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P56102

- MAP1_HELPY

UniProt

P56102 - MAP1_HELPY

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Protein

Methionine aminopeptidase

Gene

map

Organism
Helicobacter pylori (strain ATCC 700392 / 26695) (Campylobacter pylori)
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

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 sitei78 – 781SubstrateUniRule annotation
Metal bindingi95 – 951Divalent metal cation 1UniRule annotation
Metal bindingi106 – 1061Divalent metal cation 1UniRule annotation
Metal bindingi106 – 1061Divalent metal cation 2; catalyticUniRule annotation
Metal bindingi169 – 1691Divalent metal cation 2; catalytic; via tele nitrogenUniRule annotation
Binding sitei176 – 1761SubstrateUniRule annotation
Metal bindingi206 – 2061Divalent metal cation 2; catalyticUniRule annotation
Metal bindingi237 – 2371Divalent metal cation 1UniRule annotation
Metal bindingi237 – 2371Divalent 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

BioCyciHPY:HP1299-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:HP_1299
OrganismiHelicobacter pylori (strain ATCC 700392 / 26695) (Campylobacter pylori)
Taxonomic identifieri85962 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaEpsilonproteobacteriaCampylobacteralesHelicobacteraceaeHelicobacter
ProteomesiUP000000429: Chromosome

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 253253Methionine aminopeptidasePRO_0000148941Add
BLAST

Proteomic databases

PRIDEiP56102.

Interactioni

Subunit structurei

Monomer.UniRule annotation

Protein-protein interaction databases

DIPiDIP-3487N.
IntActiP56102. 4 interactions.
MINTiMINT-173189.
STRINGi85962.HP1299.

Structurei

3D structure databases

ProteinModelPortaliP56102.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

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

Phylogenomic databases

eggNOGiCOG0024.
KOiK01265.
OMAiPAFLGYM.
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.

P56102-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MAISIKSPKE IKALRKAGEL TAQALALLER EVRPGVSLLE LDKMAEDFIK
60 70 80 90 100
SSHARPAFKG LYGFPNSVCM SLNEVVIHGI PTDYVLQEGD IIGLDLGVEV
110 120 130 140 150
DGYYGDSALT LPIGAISPQD EKLLACSKES LMHAINSIRV GMHFKELSQI
160 170 180 190 200
LESTITERGF VPLKGFCGHG IGKKPHEEPE IPNYLEKGVK PNSGPKIKEG
210 220 230 240 250
MVFCLEPMVC QKQGEPKILA DKWSVVSVDG LNTSHHEHTI AIVGNKAVIL

TER
Length:253
Mass (Da):27,577
Last modified:November 1, 1997 - v1
Checksum:iC09772EB85A6A8DA
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AE000511 Genomic DNA. Translation: AAD08340.1.
PIRiC64682.
RefSeqiNP_208091.1. NC_000915.1.
YP_006935220.1. NC_018939.1.

Genome annotation databases

EnsemblBacteriaiAAD08340; AAD08340; HP_1299.
GeneIDi13870507.
898824.
KEGGiheo:C694_06710.
hpy:HP1299.
PATRICi20593979. VBIHelPyl33062_1360.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AE000511 Genomic DNA. Translation: AAD08340.1 .
PIRi C64682.
RefSeqi NP_208091.1. NC_000915.1.
YP_006935220.1. NC_018939.1.

3D structure databases

ProteinModelPortali P56102.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

DIPi DIP-3487N.
IntActi P56102. 4 interactions.
MINTi MINT-173189.
STRINGi 85962.HP1299.

Protein family/group databases

MEROPSi M24.001.

Proteomic databases

PRIDEi P56102.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblBacteriai AAD08340 ; AAD08340 ; HP_1299 .
GeneIDi 13870507.
898824.
KEGGi heo:C694_06710.
hpy:HP1299.
PATRICi 20593979. VBIHelPyl33062_1360.

Phylogenomic databases

eggNOGi COG0024.
KOi K01265.
OMAi PAFLGYM.
OrthoDBi EOG6MWNDS.

Enzyme and pathway databases

BioCyci HPY:HP1299-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

  1. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: ATCC 700392 / 26695.

Entry informationi

Entry nameiMAP1_HELPY
AccessioniPrimary (citable) accession number: P56102
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: November 1, 1997
Last modified: October 1, 2014
This is version 100 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. Helicobacter pylori
    Helicobacter pylori (strain 26695): entries and gene names
  2. Peptidase families
    Classification of peptidase families and list of entries
  3. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3