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Q10730 (AMPN_LACHE) Reviewed, UniProtKB/Swiss-Prot

Last modified September 18, 2013. Version 76. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Aminopeptidase N

EC=3.4.11.2
Alternative name(s):
Alanine aminopeptidase
Lysyl aminopeptidase
Short name=Lys-AP
Gene names
Name:pepN
OrganismLactobacillus helveticus (Lactobacillus suntoryeus)
Taxonomic identifier1587 [NCBI]
Taxonomic lineageBacteriaFirmicutesBacilliLactobacillalesLactobacillaceaeLactobacillus

Protein attributes

Sequence length844 AA.
Sequence statusComplete.
Protein existenceInferred from homology

General annotation (Comments)

Function

Aminopeptidase N is involved in the degradation of intracellular peptides generated by protein breakdown during normal growth as well as in response to nutrient starvation By similarity.

Catalytic activity

Release of an N-terminal amino acid, Xaa-|-Yaa- from a peptide, amide or arylamide. Xaa is preferably Ala, but may be most amino acids including Pro (slow action). When a terminal hydrophobic residue is followed by a prolyl residue, the two may be released as an intact Xaa-Pro dipeptide.

Cofactor

Binds 1 zinc ion per subunit By similarity.

Subunit structure

Monomer By similarity.

Subcellular location

Cytoplasm.

Sequence similarities

Belongs to the peptidase M1 family.

Ontologies

Keywords
   Cellular componentCytoplasm
   LigandMetal-binding
Zinc
   Molecular functionAminopeptidase
Hydrolase
Metalloprotease
Protease
Gene Ontology (GO)
   Biological_processproteolysis

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular_componentcytoplasm

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular_functionaminopeptidase activity

Inferred from electronic annotation. Source: UniProtKB-KW

metallopeptidase activity

Inferred from electronic annotation. Source: UniProtKB-KW

zinc ion binding

Inferred from electronic annotation. Source: InterPro

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 844844Aminopeptidase N
PRO_0000095072

Regions

Region253 – 2575Substrate binding By similarity

Sites

Active site2901Proton acceptor By similarity
Metal binding2891Zinc; catalytic By similarity
Metal binding2931Zinc; catalytic By similarity
Metal binding3121Zinc; catalytic By similarity
Binding site1201Substrate By similarity
Site3761Transition state stabilizer By similarity

Natural variations

Natural variant391F → I in strain: 53/7.
Natural variant441L → F in strain: 53/7.
Natural variant3421S → A in strain: 53/7.
Natural variant4551K → R in strain: 53/7.
Natural variant4961S → N in strain: 53/7.
Natural variant5271H → L in strain: 53/7.

Sequences

Sequence LengthMass (Da)Tools
Q10730 [UniParc].

Last modified October 1, 1996. Version 1.
Checksum: 1EA5DE6AC69410F4

FASTA84495,838
        10         20         30         40         50         60 
MAVKRFYKTF HPEHYDLRIN VNRKNKTING TSTITGDVFE NPVLINQKFM TIDSVKVDGK 

        70         80         90        100        110        120 
NVDFDVIEKD EAIKIKTGVT GKAVIEIAYS APLTDTMMGI YPSYYELEGK KKQIIGTQFE 

       130        140        150        160        170        180 
TTFARQAFPC VDEPEAKATF SLALKWDEQD GEVALANMPE VEVDKDGYHH FEETVRMSSY 

       190        200        210        220        230        240 
LVAFAFGELQ SKTTHTKDGV LIGVYATKAH KPKELDFALD IAKRAIEFYE EFYQTKYPLP 

       250        260        270        280        290        300 
QSLQLALPDF SAGAMENWGL VTYREAYLLL DPDNTSLEMK KLVATVITHE LAHQWFGDLV 

       310        320        330        340        350        360 
TMKWWDNLWL NESFANMMEY LSVDGLEPDW HIWEMFQTSE ASSALNRDAT DGVQPIQMEI 

       370        380        390        400        410        420 
NDPADIDSVF DSAIVYAKGS RMLVMVRSLL GDDALRKGLK YYFDHHKFGN ATGDDLWDAL 

       430        440        450        460        470        480 
STATDLDIGK IMHSWLKQPG YPVVNAFVAE DGHLKLTQKQ FFIGEGEDKG RQWQIPLNAN 

       490        500        510        520        530        540 
FDAPKIMSDK EIDLGSYKVL REEAGHPLRL NVGNNSHFIV EYDKTLHDDI LSDVNELDPI 

       550        560        570        580        590        600 
DKLQLLQDLR LLAEGKQISY ASIVPLLVKF ADSKSSLVIN ALYTTAAKLR QFVEPESNEE 

       610        620        630        640        650        660 
KNLKKLYDLL SKDQVARLGW EVKPGESDED VQIRPYELSA SLYAENADSI KAAHQIFTEN 

       670        680        690        700        710        720 
EDNLEALNAD IRPYVLINEV KNFGNAELVD KLIKEYQRTA DPSYKVDLRS AVTSTKDLAA 

       730        740        750        760        770        780 
IKAIVGDFEN ADVVKPQDLC DWYRGLLANH YGQQAAWDWI REDWDWLDKT VGGDMEFAKF 

       790        800        810        820        830        840 
ITVTAGVFHT PERLKEFKEF FEPKINVPLL SREIKMDVKV IESKVNLIEA EKDAVNDAVA 


KAID 

« Hide

References

[1]"Sequence analysis, distribution and expression of an aminopeptidase N-encoding gene from Lactobacillus helveticus CNRZ32."
Christensen J.E., Lin D.-L., Palva A., Steele J.L.
Gene 155:89-93(1995) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: CNRZ 32.
[2]"Characterization and expression of the pepN gene encoding a general aminopeptidase from Lactobacillus helveticus."
Varmanen P., Vesanto E., Steele J.L., Palva A.
FEMS Microbiol. Lett. 124:315-320(1994) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: 53/7.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
U08224 Genomic DNA. Translation: AAA81951.1.
Z30323 Genomic DNA. Translation: CAA82978.1.
PIRJC4054.
S47274.

3D structure databases

ProteinModelPortalQ10730.
ModBaseSearch...
MobiDBSearch...

Protein family/group databases

MEROPSM01.002.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Family and domain databases

InterProIPR024571. ERAP1-like_C_dom.
IPR001930. Peptidase_M1.
IPR014782. Peptidase_M1_N.
[Graphical view]
PANTHERPTHR11533. PTHR11533. 1 hit.
PfamPF11838. ERAP1_C. 1 hit.
PF01433. Peptidase_M1. 1 hit.
[Graphical view]
PRINTSPR00756. ALADIPTASE.
PROSITEPS00142. ZINC_PROTEASE. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameAMPN_LACHE
AccessionPrimary (citable) accession number: Q10730
Entry history
Integrated into UniProtKB/Swiss-Prot: October 1, 1996
Last sequence update: October 1, 1996
Last modified: September 18, 2013
This is version 76 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

Peptidase families

Classification of peptidase families and list of entries