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P0A1X6

- MAP1_SALTY

UniProt

P0A1X6 - MAP1_SALTY

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Protein
Methionine aminopeptidase
Gene
map, pepM, STM0215
Organism
Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720)
Status
Reviewed - Annotation score: 3 out of 5 - Experimental evidence at protein leveli

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.1 Publication

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 By similarity.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei79 – 791Substrate By similarity
Metal bindingi97 – 971Divalent metal cation 1 By similarity
Metal bindingi108 – 1081Divalent metal cation 1 By similarity
Metal bindingi108 – 1081Divalent metal cation 2; catalytic By similarity
Metal bindingi171 – 1711Divalent metal cation 2; catalytic; via tele nitrogen By similarity
Binding sitei178 – 1781Substrate By similarity
Metal bindingi204 – 2041Divalent metal cation 2; catalytic By similarity
Metal bindingi235 – 2351Divalent metal cation 1 By similarity
Metal bindingi235 – 2351Divalent metal cation 2; catalytic By similarity

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

BioCyciSENT99287:GCTI-214-MONOMER.

Names & Taxonomyi

Protein namesi
Recommended name:
Methionine aminopeptidase (EC:3.4.11.18)
Short name:
MAP
Short name:
MetAP
Alternative name(s):
Peptidase M
Gene namesi
Name:map
Synonyms:pepM
Ordered Locus Names:STM0215
OrganismiSalmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720)
Taxonomic identifieri99287 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeSalmonella
ProteomesiUP000001014: Chromosome

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11Removed1 Publication
Chaini2 – 264263Methionine aminopeptidaseUniRule annotation
PRO_0000148952Add
BLAST

Proteomic databases

PaxDbiP0A1X6.
PRIDEiP0A1X6.

Interactioni

Subunit structurei

Monomer By similarity.UniRule annotation

Protein-protein interaction databases

STRINGi99287.STM0215.

Structurei

3D structure databases

ProteinModelPortaliP0A1X6.
SMRiP0A1X6. Positions 2-264.

Family & Domainsi

Sequence similaritiesi

Phylogenomic databases

eggNOGiCOG0024.
HOGENOMiHOG000030427.
KOiK01265.
OMAiEGMCFTI.
OrthoDBiEOG6MWNDS.
PhylomeDBiP0A1X6.

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.

Sequence processingi: The displayed sequence is further processed into a mature form.

P0A1X6-1 [UniParc]FASTAAdd to Basket

« Hide

MAISIKTSED IEKMRVAGRL AAEVLEMIEP YIKPGVTTGE LDRICNDYIV    50
NEQHAISACL GYHGYPKSVC ISINEVVCHG IPDDAKHLKD GDIVNIDVTV 100
IKDEFHGDTS KMFIVGKPTI LGERLCRVTQ ESLYLGIKMV KPGIRLRTIG 150
AAIQKYAEGE GFSVVREYCG HGIGRGFHEE PQVLHYDADD GGVVLQPGMT 200
FTIEPMLNAG DYRIRTMKDG WTVKTKDRSL SAQYEHTIVV TENGCEILTL 250
RKDDTIPAII THDE 264
Length:264
Mass (Da):29,292
Last modified:January 23, 2007 - v2
Checksum:i8563A54BBE98A860
GO

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti136 – 1383GIK → ALR AA sequence 1 Publication
Sequence conflicti145 – 1451R → N AA sequence 1 Publication
Sequence conflicti148 – 1481T → E AA sequence 1 Publication
Sequence conflicti159 – 1591G → A AA sequence 1 Publication

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
X55778 Genomic DNA. Translation: CAA39298.1.
AE006468 Genomic DNA. Translation: AAL19179.1.
PIRiS12027.
RefSeqiNP_459220.1. NC_003197.1.

Genome annotation databases

EnsemblBacteriaiAAL19179; AAL19179; STM0215.
GeneIDi1251733.
KEGGistm:STM0215.
PATRICi32378717. VBISalEnt20916_0228.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
X55778 Genomic DNA. Translation: CAA39298.1 .
AE006468 Genomic DNA. Translation: AAL19179.1 .
PIRi S12027.
RefSeqi NP_459220.1. NC_003197.1.

3D structure databases

ProteinModelPortali P0A1X6.
SMRi P0A1X6. Positions 2-264.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

STRINGi 99287.STM0215.

Proteomic databases

PaxDbi P0A1X6.
PRIDEi P0A1X6.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblBacteriai AAL19179 ; AAL19179 ; STM0215 .
GeneIDi 1251733.
KEGGi stm:STM0215.
PATRICi 32378717. VBISalEnt20916_0228.

Phylogenomic databases

eggNOGi COG0024.
HOGENOMi HOG000030427.
KOi K01265.
OMAi EGMCFTI.
OrthoDBi EOG6MWNDS.
PhylomeDBi P0A1X6.

Enzyme and pathway databases

BioCyci SENT99287:GCTI-214-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. "Cloning and nucleotide sequence of the Salmonella typhimurium pepM gene."
    Movva N.R., Semon D., Meyer C., Kawashima E., Wingfield P., Miller J.L., Miller C.G.
    Mol. Gen. Genet. 223:345-348(1990) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: LT2.
  2. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: LT2 / SGSC1412 / ATCC 700720.
  3. "Purification and characterization of a methionine-specific aminopeptidase from Salmonella typhimurium."
    Wingfield P., Graber P., Turcatti G., Movva N.R., Pelletier M., Craig S., Rose K., Miller C.G.
    Eur. J. Biochem. 180:23-32(1989) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 2-264, FUNCTION.

Entry informationi

Entry nameiMAP1_SALTY
AccessioniPrimary (citable) accession number: P0A1X6
Secondary accession number(s): P10882
Entry historyi
Integrated into UniProtKB/Swiss-Prot: March 1, 2005
Last sequence update: January 23, 2007
Last modified: July 9, 2014
This is version 74 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, Direct protein sequencing, Reference 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

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