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Protein

Aminopeptidase N

Gene

pepN

Organism
Escherichia coli (strain K12)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

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.1 Publication3 Publications

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.3 Publications

Cofactori

Zn2+3 PublicationsNote: Binds 1 zinc ion per subunit.3 Publications

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Binding sitei121Substrate1
Metal bindingi297Zinc; catalytic1
Active sitei298Proton acceptor3 Publications1
Metal bindingi301Zinc; catalytic1
Metal bindingi320Zinc; catalytic1
Sitei381Transition state stabilizerCurated1

GO - Molecular functioni

GO - Biological processi

  • peptide catabolic process Source: EcoliWiki
  • proteolysis Source: EcoCyc
Complete GO annotation...

Keywords - Molecular functioni

Aminopeptidase, Hydrolase, Metalloprotease, Protease

Keywords - Ligandi

Metal-binding, Zinc

Enzyme and pathway databases

BioCyciEcoCyc:EG10696-MONOMER.
ECOL316407:JW0915-MONOMER.
MetaCyc:EG10696-MONOMER.
BRENDAi3.4.11.2. 2026.

Protein family/group databases

MEROPSiM01.005.

Names & Taxonomyi

Protein namesi
Recommended name:
Aminopeptidase N (EC:3.4.11.23 Publications)
Alternative name(s):
Alpha-aminoacylpeptide hydrolase
Gene namesi
Name:pepN
Ordered Locus Names:b0932, JW0915
OrganismiEscherichia coli (strain K12)
Taxonomic identifieri83333 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacteralesEnterobacteriaceaeEscherichia
Proteomesi
  • UP000000318 Componenti: Chromosome
  • UP000000625 Componenti: Chromosome

Organism-specific databases

EcoGeneiEG10696. pepN.

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cell inner membrane, Cell membrane, Membrane

Pathology & Biotechi

Disruption phenotypei

A quadruple peptidase disruption (pepA, pepB, pepD and pepN) does not grow in M9 minimal medium, does grow better when supplemented with casamino acids (PubMed:20067529).1 Publication

Chemistry databases

ChEMBLiCHEMBL4325.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Initiator methionineiRemoved1 Publication
ChainiPRO_00000950692 – 870Aminopeptidase NAdd BLAST869

Proteomic databases

EPDiP04825.
PaxDbiP04825.
PRIDEiP04825.

Interactioni

Binary interactionsi

WithEntry#Exp.IntActNotes
itself2EBI-545385,EBI-545385

Protein-protein interaction databases

BioGridi4261880. 12 interactors.
851583. 1 interactor.
DIPiDIP-10458N.
IntActiP04825. 13 interactors.
MINTiMINT-1310653.
STRINGi511145.b0932.

Chemistry databases

BindingDBiP04825.

Structurei

Secondary structure

1870
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi10 – 12Combined sources3
Beta strandi17 – 28Combined sources12
Beta strandi34 – 44Combined sources11
Beta strandi52 – 55Combined sources4
Beta strandi60 – 66Combined sources7
Beta strandi73 – 77Combined sources5
Beta strandi80 – 83Combined sources4
Beta strandi88 – 98Combined sources11
Helixi100 – 102Combined sources3
Beta strandi108 – 112Combined sources5
Beta strandi115 – 119Combined sources5
Turni121 – 124Combined sources4
Helixi125 – 127Combined sources3
Beta strandi129 – 131Combined sources3
Beta strandi139 – 148Combined sources10
Turni149 – 151Combined sources3
Beta strandi154 – 166Combined sources13
Helixi168 – 170Combined sources3
Beta strandi171 – 182Combined sources12
Helixi184 – 186Combined sources3
Beta strandi189 – 192Combined sources4
Beta strandi195 – 202Combined sources8
Beta strandi208 – 215Combined sources8
Helixi220 – 222Combined sources3
Helixi224 – 241Combined sources18
Beta strandi247 – 256Combined sources10
Beta strandi259 – 263Combined sources5
Beta strandi268 – 272Combined sources5
Helixi273 – 275Combined sources3
Turni280 – 282Combined sources3
Helixi285 – 300Combined sources16
Turni301 – 303Combined sources3
Turni305 – 307Combined sources3
Beta strandi308 – 312Combined sources5
Helixi313 – 315Combined sources3
Helixi316 – 334Combined sources19
Helixi337 – 350Combined sources14
Helixi352 – 356Combined sources5
Beta strandi367 – 370Combined sources4
Helixi372 – 375Combined sources4
Helixi378 – 411Combined sources34
Beta strandi414 – 416Combined sources3
Helixi418 – 429Combined sources12
Turni434 – 437Combined sources4
Helixi438 – 441Combined sources4
Beta strandi447 – 455Combined sources9
Turni456 – 459Combined sources4
Beta strandi460 – 468Combined sources9
Beta strandi483 – 490Combined sources8
Beta strandi500 – 505Combined sources6
Beta strandi508 – 512Combined sources5
Beta strandi514 – 521Combined sources8
Beta strandi529 – 533Combined sources5
Helixi534 – 536Combined sources3
Beta strandi541 – 543Combined sources3
Helixi548 – 557Combined sources10
Helixi561 – 584Combined sources24
Helixi593 – 604Combined sources12
Beta strandi606 – 608Combined sources3
Helixi610 – 616Combined sources7
Helixi622 – 626Combined sources5
Helixi634 – 651Combined sources18
Helixi653 – 662Combined sources10
Helixi672 – 689Combined sources18
Helixi693 – 706Combined sources14
Helixi710 – 722Combined sources13
Helixi728 – 739Combined sources12
Helixi743 – 754Combined sources12
Helixi761 – 768Combined sources8
Helixi779 – 792Combined sources14
Helixi794 – 797Combined sources4
Helixi803 – 818Combined sources16
Helixi820 – 831Combined sources12
Helixi832 – 835Combined sources4
Helixi838 – 852Combined sources15
Helixi859 – 869Combined sources11

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
2DQ6X-ray1.50A1-870[»]
2DQMX-ray1.60A1-870[»]
2HPOX-ray1.65A1-870[»]
2HPTX-ray2.30A1-870[»]
2ZXGX-ray1.55A1-870[»]
3B2PX-ray2.00A1-870[»]
3B2XX-ray1.50A1-870[»]
3B34X-ray1.30A1-870[»]
3B37X-ray1.70A1-870[»]
3B3BX-ray1.85A1-870[»]
3KEDX-ray2.30A1-870[»]
3PUUX-ray2.15A1-870[»]
3QJXX-ray1.45A1-870[»]
4Q4EX-ray1.90A1-870[»]
4Q4IX-ray2.31A1-870[»]
4XMTX-ray2.00A4-870[»]
4XMUX-ray2.91A5-870[»]
4XMVX-ray2.92A5-870[»]
4XMWX-ray2.20A4-870[»]
4XMXX-ray2.30A5-870[»]
4XMZX-ray2.15A4-870[»]
4XN1X-ray2.20A4-870[»]
4XN2X-ray2.11A5-870[»]
4XN4X-ray1.99A5-870[»]
4XN5X-ray2.66A5-870[»]
4XN7X-ray2.22A5-870[»]
4XN8X-ray1.89A5-870[»]
4XN9X-ray2.80A5-870[»]
4XNAX-ray2.40A5-870[»]
4XNBX-ray1.95A5-870[»]
4XNDX-ray1.93A5-870[»]
4XO3X-ray2.00A5-870[»]
4XO4X-ray2.18A1-870[»]
4XO5X-ray1.98A5-870[»]
ProteinModelPortaliP04825.
SMRiP04825.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP04825.

Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni261 – 265Substrate binding5

Sequence similaritiesi

Belongs to the peptidase M1 family.Curated

Phylogenomic databases

eggNOGiENOG4105CD8. Bacteria.
COG0308. LUCA.
HOGENOMiHOG000257670.
InParanoidiP04825.
KOiK01256.
OMAiMIVAVND.
PhylomeDBiP04825.

Family and domain databases

CDDicd09600. M1_APN_1. 1 hit.
Gene3Di1.25.50.10. 1 hit.
InterProiIPR001930. Peptidase_M1.
IPR014782. Peptidase_M1_N.
IPR012779. Peptidase_M1_pepN.
IPR024601. Peptidase_M1_pepN_C.
[Graphical view]
PANTHERiPTHR11533. PTHR11533. 2 hits.
PfamiPF11940. DUF3458. 1 hit.
PF01433. Peptidase_M1. 1 hit.
[Graphical view]
PRINTSiPR00756. ALADIPTASE.
TIGRFAMsiTIGR02414. pepN_proteo. 1 hit.
PROSITEiPS00142. ZINC_PROTEASE. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

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

P04825-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MTQQPQAKYR HDYRAPDYQI TDIDLTFDLD AQKTVVTAVS QAVRHGASDA
60 70 80 90 100
PLRLNGEDLK LVSVHINDEP WTAWKEEEGA LVISNLPERF TLKIINEISP
110 120 130 140 150
AANTALEGLY QSGDALCTQC EAEGFRHITY YLDRPDVLAR FTTKIIADKI
160 170 180 190 200
KYPFLLSNGN RVAQGELENG RHWVQWQDPF PKPCYLFALV AGDFDVLRDT
210 220 230 240 250
FTTRSGREVA LELYVDRGNL DRAPWAMTSL KNSMKWDEER FGLEYDLDIY
260 270 280 290 300
MIVAVDFFNM GAMENKGLNI FNSKYVLART DTATDKDYLD IERVIGHEYF
310 320 330 340 350
HNWTGNRVTC RDWFQLSLKE GLTVFRDQEF SSDLGSRAVN RINNVRTMRG
360 370 380 390 400
LQFAEDASPM AHPIRPDMVI EMNNFYTLTV YEKGAEVIRM IHTLLGEENF
410 420 430 440 450
QKGMQLYFER HDGSAATCDD FVQAMEDASN VDLSHFRRWY SQSGTPIVTV
460 470 480 490 500
KDDYNPETEQ YTLTISQRTP ATPDQAEKQP LHIPFAIELY DNEGKVIPLQ
510 520 530 540 550
KGGHPVNSVL NVTQAEQTFV FDNVYFQPVP ALLCEFSAPV KLEYKWSDQQ
560 570 580 590 600
LTFLMRHARN DFSRWDAAQS LLATYIKLNV ARHQQGQPLS LPVHVADAFR
610 620 630 640 650
AVLLDEKIDP ALAAEILTLP SVNEMAELFD IIDPIAIAEV REALTRTLAT
660 670 680 690 700
ELADELLAIY NANYQSEYRV EHEDIAKRTL RNACLRFLAF GETHLADVLV
710 720 730 740 750
SKQFHEANNM TDALAALSAA VAAQLPCRDA LMQEYDDKWH QNGLVMDKWF
760 770 780 790 800
ILQATSPAAN VLETVRGLLQ HRSFTMSNPN RIRSLIGAFA GSNPAAFHAE
810 820 830 840 850
DGSGYLFLVE MLTDLNSRNP QVASRLIEPL IRLKRYDAKR QEKMRAALEQ
860 870
LKGLENLSGD LYEKITKALA
Length:870
Mass (Da):98,919
Last modified:January 23, 2007 - v2
Checksum:i7C18C6BD8F2E5131
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti76E → D in CAA27647 (PubMed:2869947).Curated1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X04020 Genomic DNA. Translation: CAA27647.1.
X03709 Genomic DNA. Translation: CAA27336.1.
M15676 Genomic DNA. Translation: AAA24318.1.
U00096 Genomic DNA. Translation: AAC74018.1.
AP009048 Genomic DNA. Translation: BAA35684.1.
M15273 Genomic DNA. Translation: AAA24317.1.
PIRiC64833. DPECN.
RefSeqiNP_415452.1. NC_000913.3.
WP_000193841.1. NZ_LN832404.1.

Genome annotation databases

EnsemblBacteriaiAAC74018; AAC74018; b0932.
BAA35684; BAA35684; BAA35684.
GeneIDi947253.
KEGGiecj:JW0915.
eco:b0932.
PATRICi32117083. VBIEscCol129921_0966.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X04020 Genomic DNA. Translation: CAA27647.1.
X03709 Genomic DNA. Translation: CAA27336.1.
M15676 Genomic DNA. Translation: AAA24318.1.
U00096 Genomic DNA. Translation: AAC74018.1.
AP009048 Genomic DNA. Translation: BAA35684.1.
M15273 Genomic DNA. Translation: AAA24317.1.
PIRiC64833. DPECN.
RefSeqiNP_415452.1. NC_000913.3.
WP_000193841.1. NZ_LN832404.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
2DQ6X-ray1.50A1-870[»]
2DQMX-ray1.60A1-870[»]
2HPOX-ray1.65A1-870[»]
2HPTX-ray2.30A1-870[»]
2ZXGX-ray1.55A1-870[»]
3B2PX-ray2.00A1-870[»]
3B2XX-ray1.50A1-870[»]
3B34X-ray1.30A1-870[»]
3B37X-ray1.70A1-870[»]
3B3BX-ray1.85A1-870[»]
3KEDX-ray2.30A1-870[»]
3PUUX-ray2.15A1-870[»]
3QJXX-ray1.45A1-870[»]
4Q4EX-ray1.90A1-870[»]
4Q4IX-ray2.31A1-870[»]
4XMTX-ray2.00A4-870[»]
4XMUX-ray2.91A5-870[»]
4XMVX-ray2.92A5-870[»]
4XMWX-ray2.20A4-870[»]
4XMXX-ray2.30A5-870[»]
4XMZX-ray2.15A4-870[»]
4XN1X-ray2.20A4-870[»]
4XN2X-ray2.11A5-870[»]
4XN4X-ray1.99A5-870[»]
4XN5X-ray2.66A5-870[»]
4XN7X-ray2.22A5-870[»]
4XN8X-ray1.89A5-870[»]
4XN9X-ray2.80A5-870[»]
4XNAX-ray2.40A5-870[»]
4XNBX-ray1.95A5-870[»]
4XNDX-ray1.93A5-870[»]
4XO3X-ray2.00A5-870[»]
4XO4X-ray2.18A1-870[»]
4XO5X-ray1.98A5-870[»]
ProteinModelPortaliP04825.
SMRiP04825.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi4261880. 12 interactors.
851583. 1 interactor.
DIPiDIP-10458N.
IntActiP04825. 13 interactors.
MINTiMINT-1310653.
STRINGi511145.b0932.

Chemistry databases

BindingDBiP04825.
ChEMBLiCHEMBL4325.

Protein family/group databases

MEROPSiM01.005.

Proteomic databases

EPDiP04825.
PaxDbiP04825.
PRIDEiP04825.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAC74018; AAC74018; b0932.
BAA35684; BAA35684; BAA35684.
GeneIDi947253.
KEGGiecj:JW0915.
eco:b0932.
PATRICi32117083. VBIEscCol129921_0966.

Organism-specific databases

EchoBASEiEB0690.
EcoGeneiEG10696. pepN.

Phylogenomic databases

eggNOGiENOG4105CD8. Bacteria.
COG0308. LUCA.
HOGENOMiHOG000257670.
InParanoidiP04825.
KOiK01256.
OMAiMIVAVND.
PhylomeDBiP04825.

Enzyme and pathway databases

BioCyciEcoCyc:EG10696-MONOMER.
ECOL316407:JW0915-MONOMER.
MetaCyc:EG10696-MONOMER.
BRENDAi3.4.11.2. 2026.

Miscellaneous databases

EvolutionaryTraceiP04825.
PROiP04825.

Family and domain databases

CDDicd09600. M1_APN_1. 1 hit.
Gene3Di1.25.50.10. 1 hit.
InterProiIPR001930. Peptidase_M1.
IPR014782. Peptidase_M1_N.
IPR012779. Peptidase_M1_pepN.
IPR024601. Peptidase_M1_pepN_C.
[Graphical view]
PANTHERiPTHR11533. PTHR11533. 2 hits.
PfamiPF11940. DUF3458. 1 hit.
PF01433. Peptidase_M1. 1 hit.
[Graphical view]
PRINTSiPR00756. ALADIPTASE.
TIGRFAMsiTIGR02414. pepN_proteo. 1 hit.
PROSITEiPS00142. ZINC_PROTEASE. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiAMPN_ECOLI
AccessioniPrimary (citable) accession number: P04825
Entry historyi
Integrated into UniProtKB/Swiss-Prot: August 13, 1987
Last sequence update: January 23, 2007
Last modified: November 2, 2016
This is version 167 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. Escherichia coli
    Escherichia coli (strain K12): entries and cross-references to EcoGene
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. Peptidase families
    Classification of peptidase families and list of entries
  4. 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.