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Q5HN46

- MAP1_STAEQ

UniProt

Q5HN46 - MAP1_STAEQ

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Protein

Methionine aminopeptidase

Gene

map

Organism
Staphylococcus epidermidis (strain ATCC 35984 / RP62A)
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 sitei76 – 761SubstrateUniRule annotation
Metal bindingi93 – 931Divalent metal cation 1UniRule annotation
Metal bindingi104 – 1041Divalent metal cation 1UniRule annotation
Metal bindingi104 – 1041Divalent metal cation 2; catalyticUniRule annotation
Metal bindingi168 – 1681Divalent metal cation 2; catalytic; via tele nitrogenUniRule annotation
Binding sitei175 – 1751SubstrateUniRule 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

BioCyciRETL1328306-WGS:GSTH-3162-MONOMER.
SEPI176279:GJJB-1490-MONOMER.

Protein family/group databases

MEROPSiM24.036.

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:SERP1426
OrganismiStaphylococcus epidermidis (strain ATCC 35984 / RP62A)
Taxonomic identifieri176279 [NCBI]
Taxonomic lineageiBacteriaFirmicutesBacilliBacillalesStaphylococcus
ProteomesiUP000000531: Chromosome

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 251251Methionine aminopeptidasePRO_0000148962Add
BLAST

Interactioni

Subunit structurei

Monomer.UniRule annotation

Protein-protein interaction databases

STRINGi176279.SERP1426.

Structurei

3D structure databases

ProteinModelPortaliQ5HN46.
SMRiQ5HN46. Positions 1-249.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

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

Phylogenomic databases

eggNOGiCOG0024.
HOGENOMiHOG000030426.
KOiK01265.
OMAiEGMCFTI.
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.

Sequencei

Sequence statusi: Complete.

Q5HN46-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MIVKTDEELQ ALKEIGYICA KVRDTMKEAT KPGVTTRELD HIAKDLFEEH
60 70 80 90 100
GAISAPIHDE NFPGQTCISV NEEVAHGIPG KRVIHEGDLV NIDVSALKNG
110 120 130 140 150
YYADTGISFV VGKSDQPLKQ KVCDVATMAF ENAMKKVKPG TKLSNIGKAV
160 170 180 190 200
HATARQNDLT VIKNLTGHGV GQSLHEAPNH VMNYFDPKDK TLLKEGQVIA
210 220 230 240 250
VEPFISTHAT FVTEGKNEWA FETKDKSYVA QIEHTVIVTK DGPLLTTKID

D
Length:251
Mass (Da):27,531
Last modified:February 15, 2005 - v1
Checksum:iA105F719EC8571E5
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
CP000029 Genomic DNA. Translation: AAW54790.1.
RefSeqiYP_188995.1. NC_002976.3.

Genome annotation databases

EnsemblBacteriaiAAW54790; AAW54790; SERP1426.
GeneIDi3241924.
KEGGiser:SERP1426.
PATRICi19613781. VBIStaEpi130894_1394.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
CP000029 Genomic DNA. Translation: AAW54790.1 .
RefSeqi YP_188995.1. NC_002976.3.

3D structure databases

ProteinModelPortali Q5HN46.
SMRi Q5HN46. Positions 1-249.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

STRINGi 176279.SERP1426.

Protein family/group databases

MEROPSi M24.036.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblBacteriai AAW54790 ; AAW54790 ; SERP1426 .
GeneIDi 3241924.
KEGGi ser:SERP1426.
PATRICi 19613781. VBIStaEpi130894_1394.

Phylogenomic databases

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

Enzyme and pathway databases

BioCyci RETL1328306-WGS:GSTH-3162-MONOMER.
SEPI176279:GJJB-1490-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.
ProtoNeti Search...

Publicationsi

  1. "Insights on evolution of virulence and resistance from the complete genome analysis of an early methicillin-resistant Staphylococcus aureus strain and a biofilm-producing methicillin-resistant Staphylococcus epidermidis strain."
    Gill S.R., Fouts D.E., Archer G.L., Mongodin E.F., DeBoy R.T., Ravel J., Paulsen I.T., Kolonay J.F., Brinkac L.M., Beanan M.J., Dodson R.J., Daugherty S.C., Madupu R., Angiuoli S.V., Durkin A.S., Haft D.H., Vamathevan J.J., Khouri H.
    , Utterback T.R., Lee C., Dimitrov G., Jiang L., Qin H., Weidman J., Tran K., Kang K.H., Hance I.R., Nelson K.E., Fraser C.M.
    J. Bacteriol. 187:2426-2438(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: ATCC 35984 / RP62A.

Entry informationi

Entry nameiMAP1_STAEQ
AccessioniPrimary (citable) accession number: Q5HN46
Entry historyi
Integrated into UniProtKB/Swiss-Prot: December 6, 2005
Last sequence update: February 15, 2005
Last modified: October 1, 2014
This is version 72 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. Peptidase families
    Classification of peptidase families and list of entries
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3