Reviewed, UniProtKB/Swiss-Prot P37896 (AMPN_LACDL)

Names and origin

Protein names

Recommended name:
    Aminopeptidase N
    EC=3.4.11.2
Alternative name(s):
    Lysyl aminopeptidase
      Short name=Lys-AP
    Alanine aminopeptidase

Gene names

Name:

pepN

Organism

Lactobacillus delbrueckii subsp. lactis

Taxonomic identifier

29397 [NCBI]

Taxonomic lineage

Bacteria › Firmicutes › Lactobacillales › Lactobacillaceae › Lactobacillus

Protein attributes

Sequence length	843 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level.

General annotation (Comments)

Function	Aminopeptidase with broad substrate specificity to several peptides.
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. Note: It may be secreted through an unknown mechanism.
Sequence similarities	Belongs to the peptidase M1 family.
Biophysicochemical properties	pH dependence: Optimum pH is 6.5-7.0. Temperature dependence: Optimum temperature is 54-55 degrees Celsius.

Ontologies

Keywords
Cellular component	Cytoplasm
Ligand	Metal-binding Zinc
Molecular function	Aminopeptidase Hydrolase Metalloprotease Protease
Gene Ontology (GO)
Biological process	proteolysis Inferred from electronic annotation. Source: InterPro
Cellular component	cytoplasm Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular function	aminopeptidase 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: UniProtKB-KW
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Initiator methionine	1	1	Removed By similarity
	Chain	2 – 843	842	Aminopeptidase N		PRO_0000095071
Sites
	Active site	289	1	By similarity
	Active site	375	1	Proton donor Potential
	Metal binding	288	1	Zinc; catalytic By similarity
	Metal binding	292	1	Zinc; catalytic By similarity
	Metal binding	311	1	Zinc; catalytic By similarity

Sequences

	Sequence		Length	Mass (Da)
	P37896-1 [UniParc]. Last modified January 23, 2007. Version 3. Checksum: 08EF9F8CBD7AB1B0	FASTA	843	95,348
	10 20 30 40 50 60 MAVKRFYETF HPDHYDLYID VDRAARSFSG TSTIHGEIQE ETVLVHQKYM TISKVTVDGK 70 80 90 100 110 120 EVPFTFGDDF EGIKIEAGKT GEAVIAIDYS APLTDTMMGI YPSYYQVDGV KKELIGTQFE 130 140 150 160 170 180 TTFAREAFPC VDEPEAKATF SLALKFDEHE GETVLANMPE DRVENGVHYF KETVRMSSYL 190 200 210 220 230 240 VAFAFGEMRS LTTHTKSGVL IGVYSTQAHT EKELTFSLDI AKRAIEFYED FYQTPYPLPQ 250 260 270 280 290 300 SLQLALPDFS AGAMENWGLV TYREAYLLLD PDNTTLEMKK LVATVVTHEL AHQWFGDLVT 310 320 330 340 350 360 MEWWDNLWLN ESFANMMEYL SVDHLEPNWH IWEMFQTSEA AAALTRDATD GVQSVHVEVN 370 380 390 400 410 420 DPAEIDALFD GAIVYAKGSR MLVMVRSLLG DEALRKGLKR YFDKHKFGNA AGDDLWDALS 430 440 450 460 470 480 TATDLNIGEI MHTWLDQPGY PVVNAFVEDG HLKLTQKQFF IGEGKEVGRK WEIPLNANFK 490 500 510 520 530 540 APKIMSDVEL DLGDYQALRA EAGHALRLNV GNNSHFIVKY DQTLMDDIMK EAKDLDPVSQ 550 560 570 580 590 600 LQLLQDLRLL AEGKQASYAD VVPVLELFKN SESHIVNDAL YTTADKLRQF APAGSEADKN 610 620 630 640 650 660 LRALYNDLSK DQVARLGWLP KAGESDEDIQ TRPYVLSASL YGRNADSEKQ AHEIYVEYAD 670 680 690 700 710 720 KLAELSADIR PYVLINEVEN YGSSELTDKL IGLYQATSDP SFKMDLEAAI VKSKDEGELK 730 740 750 760 770 780 KIVSWFKNAE IVKPQDLRGW FSGVLSNPAG EQLAWDWIRD EWAWLEKTVG GDMEFATFIT 790 800 810 820 830 840 VISRVFKTKE RYDEYNAFFT DKESNMLLNR EIKMDRKVIA NRVDLIASEQ ADVNAAVAAA LQK

References

[1]

"Cloning, DNA sequence analysis and partial characterization of pepN, a lysyl aminopeptidase from Lactobacillus delbruckii ssp. lactis DSM7290." Klein J.R., Klein U., Schad M., Plapp R. Eur. J. Biochem. 217:105-114(1993) [PubMed: 8223547] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: DSM 7290.

Cross-references

Sequence databases
EMBL GenBank DDBJ	Z21701 Genomic DNA. Translation: CAA79805.1.
PIR	S38364.
3D structure databases
ModBase	Search...
Protein family/group databases
MEROPS	M01.002.
Enzyme and pathway databases
BRENDA	3.4.11.2. 270587.
Family and domain databases
InterPro	IPR001930. Peptidase_M1. IPR014782. Peptidase_M1_N. [Graphical view]
PANTHER	PTHR11533. Peptidase_M1. 1 hit.
Pfam	PF01433. Peptidase_M1. 1 hit. [Graphical view]
PRINTS	PR00756. ALADIPTASE.
PROSITE	PS00142. ZINC_PROTEASE. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

AMPN_LACDL

Accession

Primary (citable) accession number: P37896

Entry history

Integrated into UniProtKB/Swiss-Prot:	October 1, 1994
Last sequence update:	January 23, 2007
Last modified:	November 24, 2009
This is version 62 of the entry and version 3 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HAMAP (High-quality Automated and Manual Annotation of microbial Proteomes)