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Q59509

- MAP1_MYCCT

UniProt

Q59509 - MAP1_MYCCT

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Protein

Methionine aminopeptidase

Gene

map

Organism
Mycoplasma capricolum subsp. capricolum (strain California kid / ATCC 27343 / NCTC 10154)
Status
Reviewed - 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 Fe(2+)-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 sitei77 – 771SubstrateUniRule annotation
Metal bindingi94 – 941Divalent metal cation 1UniRule annotation
Metal bindingi105 – 1051Divalent metal cation 1UniRule annotation
Metal bindingi105 – 1051Divalent metal cation 2; catalyticUniRule annotation
Metal bindingi169 – 1691Divalent metal cation 2; catalytic; via tele nitrogenUniRule annotation
Binding sitei176 – 1761SubstrateUniRule annotation
Metal bindingi202 – 2021Divalent metal cation 2; catalyticUniRule annotation
Metal bindingi233 – 2331Divalent metal cation 1UniRule annotation
Metal bindingi233 – 2331Divalent 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

BioCyciMCAP340047:GC0H-672-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:MCAP_0675
OrganismiMycoplasma capricolum subsp. capricolum (strain California kid / ATCC 27343 / NCTC 10154)
Taxonomic identifieri340047 [NCBI]
Taxonomic lineageiBacteriaTenericutesMollicutesMycoplasmataceaeMycoplasma
ProteomesiUP000001928: Chromosome

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 251251Methionine aminopeptidasePRO_0000148944Add
BLAST

Interactioni

Subunit structurei

Monomer.UniRule annotation

Protein-protein interaction databases

STRINGi340047.MCAP_0675.

Structurei

3D structure databases

ProteinModelPortaliQ59509.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

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

Phylogenomic databases

eggNOGiCOG0024.
HOGENOMiHOG000030426.
KOiK01265.
OMAiMERFIGH.
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.

Q59509-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MITIKNQEQI QKMKIAGQVL AKGLNLLKSM IKPGVNCLDL DKAFEEFIKQ
60 70 80 90 100
NGCESNFKNY QGFPKTICIS INDQLIHGIP RDRVLLDGDV VSIDAGCMYE
110 120 130 140 150
KWHADSAFTM VCGIAKNKKN DILIRVTEEA LELAIAELKP GIRVGTIGSI
160 170 180 190 200
IQNYVESFDF SVPRDYTGHG IGLALHEDPY IPNYGIPNTG IRLQEGMVIC
210 220 230 240 250
IEPMVQMGTY KTKIADDKWT VYSADHSITA HFEHTILITK DGCEVLTKTE

R
Length:251
Mass (Da):28,036
Last modified:March 21, 2006 - v2
Checksum:i6AD06BE56A670EF9
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti113 – 1153GIA → EIR in CAA83714. (PubMed:7476192)Curated
Sequence conflicti125 – 1251R → G in CAA83714. (PubMed:7476192)Curated
Sequence conflicti161 – 1611S → N in CAA83714. (PubMed:7476192)Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CP000123 Genomic DNA. Translation: ABC01688.1.
Z33034 Genomic DNA. Translation: CAA83714.1.
PIRiS77843. S48593.
RefSeqiYP_424639.1. NC_007633.1.

Genome annotation databases

EnsemblBacteriaiABC01688; ABC01688; MCAP_0675.
GeneIDi3829108.
KEGGimcp:MCAP_0675.
PATRICi20005827. VBIMycCap130493_0668.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CP000123 Genomic DNA. Translation: ABC01688.1 .
Z33034 Genomic DNA. Translation: CAA83714.1 .
PIRi S77843. S48593.
RefSeqi YP_424639.1. NC_007633.1.

3D structure databases

ProteinModelPortali Q59509.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

STRINGi 340047.MCAP_0675.

Protein family/group databases

MEROPSi M24.001.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblBacteriai ABC01688 ; ABC01688 ; MCAP_0675 .
GeneIDi 3829108.
KEGGi mcp:MCAP_0675.
PATRICi 20005827. VBIMycCap130493_0668.

Phylogenomic databases

eggNOGi COG0024.
HOGENOMi HOG000030426.
KOi K01265.
OMAi MERFIGH.
OrthoDBi EOG6MWNDS.

Enzyme and pathway databases

BioCyci MCAP340047:GC0H-672-MONOMER.

Family and domain databases

Gene3Di 3.90.230.10. 1 hit.
HAMAPi MF_01974. MetAP_1.
InterProi IPR001714. Pept_M24_MAP.
IPR000994. Pept_M24_structural-domain.
IPR002467. Pept_M24A_MAP1.
[Graphical view ]
Pfami PF00557. Peptidase_M24. 1 hit.
[Graphical view ]
PRINTSi PR00599. MAPEPTIDASE.
SUPFAMi SSF55920. SSF55920. 1 hit.
TIGRFAMsi TIGR00500. met_pdase_I. 1 hit.
PROSITEi PS00680. MAP_1. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: California kid / ATCC 27343 / NCTC 10154.
  2. "Exploring the Mycoplasma capricolum genome: a minimal cell reveals its physiology."
    Bork P., Ouzounis C., Casari G., Schneider R., Sander C., Dolan M., Gilbert W., Gillevet P.M.
    Mol. Microbiol. 16:955-967(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 111-251.

Entry informationi

Entry nameiMAP1_MYCCT
AccessioniPrimary (citable) accession number: Q59509
Secondary accession number(s): Q2SRH4
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: March 21, 2006
Last modified: November 26, 2014
This is version 105 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