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Q48656 (AMPN_LACLL) Reviewed, UniProtKB/Swiss-Prot

Last modified May 14, 2014. Version 80. 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
OrganismLactococcus lactis subsp. lactis (Streptococcus lactis)
Taxonomic identifier1360 [NCBI]
Taxonomic lineageBacteriaFirmicutesBacilliLactobacillalesStreptococcaceaeLactococcus

Protein attributes

Sequence length849 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Aminopeptidase with broad substrate specificity to several peptides. It has more affinity for oligopeptides than for dipeptides. It plays an essential role in the metabolism, it may be involved in nitrogen supply or protein turnover.

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.

Subcellular location

Cytoplasm. Note: It may be secreted through an unknown mechanism.

Sequence similarities

Belongs to the peptidase M1 family.

Ontologies

Keywords
   Cellular componentCytoplasm
   LigandMetal-binding
Zinc
   Molecular functionAminopeptidase
Hydrolase
Metalloprotease
Protease
   Technical termDirect protein sequencing
Gene Ontology (GO)
   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

Initiator methionine11Removed
Chain2 – 849848Aminopeptidase N
PRO_0000095074

Regions

Region259 – 2635Substrate binding By similarity

Sites

Active site2951Proton acceptor By similarity
Metal binding2941Zinc; catalytic By similarity
Metal binding2981Zinc; catalytic By similarity
Metal binding3171Zinc; catalytic By similarity
Binding site1221Substrate By similarity
Site3821Transition state stabilizer By similarity

Sequences

Sequence LengthMass (Da)Tools
Q48656 [UniParc].

Last modified January 23, 2007. Version 2.
Checksum: E809F5437DFBD50F

FASTA84996,565
        10         20         30         40         50         60 
MTASVARFIE SFIPENYNLF LDINRSEKTF TGNVAITGEA IDNHISLHQK DLTINSVLLD 

        70         80         90        100        110        120 
NESLNFQMDD ANEAFHIELP ETGVLTIFIE FSGRITDNMT GIYPSYYTYN GEKKEIISTQ 

       130        140        150        160        170        180 
FEISHFAREA FPCVDEPEAK ATFDLSLKFD AEEGDTALSN MPEINSHLRE ETGVWTFETT 

       190        200        210        220        230        240 
PRMSTYLLAF GFGALHGKTA KTKNGTEVGV FATVAQAENS FDFALDIAVR VIEFYEDYFQ 

       250        260        270        280        290        300 
VKYPIPLSYH LALPDFSAGA MENWGLVTYR EVYLLVDENS SAASRQQVAL VVAHELAHQW 

       310        320        330        340        350        360 
FGNLVTMKWW DDLWLNESFA NMMEYVSVNA IEPSWNIFEG FPNKLGVPNA LQRDATDGVQ 

       370        380        390        400        410        420 
SVHMEVSHPD EINTLFDSAI VYAKGSRLMH MLRRWLGDEA FAKGLKAYFE KHQYNNTVGR 

       430        440        450        460        470        480 
DLWNALSEAS GKDVSSFMDT WLEQPGYPVV SAEVVDDTLI LSQKQFFIGE HEDKGRLWEI 

       490        500        510        520        530        540 
PLNTNWNGLP DTLSGERIEI PNYSQLATEN NGVLRLNTAN TAHYITDYQG QLLDNILEDF 

       550        560        570        580        590        600 
ANLDTVSKLQ ILQERRLLAE SGRISYASLV GLLDLVEKEE SFFLISQAKS QILAGLKRFI 

       610        620        630        640        650        660 
DEDTEAEVHY KALVRRQFQN DFERLGFDAK EGESDEDEMV RQTALSYLIE ADYQPTVLAA 

       670        680        690        700        710        720 
ANVFQAHKEN IESIPASIRG LVLINQMKQE NSLSLVEEYI NAYVATNDSN FRRQLTQALS 

       730        740        750        760        770        780 
YLKNQEGLDY VLGQLKDKNV VKPQDLYLWY MNFLSKSFAQ ETVWDWAKEN WEWIKAALGG 

       790        800        810        820        830        840 
DMSFDSFVNI PAGIFKNQER LDQYIAFFEP QTSDKALERN ILMGIKTIAA RVDLIEKEKA 


AVESALKDY 

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References

[1]"Cloning of lysyl-aminopeptidase gene from Lactococcus lactis."
Tsukasaki F., Motoshima H., Minagawa E., Kaminogawa S.
Submitted (APR-1996) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], PARTIAL PROTEIN SEQUENCE.
Strain: YRC001.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
D38040 Genomic DNA. Translation: BAA07234.1.
PIRJU0191.

3D structure databases

ProteinModelPortalQ48656.
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_LACLL
AccessionPrimary (citable) accession number: Q48656
Entry history
Integrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: January 23, 2007
Last modified: May 14, 2014
This is version 80 of the entry and version 2 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