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P04825 (AMPN_ECOLI) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 127. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (4) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Aminopeptidase N
EC=3.4.11.2
Alternative name(s):
Alpha-aminoacylpeptide hydrolase
Gene names
Name:pepN
Ordered Locus Names:b0932, JW0915
OrganismEscherichia coli (strain K12)
Taxonomic identifier83333 [NCBI]
Taxonomic lineageBacteria › Proteobacteria › Gammaproteobacteria › Enterobacteriales › Enterobacteriaceae › Escherichia

Protein attributes

Sequence length870 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

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.

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. Ref.8 Ref.9 Ref.10

Cofactor

Binds 1 zinc ion per subunit. Ref.8 Ref.9 Ref.10

Subcellular location

Cell inner membrane; Peripheral membrane protein; Cytoplasmic side.

Sequence similarities

Belongs to the peptidase M1 family.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed Ref.7
Chain2 – 870869Aminopeptidase N
PRO_0000095069

Regions

Region261 – 2655Substrate binding

Sites

Active site2981Proton acceptor Probable
Metal binding2971Zinc; catalytic
Metal binding3011Zinc; catalytic
Metal binding3201Zinc; catalytic
Binding site1211Substrate
Site3811Transition state stabilizer Probable

Experimental info

Sequence conflict761E → D in CAA27647. Ref.7

Secondary structure

1 ........................................................................................................................................ 870
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P04825 [UniParc].

Last modified January 23, 2007. Version 2.
Checksum: 7C18C6BD8F2E5131

FASTA87098,919
        10         20         30         40         50         60 
MTQQPQAKYR HDYRAPDYQI TDIDLTFDLD AQKTVVTAVS QAVRHGASDA PLRLNGEDLK 

        70         80         90        100        110        120 
LVSVHINDEP WTAWKEEEGA LVISNLPERF TLKIINEISP AANTALEGLY QSGDALCTQC 

       130        140        150        160        170        180 
EAEGFRHITY YLDRPDVLAR FTTKIIADKI KYPFLLSNGN RVAQGELENG RHWVQWQDPF 

       190        200        210        220        230        240 
PKPCYLFALV AGDFDVLRDT FTTRSGREVA LELYVDRGNL DRAPWAMTSL KNSMKWDEER 

       250        260        270        280        290        300 
FGLEYDLDIY MIVAVDFFNM GAMENKGLNI FNSKYVLART DTATDKDYLD IERVIGHEYF 

       310        320        330        340        350        360 
HNWTGNRVTC RDWFQLSLKE GLTVFRDQEF SSDLGSRAVN RINNVRTMRG LQFAEDASPM 

       370        380        390        400        410        420 
AHPIRPDMVI EMNNFYTLTV YEKGAEVIRM IHTLLGEENF QKGMQLYFER HDGSAATCDD 

       430        440        450        460        470        480 
FVQAMEDASN VDLSHFRRWY SQSGTPIVTV KDDYNPETEQ YTLTISQRTP ATPDQAEKQP 

       490        500        510        520        530        540 
LHIPFAIELY DNEGKVIPLQ KGGHPVNSVL NVTQAEQTFV FDNVYFQPVP ALLCEFSAPV 

       550        560        570        580        590        600 
KLEYKWSDQQ LTFLMRHARN DFSRWDAAQS LLATYIKLNV ARHQQGQPLS LPVHVADAFR 

       610        620        630        640        650        660 
AVLLDEKIDP ALAAEILTLP SVNEMAELFD IIDPIAIAEV REALTRTLAT ELADELLAIY 

       670        680        690        700        710        720 
NANYQSEYRV EHEDIAKRTL RNACLRFLAF GETHLADVLV SKQFHEANNM TDALAALSAA 

       730        740        750        760        770        780 
VAAQLPCRDA LMQEYDDKWH QNGLVMDKWF ILQATSPAAN VLETVRGLLQ HRSFTMSNPN 

       790        800        810        820        830        840 
RIRSLIGAFA GSNPAAFHAE DGSGYLFLVE MLTDLNSRNP QVASRLIEPL IRLKRYDAKR 

       850        860        870 
QEKMRAALEQ LKGLENLSGD LYEKITKALA

« Hide

References

« Hide 'large scale' references
[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: 2436977] [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: 3549459] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: K12.
[3]"A 718-kb DNA sequence of the Escherichia coli K-12 genome corresponding to the 12.7-28.0 min region on the linkage map."
Oshima T., Aiba H., Baba T., Fujita K., Hayashi K., Honjo A., Ikemoto K., Inada T., Itoh T., Kajihara M., Kanai K., Kashimoto K., Kimura S., Kitagawa M., Makino K., Masuda S., Miki T., Mizobuchi K. expand/collapse author list , Mori H., Motomura K., Nakamura Y., Nashimoto H., Nishio Y., Saito N., Sampei G., Seki Y., Tagami H., Takemoto K., Wada C., Yamamoto Y., Yano M., Horiuchi T.
DNA Res. 3:137-155(1996) [PubMed: 8905232] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
[4]"The complete genome sequence of Escherichia coli K-12."
Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V., Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F., Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B., Shao Y.
Science 277:1453-1474(1997) [PubMed: 9278503] [Abstract]
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: 16738553] [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: 3018440] [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: 2869947] [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: 16885166] [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: 18416562] [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: 19622865] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.55 ANGSTROMS) IN COMPLEX WITH ZINC IONS AND TRANSITION-STATE ANALOG PL250, ACTIVE SITE, COFACTOR, CATALYTIC ACTIVITY.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		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.
PIRDPECN. C64833.
RefSeqNP_415452.1. NC_000913.2.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
2DQ6X-ray1.50A1-870[»]
2DQMX-ray1.60A1-870[»]
2HPOX-ray1.65A2-869[»]
2HPTX-ray2.30A2-869[»]
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[»]
ProteinModelPortalP04825.
SMRP04825. Positions 5-870.
ModBaseSearch...

Protein-protein interaction databases

DIPDIP-10458N.
IntActP04825. 8 interactions.
MINTMINT-1310653.

Protein family/group databases

MEROPSM01.005.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaEBESCT00000004980; EBESCP00000004980; EBESCG00000004065.
EBESCT00000015837; EBESCP00000015128; EBESCG00000014897.
GeneID947253.
GenomeReviewsGene locus JW0915 in contig AP009048_GR.
Gene locus b0932 in contig U00096_GR.
KEGGecj:JW0915.
eco:b0932.
PATRIC32117083. VBIEscCol129921_0966.

Organism-specific databases

EchoBASEEB0690.
EcoGeneEG10696. pepN.

Phylogenomic databases

eggNOGCOG0308.
GeneTreeEBGT00050000010234.
HOGENOMHBG289207.
OMADIFMIVA.
PhylomeDBP04825.
ProtClustDBPRK14015.

Enzyme and pathway databases

BioCycEcoCyc:EG10696-MONOMER.
MetaCyc:EG10696-MONOMER.
BRENDA3.4.11.2. 2026.

Gene expression databases

GenevestigatorP04825.

Family and domain databases

InterProIPR001930. Peptidase_M1.
IPR014782. Peptidase_M1_N.
IPR012779. Peptidase_M1_pepN.
IPR024601. Peptidase_M1_pepN_C.
[Graphical view]
Gene3DG3DSA:1.25.50.10. G3DSA:1.25.50.10. 1 hit.
KOK01256.
PANTHERPTHR11533:SF8. Pept_M1_pepN. 1 hit.
PTHR11533. Peptidase_M1. 1 hit.
PfamPF11940. DUF3458. 1 hit.
PF01433. Peptidase_M1. 1 hit.
[Graphical view]
PRINTSPR00756. ALADIPTASE.
TIGRFAMsTIGR02414. PepN_proteo. 1 hit.
PROSITEPS00142. ZINC_PROTEASE. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameAMPN_ECOLI
AccessionPrimary (citable) accession number: P04825
Entry history
Integrated into UniProtKB/Swiss-Prot: August 13, 1987
Last sequence update: January 23, 2007
Last modified: January 25, 2012
This is version 127 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

Peptidase families

Classification of peptidase families and list of entries

Escherichia coli

Escherichia coli (strain K12): entries and cross-references to EcoGene

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families

to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents