUniRule annotation1
Metal bindingi209Divalent metal cation 2; catalytic; via tele nitrogenUniRule annotation1
Binding sitei216SubstrateUniRule annotation1
Metal bindingi241Divalent metal cation 2; catalyticUniRule annotation1
Metal bindingi273Divalent metal cation 1UniRule annotation1
Metal bindingi273Divalent metal cation 2; catalyticUniRule annotation1

GO - Molecular functioni

Keywordsi

Molecular functionAminopeptidase, Hydrolase, Protease
LigandMetal-binding

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:CPn_1009, CP_0844, CpB1046
OrganismiChlamydia pneumoniae (Chlamydophila pneumoniae)
Taxonomic identifieri83558 [NCBI]
Taxonomic lineageiBacteriaChlamydiaeChlamydialesChlamydiaceaeChlamydia/Chlamydophila groupChlamydia
Proteomesi
  • UP000000583 Componenti: Chromosome
  • UP000000801 Componenti: Chromosome

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00001489331 – 291Methionine aminopeptidaseAdd BLAST291

Interactioni

Subunit structurei

Monomer.UniRule annotation

Protein-protein interaction databases

STRINGi182082.CpB1046

Structurei

3D structure databases

ProteinModelPortaliQ9Z6Q0
SMRiQ9Z6Q0
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

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

Phylogenomic databases

eggNOGiENOG4105CA1 Bacteria
COG0024 LUCA
HOGENOMiHOG000030427
KOiK01265
OMAiGDHAYTF
OrthoDBiPOG091H01DX

Family and domain databases

CDDicd01086 MetAP1, 1 hit
HAMAPiMF_01974 MetAP_1, 1 hit
InterProiView protein in InterPro
IPR036005 Creatinase/aminopeptidase-like
IPR000994 Pept_M24
IPR001714 Pept_M24_MAP
IPR002467 Pept_M24A_MAP1
IPR004027 SEC_C_motif
PfamiView protein in Pfam
PF00557 Peptidase_M24, 1 hit
PF02810 SEC-C, 1 hit
PRINTSiPR00599 MAPEPTIDASE
SUPFAMiSSF55920 SSF55920, 1 hit
TIGRFAMsiTIGR00500 met_pdase_I, 1 hit
PROSITEiView protein in PROSITE
PS00680 MAP_1, 1 hit

Sequencei

Sequence statusi: Complete.

Q9Z6Q0-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MKRNDPCWCG SGRKWKQCHY PQPPKMSPEA LKQHYASQYN ILLKTPEQKA
60 70 80 90 100
KIYNACQITA RILDELCKAS QKGVTTNELD ELSQELHKKY DAIAAPFHYG
110 120 130 140 150
SPPFPKTICT SLNEVICHGI PNDIPLKDGD IMNIDVSCIV DGYYGDCSRM
160 170 180 190 200
VMIGEVPEIK KKICQAALEC LNDSIAILKP GIPLCEIGEA IEARADTYGF
210 220 230 240 250
SVVDQFVGHG VGIEFHENPY VPHYRNRSMI PLAPGMIFTI EPMINVGKKE
260 270 280 290
GVVDPKNQWE ARTCDNQPSA QWEHTIAITE TGYEILTLLN D
Length:291
Mass (Da):32,596
Last modified:May 1, 1999 - v1
Checksum:i094F6D6E17F23DE9
GO

Sequence cautioni

The sequence AAF38634 differs from that shown. Reason: Erroneous initiation.Curated
The sequence AAP98976 differs from that shown. Reason: Erroneous initiation.Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AE001363 Genomic DNA Translation: AAD19146.1
AE002161 Genomic DNA Translation: AAF38634.1 Different initiation.
BA000008 Genomic DNA Translation: BAA99216.1
AE009440 Genomic DNA Translation: AAP98976.1 Different initiation.
PIRiA81531
E72008
F86616
RefSeqiNP_225203.1, NC_000922.1
WP_010883642.1, NZ_LN847257.1

Genome annotation databases

EnsemblBacteriaiAAD19146; AAD19146; CPn_1009
AAF38634; AAF38634; CP_0844
AAP98976; AAP98976; CpB1046
BAA99216; BAA99216; BAA99216
GeneIDi894643
KEGGicpa:CP_0844
cpj:map
cpn:CPn1009
cpt:CpB1046
PATRICifig|115713.3.peg.1105

Similar proteinsi

Entry informationi

Entry nameiMAP1_CHLPN
AccessioniPrimary (citable) accession number: Q9Z6Q0
Secondary accession number(s): Q9JQD4, Q9K1X1
Entry historyiIntegrated into UniProtKB/Swiss-Prot: May 30, 2000
Last sequence update: May 1, 1999
Last modified: March 28, 2018
This is version 134 of the entry and version 1 of the sequence. See 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
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