Q10730 (AMPN_LACHE) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Aminopeptidase N
EC=3.4.11.2

Alternative name(s):
Alanine aminopeptidase
Lysyl aminopeptidase
Short name=Lys-AP

Gene names

Name:

pepN

Organism

Lactobacillus helveticus (Lactobacillus suntoryeus)

Taxonomic identifier

1587 [NCBI]

Taxonomic lineage

Bacteria › Firmicutes › Lactobacillales › Lactobacillaceae › Lactobacillus

Protein attributes

Sequence length	844 AA.
Sequence status	Complete.
Protein existence	Inferred 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 component	Cytoplasm
Ligand	Metal-binding Zinc
Molecular function	Aminopeptidase Hydrolase Metalloprotease Protease
Gene Ontology (GO)
Biological process	proteolysis Inferred from electronic annotation. Source: UniProtKB-KW
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: InterPro
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 844	844	Aminopeptidase N		PRO_0000095072
Regions
	Region	253 – 257	5	Substrate binding By similarity
Sites
	Active site	290	1	Proton acceptor By similarity
	Metal binding	289	1	Zinc; catalytic By similarity
	Metal binding	293	1	Zinc; catalytic By similarity
	Metal binding	312	1	Zinc; catalytic By similarity
	Binding site	120	1	Substrate By similarity
	Site	376	1	Transition state stabilizer By similarity
Natural variations
	Natural variant	39	1	F → I in strain: 53/7.
	Natural variant	44	1	L → F in strain: 53/7.
	Natural variant	342	1	S → A in strain: 53/7.
	Natural variant	455	1	K → R in strain: 53/7.
	Natural variant	496	1	S → N in strain: 53/7.
	Natural variant	527	1	H → L in strain: 53/7.

Sequences

	Sequence		Length	Mass (Da)
	Q10730 [UniParc]. Last modified October 1, 1996. Version 1. Checksum: 1EA5DE6AC69410F4	FASTA	844	95,838
	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

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: 7698673] [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: 7851738] [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.
PIR	JC4054. S47274.
3D structure databases
ProteinModelPortal	Q10730.
ModBase	Search...
Protein family/group databases
MEROPS	M01.002.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
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_LACHE

Accession

Primary (citable) accession number: Q10730

Entry history

Integrated into UniProtKB/Swiss-Prot:	October 1, 1996
Last sequence update:	October 1, 1996
Last modified:	November 16, 2011
This is version 66 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program