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P04825

- AMPN_ECOLI

UniProt

P04825 - AMPN_ECOLI

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Protein

Aminopeptidase N

Gene

pepN

Organism
Escherichia coli (strain K12)
Status
Reviewed - 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.

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

Binds 1 zinc ion per subunit.3 Publications

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei121 – 1211Substrate
Metal bindingi297 – 2971Zinc; catalytic
Active sitei298 – 2981Proton acceptor3 Publications
Metal bindingi301 – 3011Zinc; catalytic
Metal bindingi320 – 3201Zinc; catalytic
Sitei381 – 3811Transition state stabilizerCurated

GO - Molecular functioni

  1. aminopeptidase activity Source: EcoliWiki
  2. identical protein binding Source: IntAct
  3. metallopeptidase activity Source: UniProtKB-KW
  4. zinc ion binding Source: InterPro

GO - Biological processi

  1. peptide catabolic process Source: EcoliWiki
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.
RETL1328306-WGS:GSTH-1303-MONOMER.
BRENDAi3.4.11.2. 2026.

Protein family/group databases

MEROPSiM01.005.

Names & Taxonomyi

Protein namesi
Recommended name:
Aminopeptidase N (EC:3.4.11.2)
Alternative name(s):
Alpha-aminoacylpeptide hydrolase
Gene namesi
Name:pepN
Ordered Locus Names:b0932, JW0915
OrganismiEscherichia coli (strain K12)
Taxonomic identifieri83333 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia
ProteomesiUP000000318: Chromosome, UP000000625: Chromosome

Organism-specific databases

EcoGeneiEG10696. pepN.

Subcellular locationi

GO - Cellular componenti

  1. plasma membrane Source: UniProtKB-KW
Complete GO annotation...

Keywords - Cellular componenti

Cell inner membrane, Cell membrane, Membrane

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11Removed1 Publication
Chaini2 – 870869Aminopeptidase NPRO_0000095069Add
BLAST

Proteomic databases

PaxDbiP04825.
PRIDEiP04825.

Expressioni

Gene expression databases

GenevestigatoriP04825.

Interactioni

Binary interactionsi

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

Protein-protein interaction databases

BioGridi851583. 1 interaction.
DIPiDIP-10458N.
IntActiP04825. 13 interactions.
MINTiMINT-1310653.
STRINGi511145.b0932.

Structurei

Secondary structure

1
870
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi10 – 123
Beta strandi17 – 2812
Beta strandi34 – 4411
Beta strandi52 – 554
Beta strandi60 – 667
Beta strandi73 – 775
Beta strandi80 – 834
Beta strandi88 – 9811
Helixi100 – 1023
Beta strandi108 – 1125
Beta strandi115 – 1195
Turni121 – 1244
Helixi125 – 1273
Beta strandi129 – 1313
Beta strandi139 – 14810
Turni149 – 1513
Beta strandi154 – 16613
Beta strandi171 – 18212
Helixi184 – 1863
Beta strandi189 – 1924
Beta strandi195 – 2028
Beta strandi208 – 2158
Helixi220 – 2223
Helixi224 – 24118
Beta strandi247 – 25610
Beta strandi259 – 2635
Beta strandi268 – 2725
Helixi273 – 2753
Turni280 – 2823
Helixi285 – 30016
Turni301 – 3033
Turni305 – 3073
Beta strandi308 – 3125
Helixi313 – 3153
Helixi316 – 33419
Helixi337 – 35014
Helixi352 – 3565
Beta strandi367 – 3704
Helixi372 – 3754
Helixi378 – 41134
Beta strandi414 – 4163
Helixi418 – 42912
Turni434 – 4374
Helixi438 – 4414
Beta strandi447 – 4559
Turni456 – 4594
Beta strandi460 – 4689
Beta strandi483 – 4908
Beta strandi508 – 5125
Beta strandi514 – 5218
Beta strandi529 – 5335
Helixi534 – 5363
Beta strandi541 – 5433
Helixi548 – 55710
Helixi561 – 58424
Helixi593 – 60412
Beta strandi606 – 6083
Helixi610 – 6167
Helixi622 – 6265
Helixi634 – 65118
Helixi653 – 66210
Helixi672 – 68918
Helixi693 – 70614
Helixi710 – 72213
Helixi728 – 73912
Helixi743 – 75412
Helixi761 – 7688
Helixi779 – 79214
Helixi794 – 7974
Helixi803 – 81816
Helixi820 – 83112
Helixi832 – 8354
Helixi838 – 85215
Helixi859 – 86911

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
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[»]
ProteinModelPortaliP04825.
SMRiP04825. Positions 5-870.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP04825.

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni261 – 2655Substrate binding

Sequence similaritiesi

Belongs to the peptidase M1 family.Curated

Phylogenomic databases

eggNOGiCOG0308.
HOGENOMiHOG000257670.
InParanoidiP04825.
KOiK01256.
OMAiRWDAAQM.
OrthoDBiEOG693GJ0.
PhylomeDBiP04825.

Family and domain databases

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. 1 hit.
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)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti76 – 761E → D in CAA27647. (PubMed:2869947)Curated

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
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.
YP_489204.1. NC_007779.1.

Genome annotation databases

EnsemblBacteriaiAAC74018; AAC74018; b0932.
BAA35684; BAA35684; BAA35684.
GeneIDi12932886.
947253.
KEGGiecj:Y75_p0904.
eco:b0932.
PATRICi32117083. VBIEscCol129921_0966.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
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 .
PIRi C64833. DPECN.
RefSeqi NP_415452.1. NC_000913.3.
YP_489204.1. NC_007779.1.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
2DQ6 X-ray 1.50 A 1-870 [» ]
2DQM X-ray 1.60 A 1-870 [» ]
2HPO X-ray 1.65 A 1-870 [» ]
2HPT X-ray 2.30 A 1-870 [» ]
2ZXG X-ray 1.55 A 1-870 [» ]
3B2P X-ray 2.00 A 1-870 [» ]
3B2X X-ray 1.50 A 1-870 [» ]
3B34 X-ray 1.30 A 1-870 [» ]
3B37 X-ray 1.70 A 1-870 [» ]
3B3B X-ray 1.85 A 1-870 [» ]
3KED X-ray 2.30 A 1-870 [» ]
3PUU X-ray 2.15 A 1-870 [» ]
3QJX X-ray 1.45 A 1-870 [» ]
ProteinModelPortali P04825.
SMRi P04825. Positions 5-870.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 851583. 1 interaction.
DIPi DIP-10458N.
IntActi P04825. 13 interactions.
MINTi MINT-1310653.
STRINGi 511145.b0932.

Chemistry

BindingDBi P04825.
ChEMBLi CHEMBL4325.

Protein family/group databases

MEROPSi M01.005.

Proteomic databases

PaxDbi P04825.
PRIDEi P04825.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblBacteriai AAC74018 ; AAC74018 ; b0932 .
BAA35684 ; BAA35684 ; BAA35684 .
GeneIDi 12932886.
947253.
KEGGi ecj:Y75_p0904.
eco:b0932.
PATRICi 32117083. VBIEscCol129921_0966.

Organism-specific databases

EchoBASEi EB0690.
EcoGenei EG10696. pepN.

Phylogenomic databases

eggNOGi COG0308.
HOGENOMi HOG000257670.
InParanoidi P04825.
KOi K01256.
OMAi RWDAAQM.
OrthoDBi EOG693GJ0.
PhylomeDBi P04825.

Enzyme and pathway databases

BioCyci EcoCyc:EG10696-MONOMER.
ECOL316407:JW0915-MONOMER.
MetaCyc:EG10696-MONOMER.
RETL1328306-WGS:GSTH-1303-MONOMER.
BRENDAi 3.4.11.2. 2026.

Miscellaneous databases

EvolutionaryTracei P04825.
PROi P04825.

Gene expression databases

Genevestigatori P04825.

Family and domain databases

Gene3Di 1.25.50.10. 1 hit.
InterProi IPR001930. Peptidase_M1.
IPR014782. Peptidase_M1_N.
IPR012779. Peptidase_M1_pepN.
IPR024601. Peptidase_M1_pepN_C.
[Graphical view ]
PANTHERi PTHR11533. PTHR11533. 1 hit.
Pfami PF11940. DUF3458. 1 hit.
PF01433. Peptidase_M1. 1 hit.
[Graphical view ]
PRINTSi PR00756. ALADIPTASE.
TIGRFAMsi TIGR02414. pepN_proteo. 1 hit.
PROSITEi PS00142. ZINC_PROTEASE. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "Nucleotide sequence of the pepN gene encoding aminopeptidase N of Escherichia coli."
    Foglino M., Gharbi S., Lazdunski A.
    Gene 49:303-309(1986) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  2. "The nucleotide sequence of the pepN gene and its over-expression in Escherichia coli."
    McCaman M.T., Gabe J.D.
    Gene 48:145-153(1986) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: K12.
  3. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
  4. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: K12 / MG1655 / ATCC 47076.
  5. "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655 and W3110."
    Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S., Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.
    Mol. Syst. Biol. 2:E1-E5(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
  6. "Sequence of the promoter and 5' coding region of pepN, and the amino-terminus of peptidase N from Escherichia coli K-12."
    McCaman M.T., Gabe J.D.
    Mol. Gen. Genet. 204:148-152(1986) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-242.
    Strain: K12.
  7. "Nucleotide sequence of the promoter and amino-terminal encoding region of the Escherichia coli pepN gene."
    Bally M., Foglino M., Bruschi M., Murgier M., Lazdunski A.
    Eur. J. Biochem. 155:565-569(1986) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-177, PROTEIN SEQUENCE OF 2-22.
  8. "Crystal structure of aminopeptidase N (proteobacteria alanyl aminopeptidase) from Escherichia coli and conformational change of methionine 260 involved in substrate recognition."
    Ito K., Nakajima Y., Onohara Y., Takeo M., Nakashima K., Matsubara F., Ito T., Yoshimoto T.
    J. Biol. Chem. 281:33664-33676(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.5 ANGSTROMS) IN COMPLEX WITH ZINC IONS AND BESTATIN, ACTIVE SITE, COFACTOR, CATALYTIC ACTIVITY.
  9. "Structural basis for the unusual specificity of Escherichia coli aminopeptidase N."
    Addlagatta A., Gay L., Matthews B.W.
    Biochemistry 47:5303-5311(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.3 ANGSTROMS) IN COMPLEXES WITH ZINC IONS AND SUBSTRATE ANALOGS, CATALYTIC ACTIVITY, ACTIVE SITE, COFACTOR.
  10. "Structure of aminopeptidase N from Escherichia coli complexed with the transition-state analogue aminophosphinic inhibitor PL250."
    Fournie-Zaluski M.C., Poras H., Roques B.P., Nakajima Y., Ito K., Yoshimoto T.
    Acta Crystallogr. D 65:814-822(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.55 ANGSTROMS) IN COMPLEX WITH ZINC IONS AND TRANSITION-STATE ANALOG PL250, ACTIVE SITE, COFACTOR, CATALYTIC ACTIVITY.

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: October 29, 2014
This is version 152 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

External Data

Dasty 3