Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

Methionine aminopeptidase

Gene

map

Organism
Chlamydia pneumoniae (Chlamydophila pneumoniae)
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

  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

BioCyciCPNE115711:GI7B-871-MONOMER.
CPNE115713:GHEY-1053-MONOMER.
CPNE138677:GH8N-1043-MONOMER.
CPNE182082:GH4N-1082-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:CPn_1009, CP_0844, CpB1046
OrganismiChlamydia pneumoniae (Chlamydophila pneumoniae)
Taxonomic identifieri83558 [NCBI]
Taxonomic lineageiBacteriaChlamydiaeChlamydialesChlamydiaceaeChlamydia/Chlamydophila groupChlamydia
ProteomesiUP000000424: Chromosome, UP000000583: Chromosome, UP000000801: Chromosome, UP000000802: Chromosome

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 291291Methionine aminopeptidasePRO_0000148933Add
BLAST

Interactioni

Subunit structurei

Monomer.UniRule annotation

Protein-protein interaction databases

STRINGi115713.CPn1009.

Structurei

3D structure databases

ProteinModelPortaliQ9Z6Q0.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

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

Phylogenomic databases

eggNOGiCOG0024.
HOGENOMiHOG000030427.
KOiK01265.
OMAiVNVDCST.
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.

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 AAF38634.1 differs from that shown. Reason: Erroneous initiation. Curated
The sequence AAP98976.1 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.
NP_301064.1. NC_002491.1.
NP_445382.2. NC_002179.2.
NP_877319.2. NC_005043.1.

Genome annotation databases

EnsemblBacteriaiAAD19146; AAD19146; CPn_1009.
AAF38634; AAF38634; CP_0844.
AAP98976; AAP98976; CpB1046.
BAA99216; BAA99216; BAA99216.
GeneIDi1467726.
894643.
919776.
963127.
KEGGicpa:CP0844.
cpj:CPj1009.
cpn:CPn1009.
cpt:CpB1046.

Cross-referencesi

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.
NP_301064.1. NC_002491.1.
NP_445382.2. NC_002179.2.
NP_877319.2. NC_005043.1.

3D structure databases

ProteinModelPortaliQ9Z6Q0.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi115713.CPn1009.

Protein family/group databases

MEROPSiM24.001.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAD19146; AAD19146; CPn_1009.
AAF38634; AAF38634; CP_0844.
AAP98976; AAP98976; CpB1046.
BAA99216; BAA99216; BAA99216.
GeneIDi1467726.
894643.
919776.
963127.
KEGGicpa:CP0844.
cpj:CPj1009.
cpn:CPn1009.
cpt:CpB1046.

Phylogenomic databases

eggNOGiCOG0024.
HOGENOMiHOG000030427.
KOiK01265.
OMAiVNVDCST.
OrthoDBiEOG6MWNDS.

Enzyme and pathway databases

BioCyciCPNE115711:GI7B-871-MONOMER.
CPNE115713:GHEY-1053-MONOMER.
CPNE138677:GH8N-1043-MONOMER.
CPNE182082:GH4N-1082-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: CWL029.
  2. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: AR39.
  3. "Comparison of whole genome sequences of Chlamydia pneumoniae J138 from Japan and CWL029 from USA."
    Shirai M., Hirakawa H., Kimoto M., Tabuchi M., Kishi F., Ouchi K., Shiba T., Ishii K., Hattori M., Kuhara S., Nakazawa T.
    Nucleic Acids Res. 28:2311-2314(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: J138.
  4. "The genome sequence of Chlamydia pneumoniae TW183 and comparison with other Chlamydia strains based on whole genome sequence analysis."
    Geng M.M., Schuhmacher A., Muehldorfer I., Bensch K.W., Schaefer K.P., Schneider S., Pohl T., Essig A., Marre R., Melchers K.
    Submitted (MAY-2002) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: TW-183.

Entry informationi

Entry nameiMAP1_CHLPN
AccessioniPrimary (citable) accession number: Q9Z6Q0
Secondary accession number(s): Q9JQD4, Q9K1X1
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 30, 2000
Last sequence update: May 1, 1999
Last modified: January 7, 2015
This is version 111 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

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.