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P15034 (AMPP_ECOLI) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 144. 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·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Xaa-Pro aminopeptidase

EC=3.4.11.9
Alternative name(s):
Aminoacylproline aminopeptidase
Aminopeptidase P II
Short name=APP-II
X-Pro aminopeptidase
Gene names
Name:pepP
Ordered Locus Names:b2908, JW2876
OrganismEscherichia coli (strain K12) [Reference proteome] [HAMAP]
Taxonomic identifier83333 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia

Protein attributes

Sequence length441 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Catalytic activity

Release of any N-terminal amino acid, including proline, that is linked to proline, even from a dipeptide or tripeptide.

Cofactor

Binds 2 manganese ions per subunit.

Subunit structure

Homotetramer.

Subcellular location

Cytoplasm.

Sequence similarities

Belongs to the peptidase M24B family.

Binary interactions

With

Entry

#Exp.

IntAct

Notes

guaCP605602EBI-554801,EBI-544491

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed Ref.1
Chain2 – 441440Xaa-Pro aminopeptidase
PRO_0000185075

Sites

Metal binding2611Manganese 2
Metal binding2721Manganese 1
Metal binding2721Manganese 2
Metal binding3551Manganese 1
Metal binding3841Manganese 1
Metal binding4071Manganese 1
Metal binding4071Manganese 2

Secondary structure

......................................................................... 441
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P15034 [UniParc].

Last modified January 23, 2007. Version 2.
Checksum: 80A6A5BDD86D84B1

FASTA44149,815
        10         20         30         40         50         60 
MSEISRQEFQ RRRQALVEQM QPGSAALIFA APEVTRSADS EYPYRQNSDF WYFTGFNEPE 

        70         80         90        100        110        120 
AVLVLIKSDD THNHSVLFNR VRDLTAEIWF GRRLGQDAAP EKLGVDRALA FSEINQQLYQ 

       130        140        150        160        170        180 
LLNGLDVVYH AQGEYAYADV IVNSALEKLR KGSRQNLTAP ATMIDWRPVV HEMRLFKSPE 

       190        200        210        220        230        240 
EIAVLRRAGE ITAMAHTRAM EKCRPGMFEY HLEGEIHHEF NRHGARYPSY NTIVGSGENG 

       250        260        270        280        290        300 
CILHYTENEC EMRDGDLVLI DAGCEYKGYA GDITRTFPVN GKFTQAQREI YDIVLESLET 

       310        320        330        340        350        360 
SLRLYRPGTS ILEVTGEVVR IMVSGLVKLG ILKGDVDELI AQNAHRPFFM HGLSHWLGLD 

       370        380        390        400        410        420 
VHDVGVYGQD RSRILEPGMV LTVEPGLYIA PDAEVPEQYR GIGIRIEDDI VITETGNENL 

       430        440 
TASVVKKPEE IEALMVAARK Q 

« Hide

References

« Hide 'large scale' references
[1]"Sequencing and high expression of aminopeptidase P gene from Escherichia coli HB101."
Yoshimoto T., Tone H., Honda T., Osatomi K., Kobayashi R., Tsuru D.
J. Biochem. 105:412-416(1989) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 2-21, CHARACTERIZATION.
Strain: ATCC 33694 / HB101.
[2]"Isolation and characterization of a light-sensitive mutant of Escherichia coli K-12 with a mutation in a gene that is required for the biosynthesis of ubiquinone."
Nakahigashi K., Miyamoto K., Nishimura K., Inokuchi H.
J. Bacteriol. 174:7352-7359(1992) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: ATCC 33694 / HB101.
[3]"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 277:1453-1462(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: K12 / MG1655 / ATCC 47076.
[4]"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.
[5]"Structure and mechanism of a proline-specific aminopeptidase from Escherichia coli."
Wilce M.C.J., Bond C.S., Dixon N.E., Freeman H.C., Guss J.M., Lilley P.E., Wilce J.A.
Proc. Natl. Acad. Sci. U.S.A. 95:3472-3477(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS).
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
D00398 Genomic DNA. Translation: BAA00299.1.
D90281 Genomic DNA. Translation: BAA14325.1.
U28377 Genomic DNA. Translation: AAA69076.1.
U00096 Genomic DNA. Translation: AAC75946.1.
AP009048 Genomic DNA. Translation: BAE76973.1.
PIRDPECP. JX0067.
RefSeqNP_417384.1. NC_000913.3.
YP_491109.1. NC_007779.1.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1A16X-ray2.30A2-441[»]
1JAWX-ray2.70A2-441[»]
1M35X-ray2.40A/B/C/D/E/F2-440[»]
1N51X-ray2.30A2-440[»]
1W2MX-ray2.40A/B/C/D/E/F2-441[»]
1W7VX-ray2.00A/B/C/D2-440[»]
1WBQX-ray2.30A/B/C/D2-440[»]
1WL6X-ray2.00A2-440[»]
1WL9X-ray1.90A2-440[»]
1WLRX-ray2.10A2-440[»]
2BH3X-ray2.40A2-440[»]
2BHAX-ray2.40A2-440[»]
2BHBX-ray2.41A2-440[»]
2BHCX-ray2.40A2-440[»]
2BHDX-ray2.50A2-440[»]
2BN7X-ray2.40A2-440[»]
2BWSX-ray1.75A2-441[»]
2BWTX-ray2.90A2-440[»]
2BWUX-ray2.20A2-440[»]
2BWVX-ray1.70A2-441[»]
2BWWX-ray2.61A2-440[»]
2BWXX-ray1.70A2-440[»]
2BWYX-ray2.40A2-440[»]
2V3XX-ray1.70A2-440[»]
2V3YX-ray1.60A2-440[»]
2V3ZX-ray1.56A2-440[»]
ProteinModelPortalP15034.
SMRP15034. Positions 2-441.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

DIPDIP-10459N.
IntActP15034. 10 interactions.
MINTMINT-1252312.
STRING511145.b2908.

Protein family/group databases

MEROPSM24.004.

Proteomic databases

PaxDbP15034.
PRIDEP15034.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAC75946; AAC75946; b2908.
BAE76973; BAE76973; BAE76973.
GeneID12930242.
947385.
KEGGecj:Y75_p2840.
eco:b2908.
PATRIC32121230. VBIEscCol129921_3003.

Organism-specific databases

EchoBASEEB0691.
EcoGeneEG10697. pepP.

Phylogenomic databases

eggNOGCOG0006.
HOGENOMHOG000008762.
KOK01262.
OMADPLMETW.
OrthoDBEOG6XHC3N.
PhylomeDBP15034.
ProtClustDBPRK10879.

Enzyme and pathway databases

BioCycEcoCyc:EG10697-MONOMER.
ECOL316407:JW2876-MONOMER.
MetaCyc:EG10697-MONOMER.

Gene expression databases

GenevestigatorP15034.

Family and domain databases

Gene3D3.90.230.10. 1 hit.
InterProIPR007865. Aminopep_P_N.
IPR001714. Pept_M24_MAP.
IPR000994. Pept_M24_structural-domain.
IPR001131. Peptidase_M24B_aminopep-P_CS.
[Graphical view]
PfamPF05195. AMP_N. 1 hit.
PF00557. Peptidase_M24. 1 hit.
[Graphical view]
PRINTSPR00599. MAPEPTIDASE.
SMARTSM01011. AMP_N. 1 hit.
[Graphical view]
SUPFAMSSF55920. SSF55920. 1 hit.
PROSITEPS00491. PROLINE_PEPTIDASE. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceP15034.
PROP15034.

Entry information

Entry nameAMPP_ECOLI
AccessionPrimary (citable) accession number: P15034
Secondary accession number(s): Q2M9T3
Entry history
Integrated into UniProtKB/Swiss-Prot: April 1, 1990
Last sequence update: January 23, 2007
Last modified: April 16, 2014
This is version 144 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

Peptidase families

Classification of peptidase families and list of entries

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

Escherichia coli

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