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Q10730

- AMPN_LACHE

UniProt

Q10730 - AMPN_LACHE

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Protein

Aminopeptidase N

Gene
pepN
Organism
Lactobacillus helveticus (Lactobacillus suntoryeus)
Status
Reviewed - Annotation score: 4 out of 5 - Protein inferred from homologyi

Functioni

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 activityi

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.

Cofactori

Binds 1 zinc ion per subunit By similarity.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei120 – 1201Substrate By similarity
Metal bindingi289 – 2891Zinc; catalytic By similarity
Active sitei290 – 2901Proton acceptor By similarity
Metal bindingi293 – 2931Zinc; catalytic By similarity
Metal bindingi312 – 3121Zinc; catalytic By similarity
Sitei376 – 3761Transition state stabilizer By similarity

GO - Molecular functioni

  1. aminopeptidase activity Source: UniProtKB-KW
  2. metallopeptidase activity Source: UniProtKB-KW
  3. zinc ion binding Source: InterPro
Complete GO annotation...

Keywords - Molecular functioni

Aminopeptidase, Hydrolase, Metalloprotease, Protease

Keywords - Ligandi

Metal-binding, Zinc

Protein family/group databases

MEROPSiM01.002.

Names & Taxonomyi

Protein namesi
Recommended name:
Aminopeptidase N (EC:3.4.11.2)
Alternative name(s):
Alanine aminopeptidase
Lysyl aminopeptidase
Short name:
Lys-AP
Gene namesi
Name:pepN
OrganismiLactobacillus helveticus (Lactobacillus suntoryeus)
Taxonomic identifieri1587 [NCBI]
Taxonomic lineageiBacteriaFirmicutesBacilliLactobacillalesLactobacillaceaeLactobacillus

Subcellular locationi

GO - Cellular componenti

  1. cytoplasm Source: UniProtKB-SubCell
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 844844Aminopeptidase NPRO_0000095072Add
BLAST

Interactioni

Subunit structurei

Monomer By similarity.

Structurei

3D structure databases

ProteinModelPortaliQ10730.

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni253 – 2575Substrate binding By similarity

Sequence similaritiesi

Belongs to the peptidase M1 family.

Family and domain databases

InterProiIPR024571. ERAP1-like_C_dom.
IPR001930. Peptidase_M1.
IPR014782. Peptidase_M1_N.
[Graphical view]
PANTHERiPTHR11533. PTHR11533. 1 hit.
PfamiPF11838. ERAP1_C. 1 hit.
PF01433. Peptidase_M1. 1 hit.
[Graphical view]
PRINTSiPR00756. ALADIPTASE.
PROSITEiPS00142. ZINC_PROTEASE. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q10730-1 [UniParc]FASTAAdd to Basket

« Hide

MAVKRFYKTF HPEHYDLRIN VNRKNKTING TSTITGDVFE NPVLINQKFM    50
TIDSVKVDGK NVDFDVIEKD EAIKIKTGVT GKAVIEIAYS APLTDTMMGI 100
YPSYYELEGK KKQIIGTQFE TTFARQAFPC VDEPEAKATF SLALKWDEQD 150
GEVALANMPE VEVDKDGYHH FEETVRMSSY LVAFAFGELQ SKTTHTKDGV 200
LIGVYATKAH KPKELDFALD IAKRAIEFYE EFYQTKYPLP QSLQLALPDF 250
SAGAMENWGL VTYREAYLLL DPDNTSLEMK KLVATVITHE LAHQWFGDLV 300
TMKWWDNLWL NESFANMMEY LSVDGLEPDW HIWEMFQTSE ASSALNRDAT 350
DGVQPIQMEI NDPADIDSVF DSAIVYAKGS RMLVMVRSLL GDDALRKGLK 400
YYFDHHKFGN ATGDDLWDAL STATDLDIGK IMHSWLKQPG YPVVNAFVAE 450
DGHLKLTQKQ FFIGEGEDKG RQWQIPLNAN FDAPKIMSDK EIDLGSYKVL 500
REEAGHPLRL NVGNNSHFIV EYDKTLHDDI LSDVNELDPI DKLQLLQDLR 550
LLAEGKQISY ASIVPLLVKF ADSKSSLVIN ALYTTAAKLR QFVEPESNEE 600
KNLKKLYDLL SKDQVARLGW EVKPGESDED VQIRPYELSA SLYAENADSI 650
KAAHQIFTEN EDNLEALNAD IRPYVLINEV KNFGNAELVD KLIKEYQRTA 700
DPSYKVDLRS AVTSTKDLAA IKAIVGDFEN ADVVKPQDLC DWYRGLLANH 750
YGQQAAWDWI REDWDWLDKT VGGDMEFAKF ITVTAGVFHT PERLKEFKEF 800
FEPKINVPLL SREIKMDVKV IESKVNLIEA EKDAVNDAVA KAID 844
Length:844
Mass (Da):95,838
Last modified:October 1, 1996 - v1
Checksum:i1EA5DE6AC69410F4
GO

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti39 – 391F → I in strain: 53/7.
Natural varianti44 – 441L → F in strain: 53/7.
Natural varianti342 – 3421S → A in strain: 53/7.
Natural varianti455 – 4551K → R in strain: 53/7.
Natural varianti496 – 4961S → N in strain: 53/7.
Natural varianti527 – 5271H → L in strain: 53/7.

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
U08224 Genomic DNA. Translation: AAA81951.1.
Z30323 Genomic DNA. Translation: CAA82978.1.
PIRiJC4054.
S47274.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
U08224 Genomic DNA. Translation: AAA81951.1 .
Z30323 Genomic DNA. Translation: CAA82978.1 .
PIRi JC4054.
S47274.

3D structure databases

ProteinModelPortali Q10730.
ModBasei Search...
MobiDBi Search...

Protein family/group databases

MEROPSi M01.002.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Family and domain databases

InterProi IPR024571. ERAP1-like_C_dom.
IPR001930. Peptidase_M1.
IPR014782. Peptidase_M1_N.
[Graphical view ]
PANTHERi PTHR11533. PTHR11533. 1 hit.
Pfami PF11838. ERAP1_C. 1 hit.
PF01433. Peptidase_M1. 1 hit.
[Graphical view ]
PRINTSi PR00756. ALADIPTASE.
PROSITEi PS00142. ZINC_PROTEASE. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

  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.

Entry informationi

Entry nameiAMPN_LACHE
AccessioniPrimary (citable) accession number: Q10730
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 1, 1996
Last sequence update: October 1, 1996
Last modified: June 11, 2014
This is version 78 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

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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