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P15034

- AMPP_ECOLI

UniProt

P15034 - AMPP_ECOLI

Protein

Xaa-Pro aminopeptidase

Gene

pepP

Organism
Escherichia coli (strain K12)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 148 (01 Oct 2014)
      Sequence version 2 (23 Jan 2007)
      Previous versions | rss
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    Functioni

    Catalytic activityi

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

    Cofactori

    Binds 2 manganese ions per subunit.

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Metal bindingi261 – 2611Manganese 2
    Metal bindingi272 – 2721Manganese 1
    Metal bindingi272 – 2721Manganese 2
    Metal bindingi355 – 3551Manganese 1
    Metal bindingi384 – 3841Manganese 1
    Metal bindingi407 – 4071Manganese 1
    Metal bindingi407 – 4071Manganese 2

    GO - Molecular functioni

    1. aminopeptidase activity Source: EcoCyc
    2. manganese ion binding Source: InterPro
    3. metalloexopeptidase activity Source: InterPro
    4. protein binding Source: IntAct

    Keywords - Molecular functioni

    Aminopeptidase, Hydrolase, Metalloprotease, Protease

    Keywords - Ligandi

    Manganese, Metal-binding

    Enzyme and pathway databases

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

    Protein family/group databases

    MEROPSiM24.004.

    Names & Taxonomyi

    Protein namesi
    Recommended 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 namesi
    Name:pepP
    Ordered Locus Names:b2908, JW2876
    OrganismiEscherichia coli (strain K12)
    Taxonomic identifieri83333 [NCBI]
    Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia
    ProteomesiUP000000318: Chromosome, UP000000625: Chromosome

    Organism-specific databases

    EcoGeneiEG10697. pepP.

    Subcellular locationi

    GO - Cellular componenti

    1. cytosol Source: UniProtKB

    Keywords - Cellular componenti

    Cytoplasm

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Initiator methioninei1 – 11Removed1 Publication
    Chaini2 – 441440Xaa-Pro aminopeptidasePRO_0000185075Add
    BLAST

    Proteomic databases

    PaxDbiP15034.
    PRIDEiP15034.

    Expressioni

    Gene expression databases

    GenevestigatoriP15034.

    Interactioni

    Subunit structurei

    Homotetramer.

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    guaCP605602EBI-554801,EBI-544491

    Protein-protein interaction databases

    DIPiDIP-10459N.
    IntActiP15034. 10 interactions.
    MINTiMINT-1252312.
    STRINGi511145.b2908.

    Structurei

    Secondary structure

    1
    441
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Helixi6 – 1914
    Beta strandi22 – 298
    Beta strandi35 – 373
    Helixi48 – 547
    Beta strandi62 – 676
    Beta strandi69 – 713
    Beta strandi73 – 797
    Helixi84 – 907
    Helixi95 – 1039
    Beta strandi106 – 1105
    Helixi111 – 1133
    Helixi114 – 1229
    Beta strandi126 – 1294
    Helixi136 – 15015
    Helixi153 – 1553
    Beta strandi161 – 1644
    Helixi167 – 1759
    Helixi179 – 20224
    Helixi209 – 22214
    Beta strandi227 – 2304
    Beta strandi233 – 2364
    Helixi237 – 2415
    Beta strandi257 – 2626
    Beta strandi264 – 2663
    Beta strandi273 – 2786
    Helixi285 – 30420
    Helixi311 – 32818
    Helixi336 – 3416
    Turni342 – 3487
    Beta strandi358 – 3625
    Helixi369 – 3713
    Beta strandi380 – 3834
    Beta strandi386 – 3894
    Helixi397 – 3993
    Beta strandi402 – 4054
    Beta strandi407 – 4137
    Beta strandi416 – 4216
    Helixi428 – 43912

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1A16X-ray2.30A2-441[»]
    1JAWX-ray2.70A2-441[»]
    1M35X-ray2.40A/B/C/D/E/F2-441[»]
    1N51X-ray2.30A2-441[»]
    1W2MX-ray2.40A/B/C/D/E/F2-441[»]
    1W7VX-ray2.00A/B/C/D2-441[»]
    1WBQX-ray2.30A/B/C/D2-441[»]
    1WL6X-ray2.00A2-441[»]
    1WL9X-ray1.90A2-441[»]
    1WLRX-ray2.10A2-441[»]
    2BH3X-ray2.40A2-441[»]
    2BHAX-ray2.40A2-441[»]
    2BHBX-ray2.41A2-441[»]
    2BHCX-ray2.40A2-441[»]
    2BHDX-ray2.50A2-441[»]
    2BN7X-ray2.40A2-441[»]
    2BWSX-ray1.75A2-441[»]
    2BWTX-ray2.90A2-441[»]
    2BWUX-ray2.20A2-441[»]
    2BWVX-ray1.70A2-441[»]
    2BWWX-ray2.61A2-441[»]
    2BWXX-ray1.70A2-441[»]
    2BWYX-ray2.40A2-441[»]
    2V3XX-ray1.70A2-441[»]
    2V3YX-ray1.60A2-441[»]
    2V3ZX-ray1.56A2-441[»]
    ProteinModelPortaliP15034.
    SMRiP15034. Positions 2-441.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP15034.

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the peptidase M24B family.Curated

    Phylogenomic databases

    eggNOGiCOG0006.
    HOGENOMiHOG000008762.
    KOiK01262.
    OMAiHDVGHYG.
    OrthoDBiEOG6XHC3N.
    PhylomeDBiP15034.

    Family and domain databases

    Gene3Di3.40.350.10. 1 hit.
    3.90.230.10. 1 hit.
    InterProiIPR007865. Aminopep_P_N.
    IPR029149. Creatin/AminoP/Spt16_NTD.
    IPR028980. Creatinase/Aminopeptidase_P_N.
    IPR001714. Pept_M24_MAP.
    IPR000994. Pept_M24_structural-domain.
    IPR001131. Peptidase_M24B_aminopep-P_CS.
    [Graphical view]
    PfamiPF05195. AMP_N. 1 hit.
    PF00557. Peptidase_M24. 1 hit.
    [Graphical view]
    PRINTSiPR00599. MAPEPTIDASE.
    SMARTiSM01011. AMP_N. 1 hit.
    [Graphical view]
    SUPFAMiSSF53092. SSF53092. 1 hit.
    SSF55920. SSF55920. 1 hit.
    PROSITEiPS00491. PROLINE_PEPTIDASE. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

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

    P15034-1 [UniParc]FASTAAdd to Basket

    « Hide

    MSEISRQEFQ RRRQALVEQM QPGSAALIFA APEVTRSADS EYPYRQNSDF    50
    WYFTGFNEPE AVLVLIKSDD THNHSVLFNR VRDLTAEIWF GRRLGQDAAP 100
    EKLGVDRALA FSEINQQLYQ LLNGLDVVYH AQGEYAYADV IVNSALEKLR 150
    KGSRQNLTAP ATMIDWRPVV HEMRLFKSPE EIAVLRRAGE ITAMAHTRAM 200
    EKCRPGMFEY HLEGEIHHEF NRHGARYPSY NTIVGSGENG CILHYTENEC 250
    EMRDGDLVLI DAGCEYKGYA GDITRTFPVN GKFTQAQREI YDIVLESLET 300
    SLRLYRPGTS ILEVTGEVVR IMVSGLVKLG ILKGDVDELI AQNAHRPFFM 350
    HGLSHWLGLD VHDVGVYGQD RSRILEPGMV LTVEPGLYIA PDAEVPEQYR 400
    GIGIRIEDDI VITETGNENL TASVVKKPEE IEALMVAARK Q 441
    Length:441
    Mass (Da):49,815
    Last modified:January 23, 2007 - v2
    Checksum:i80A6A5BDD86D84B1
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    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.
    PIRiJX0067. DPECP.
    RefSeqiNP_417384.1. NC_000913.3.
    YP_491109.1. NC_007779.1.

    Genome annotation databases

    EnsemblBacteriaiAAC75946; AAC75946; b2908.
    BAE76973; BAE76973; BAE76973.
    GeneIDi12930242.
    947385.
    KEGGiecj:Y75_p2840.
    eco:b2908.
    PATRICi32121230. VBIEscCol129921_3003.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    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 .
    PIRi JX0067. DPECP.
    RefSeqi NP_417384.1. NC_000913.3.
    YP_491109.1. NC_007779.1.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1A16 X-ray 2.30 A 2-441 [» ]
    1JAW X-ray 2.70 A 2-441 [» ]
    1M35 X-ray 2.40 A/B/C/D/E/F 2-441 [» ]
    1N51 X-ray 2.30 A 2-441 [» ]
    1W2M X-ray 2.40 A/B/C/D/E/F 2-441 [» ]
    1W7V X-ray 2.00 A/B/C/D 2-441 [» ]
    1WBQ X-ray 2.30 A/B/C/D 2-441 [» ]
    1WL6 X-ray 2.00 A 2-441 [» ]
    1WL9 X-ray 1.90 A 2-441 [» ]
    1WLR X-ray 2.10 A 2-441 [» ]
    2BH3 X-ray 2.40 A 2-441 [» ]
    2BHA X-ray 2.40 A 2-441 [» ]
    2BHB X-ray 2.41 A 2-441 [» ]
    2BHC X-ray 2.40 A 2-441 [» ]
    2BHD X-ray 2.50 A 2-441 [» ]
    2BN7 X-ray 2.40 A 2-441 [» ]
    2BWS X-ray 1.75 A 2-441 [» ]
    2BWT X-ray 2.90 A 2-441 [» ]
    2BWU X-ray 2.20 A 2-441 [» ]
    2BWV X-ray 1.70 A 2-441 [» ]
    2BWW X-ray 2.61 A 2-441 [» ]
    2BWX X-ray 1.70 A 2-441 [» ]
    2BWY X-ray 2.40 A 2-441 [» ]
    2V3X X-ray 1.70 A 2-441 [» ]
    2V3Y X-ray 1.60 A 2-441 [» ]
    2V3Z X-ray 1.56 A 2-441 [» ]
    ProteinModelPortali P15034.
    SMRi P15034. Positions 2-441.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    DIPi DIP-10459N.
    IntActi P15034. 10 interactions.
    MINTi MINT-1252312.
    STRINGi 511145.b2908.

    Protein family/group databases

    MEROPSi M24.004.

    Proteomic databases

    PaxDbi P15034.
    PRIDEi P15034.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblBacteriai AAC75946 ; AAC75946 ; b2908 .
    BAE76973 ; BAE76973 ; BAE76973 .
    GeneIDi 12930242.
    947385.
    KEGGi ecj:Y75_p2840.
    eco:b2908.
    PATRICi 32121230. VBIEscCol129921_3003.

    Organism-specific databases

    EchoBASEi EB0691.
    EcoGenei EG10697. pepP.

    Phylogenomic databases

    eggNOGi COG0006.
    HOGENOMi HOG000008762.
    KOi K01262.
    OMAi HDVGHYG.
    OrthoDBi EOG6XHC3N.
    PhylomeDBi P15034.

    Enzyme and pathway databases

    BioCyci EcoCyc:EG10697-MONOMER.
    ECOL316407:JW2876-MONOMER.
    MetaCyc:EG10697-MONOMER.

    Miscellaneous databases

    EvolutionaryTracei P15034.
    PROi P15034.

    Gene expression databases

    Genevestigatori P15034.

    Family and domain databases

    Gene3Di 3.40.350.10. 1 hit.
    3.90.230.10. 1 hit.
    InterProi IPR007865. Aminopep_P_N.
    IPR029149. Creatin/AminoP/Spt16_NTD.
    IPR028980. Creatinase/Aminopeptidase_P_N.
    IPR001714. Pept_M24_MAP.
    IPR000994. Pept_M24_structural-domain.
    IPR001131. Peptidase_M24B_aminopep-P_CS.
    [Graphical view ]
    Pfami PF05195. AMP_N. 1 hit.
    PF00557. Peptidase_M24. 1 hit.
    [Graphical view ]
    PRINTSi PR00599. MAPEPTIDASE.
    SMARTi SM01011. AMP_N. 1 hit.
    [Graphical view ]
    SUPFAMi SSF53092. SSF53092. 1 hit.
    SSF55920. SSF55920. 1 hit.
    PROSITEi PS00491. PROLINE_PEPTIDASE. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    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. 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).

    Entry informationi

    Entry nameiAMPP_ECOLI
    AccessioniPrimary (citable) accession number: P15034
    Secondary accession number(s): Q2M9T3
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: April 1, 1990
    Last sequence update: January 23, 2007
    Last modified: October 1, 2014
    This is version 148 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