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Protein

Aminopeptidase N

Gene

pepN

Organism
Lactococcus lactis subsp. cremoris (strain MG1363)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

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 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

Zn2+By similarityNote: Binds 1 zinc ion per subunit.By similarity

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Binding sitei120SubstrateBy similarity1
Metal bindingi288Zinc; catalyticPROSITE-ProRule annotation1
Active sitei289Proton acceptorPROSITE-ProRule annotation1
Metal bindingi292Zinc; catalyticPROSITE-ProRule annotation1
Metal bindingi311Zinc; catalyticPROSITE-ProRule annotation1
Sitei375Transition state stabilizerBy similarity1

GO - Molecular functioni

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
Synonyms:lap
Ordered Locus Names:llmg_0319
OrganismiLactococcus lactis subsp. cremoris (strain MG1363)
Taxonomic identifieri416870 [NCBI]
Taxonomic lineageiBacteriaFirmicutesBacilliLactobacillalesStreptococcaceaeLactococcus
Proteomesi
  • UP000000364 Componenti: Chromosome

Subcellular locationi

  • Cytoplasm

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

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Initiator methionineiRemoved1 Publication
ChainiPRO_00002852372 – 846Aminopeptidase NAdd BLAST845

Interactioni

Subunit structurei

Monomer.

Protein-protein interaction databases

STRINGi416870.llmg_0319.

Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni252 – 256Substrate bindingBy similarity5

Sequence similaritiesi

Belongs to the peptidase M1 family.Curated

Phylogenomic databases

eggNOGiENOG4105CD8. Bacteria.
COG0308. LUCA.
HOGENOMiHOG000235375.
KOiK01256.
OMAiEAMTQRK.

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.

Sequence processingi: The displayed sequence is further processed into a mature form.

A2RI32-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MAVKRLIETF VPENYKIFLD IDRKTKKIKG QVAITGEAKD TVVSFHTKGL
60 70 80 90 100
HFNKVRAFSV DTNFIENEED EEIVVKIGET GRVTVSFEYE AELTDNMMGI
110 120 130 140 150
YPSYYEVNGE KKMLIGTQFE SHFARQAFPS IDEPEAKATF DLSVKFDEEE
160 170 180 190 200
GDIIVSNMPE LLNINGIHVF ERTVKMSSYL LAFVFGELQY KKGKTKSGVE
210 220 230 240 250
VGAFATKAHS QAALDFPLDI AIRSIEFYED YYQTPYPLPH SWHIALPDFS
260 270 280 290 300
AGAMENWGCI TYREVCMLVD PENATIQSKQ YVATVIAHEL AHQWFGDLVT
310 320 330 340 350
MQWWDDLWLN ESFANNMEYV CMDALEPSWN VWESFSISEA NMALNRDATD
360 370 380 390 400
GVQSVHVEVT HPDEIGTLFD PAIVYAKGSR LMVMLRKWLG DEDFAAGLAL
410 420 430 440 450
YFKRHQYGNT VGDNLWDALA EVSGKDVAAF MHSWVNQPGY PVVTAEVVDD
460 470 480 490 500
TLILSQKQFF VGEGVDKGRL WNVPLNTNWT GLPDLLSSEK VEIPGFAALK
510 520 530 540 550
TKNNGKALFL NDANMAHYII DYKGALLTDL LSEVESLENV TKFQILQDRK
560 570 580 590 600
LLAKAGVISY ADVVNILPSF TNEESYLVNT GLSQLISELE LFVDEDSETE
610 620 630 640 650
KAFQSLVGKL FAKNYARLGW DKVAGESAGD ESLRGIVLSK TLYSENADAK
660 670 680 690 700
TKASQIFAAH KENLASIPAD IRPIVLNNEI KTTNSAELVK TYRETYIKTS
710 720 730 740 750
LQEFKRELEG AVALIKDEKV IAELLESFKN ADIVKPQDIA FSWFYLLRND
760 770 780 790 800
FSQDAAWAWE KANWAFLEEK LGGDMSYDKF VIYPGNTFKT ADKLAEYKAF
810 820 830 840
FEPKLENQGL KRSIEMAIKQ ITARVALIDS QKAAVDKAIT DIAEKL
Length:846
Mass (Da):95,369
Last modified:March 6, 2007 - v1
Checksum:i3288DB1A43DBDEF8
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M87840 Genomic DNA. Translation: AAA25205.1.
S39955 Genomic DNA. Translation: AAB22460.1.
AM406671 Genomic DNA. Translation: CAL96925.1.
M65867 Genomic DNA. Translation: AAA25162.1.
PIRiS23157.
RefSeqiWP_011834382.1. NC_009004.1.

Genome annotation databases

EnsemblBacteriaiCAL96925; CAL96925; llmg_0319.
KEGGillm:llmg_0319.
PATRICi22281679. VBILacLac4574_0328.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M87840 Genomic DNA. Translation: AAA25205.1.
S39955 Genomic DNA. Translation: AAB22460.1.
AM406671 Genomic DNA. Translation: CAL96925.1.
M65867 Genomic DNA. Translation: AAA25162.1.
PIRiS23157.
RefSeqiWP_011834382.1. NC_009004.1.

3D structure databases

ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi416870.llmg_0319.

Protein family/group databases

MEROPSiM01.002.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiCAL96925; CAL96925; llmg_0319.
KEGGillm:llmg_0319.
PATRICi22281679. VBILacLac4574_0328.

Phylogenomic databases

eggNOGiENOG4105CD8. Bacteria.
COG0308. LUCA.
HOGENOMiHOG000235375.
KOiK01256.
OMAiEAMTQRK.

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]
ProtoNetiSearch...

Entry informationi

Entry nameiAMPN_LACLM
AccessioniPrimary (citable) accession number: A2RI32
Secondary accession number(s): P37897
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 1, 2007
Last sequence update: March 6, 2007
Last modified: November 2, 2016
This is version 59 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Direct protein sequencing

Documents

  1. Peptidase families
    Classification of peptidase families and list of entries
  2. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.