Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

Xaa-Pro dipeptidase

Gene

pepQ

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

Functioni

Splits dipeptides with a prolyl residue in the C-terminal position and a polar or nonpolar amino acid at the N-terminal position. With much lower efficiency, also catalyzes the stereoselective hydrolysis of a wide variety of organophosphate triesters and organophosphonate diesters. Is able to hydrolyze the organophosphorus insecticide paraoxon and the p-nitrophenyl analogs of the nerve agents GB (sarin), GD (soman), GF, Vx and rVX.1 Publication

Miscellaneous

Has a stereoselective preference for isomers with R-configuration at the phosphorous center of organophosphonate diesters and with S-configuration in organophosphate triesters.

Catalytic activityi

Hydrolysis of Xaa-|-Pro dipeptides; also acts on aminoacyl-hydroxyproline analogs. No action on Pro-|-Pro.

Cofactori

Mn2+By similarityNote: Binds 2 manganese ions per subunit.By similarity

Kineticsi

Among the dipeptides described above, the highest catalytic efficiency is observed with dipeptides containing charge residues.
  1. KM=1.9 mM for Ala-Pro1 Publication
  2. KM=0.10 mM for Arg-Pro1 Publication
  3. KM=1.4 mM for Gly-Pro1 Publication
  4. KM=0.15 mM for His-Pro1 Publication
  5. KM=0.10 mM for Ile-Pro1 Publication
  6. KM=1.0 mM for Leu-Pro1 Publication
  7. KM=0.27 mM for Lys-Pro1 Publication
  8. KM=0.13 mM for Met-Pro1 Publication
  9. KM=0.43 mM for Phe-Pro1 Publication
  10. KM=0.31 mM for Pro-Pro1 Publication
  11. KM=0.46 mM for Ser-Pro1 Publication
  12. KM=0.16 mM for Tyr-Pro1 Publication
  13. KM=0.40 mM for Val-Pro1 Publication
  14. KM=38 mM for diisopropylfluorophosphate1 Publication

    Sites

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Metal bindingi246Manganese 2By similarity1
    Metal bindingi257Manganese 1By similarity1
    Metal bindingi257Manganese 2By similarity1
    Metal bindingi339Manganese 1By similarity1
    Metal bindingi384Manganese 1By similarity1
    Metal bindingi423Manganese 1By similarity1
    Metal bindingi423Manganese 2By similarity1

    GO - Molecular functioni

    • dipeptidase activity Source: EcoCyc
    • manganese ion binding Source: EcoCyc
    • metallodipeptidase activity Source: EcoCyc
    • phosphoric triester hydrolase activity Source: InterPro
    • proline dipeptidase activity Source: UniProtKB-EC

    GO - Biological processi

    • peptide catabolic process Source: EcoliWiki

    Keywordsi

    Molecular functionDipeptidase, Hydrolase, Metalloprotease, Protease
    LigandManganese, Metal-binding

    Enzyme and pathway databases

    BioCyciEcoCyc:EG10698-MONOMER
    MetaCyc:EG10698-MONOMER

    Protein family/group databases

    MEROPSiM24.003

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Xaa-Pro dipeptidase (EC:3.4.13.9)
    Short name:
    X-Pro dipeptidase
    Alternative name(s):
    Imidodipeptidase
    Proline dipeptidase
    Short name:
    Prolidase
    Gene namesi
    Name:pepQ
    Ordered Locus Names:b3847, JW3823
    OrganismiEscherichia coli (strain K12)
    Taxonomic identifieri83333 [NCBI]
    Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacteralesEnterobacteriaceaeEscherichia
    Proteomesi
    • UP000000318 Componenti: Chromosome
    • UP000000625 Componenti: Chromosome

    Organism-specific databases

    EcoGeneiEG10698 pepQ

    Subcellular locationi

    GO - Cellular componenti

    • cytosol Source: EcoCyc

    Pathology & Biotechi

    Biotechnological usei

    Can be utilized for the kinetic resolution of racemic phosphate esters.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    ChainiPRO_00001850891 – 443Xaa-Pro dipeptidaseAdd BLAST443

    Proteomic databases

    EPDiP21165
    PaxDbiP21165
    PRIDEiP21165

    2D gel databases

    SWISS-2DPAGEiP21165

    Interactioni

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    rluDP336432EBI-552580,EBI-558026

    Protein-protein interaction databases

    BioGridi4261838, 32 interactors
    DIPiDIP-10460N
    IntActiP21165, 4 interactors
    STRINGi316385.ECDH10B_4036

    Structurei

    Secondary structure

    1443
    Legend: HelixTurnBeta strandPDB Structure known for this area
    Show more details
    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Helixi4 – 26Combined sources23
    Beta strandi29 – 34Combined sources6
    Helixi54 – 57Combined sources4
    Beta strandi69 – 72Combined sources4
    Beta strandi74 – 76Combined sources3
    Beta strandi79 – 83Combined sources5
    Beta strandi88 – 90Combined sources3
    Helixi99 – 102Combined sources4
    Beta strandi104 – 111Combined sources8
    Helixi112 – 114Combined sources3
    Turni116 – 118Combined sources3
    Beta strandi126 – 131Combined sources6
    Helixi133 – 138Combined sources6
    Helixi143 – 145Combined sources3
    Helixi149 – 159Combined sources11
    Helixi164 – 189Combined sources26
    Helixi194 – 205Combined sources12
    Turni209 – 211Combined sources3
    Beta strandi212 – 214Combined sources3
    Beta strandi217 – 220Combined sources4
    Helixi221 – 225Combined sources5
    Beta strandi242 – 251Combined sources10
    Beta strandi254 – 264Combined sources11
    Beta strandi266 – 268Combined sources3
    Helixi269 – 287Combined sources19
    Helixi294 – 311Combined sources18
    Helixi320 – 325Combined sources6
    Turni326 – 329Combined sources4
    Helixi330 – 332Combined sources3
    Beta strandi342 – 346Combined sources5
    Beta strandi350 – 352Combined sources3
    Beta strandi380 – 383Combined sources4
    Beta strandi386 – 388Combined sources3
    Helixi391 – 399Combined sources9
    Helixi403 – 405Combined sources3
    Helixi408 – 414Combined sources7
    Helixi415 – 417Combined sources3
    Beta strandi419 – 421Combined sources3
    Beta strandi423 – 428Combined sources6
    Beta strandi433 – 435Combined sources3
    Helixi436 – 439Combined sources4

    3D structure databases

    Select the link destinations:
    PDBei
    RCSB PDBi
    PDBji
    Links Updated
    PDB entryMethodResolution (Å)ChainPositionsPDBsum
    4QR8X-ray2.00A/B1-443[»]
    ProteinModelPortaliP21165
    SMRiP21165
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Sequence similaritiesi

    Phylogenomic databases

    eggNOGiENOG4105D9Y Bacteria
    COG0006 LUCA
    HOGENOMiHOG000290531
    InParanoidiP21165
    KOiK01271
    OMAiMQDDTGT
    PhylomeDBiP21165

    Family and domain databases

    Gene3Di3.40.350.10, 1 hit
    HAMAPiMF_01279 X_Pro_dipeptid, 1 hit
    InterProiView protein in InterPro
    IPR029149 Creatin/AminoP/Spt16_NTD
    IPR036005 Creatinase/aminopeptidase-like
    IPR000994 Pept_M24
    IPR001131 Peptidase_M24B_aminopep-P_CS
    IPR022846 X_Pro_dipept
    PfamiView protein in Pfam
    PF00557 Peptidase_M24, 1 hit
    SUPFAMiSSF55920 SSF55920, 1 hit
    PROSITEiView protein in PROSITE
    PS00491 PROLINE_PEPTIDASE, 1 hit

    Sequencei

    Sequence statusi: Complete.

    P21165-1 [UniParc]FASTAAdd to basket

    « Hide

            10         20         30         40         50
    MESLASLYKN HIATLQERTR DALARFKLDA LLIHSGELFN VFLDDHPYPF
    60 70 80 90 100
    KVNPQFKAWV PVTQVPNCWL LVDGVNKPKL WFYLPVDYWH NVEPLPTSFW
    110 120 130 140 150
    TEDVEVIALP KADGIGSLLP AARGNIGYIG PVPERALQLG IEASNINPKG
    160 170 180 190 200
    VIDYLHYYRS FKTEYELACM REAQKMAVNG HRAAEEAFRS GMSEFDINIA
    210 220 230 240 250
    YLTATGHRDT DVPYSNIVAL NEHAAVLHYT KLDHQAPEEM RSFLLDAGAE
    260 270 280 290 300
    YNGYAADLTR TWSAKSDNDY AQLVKDVNDE QLALIATMKA GVSYVDYHIQ
    310 320 330 340 350
    FHQRIAKLLR KHQIITDMSE EAMVENDLTG PFMPHGIGHP LGLQVHDVAG
    360 370 380 390 400
    FMQDDSGTHL AAPAKYPYLR CTRILQPGMV LTIEPGIYFI ESLLAPWREG
    410 420 430 440
    QFSKHFNWQK IEALKPFGGI RIEDNVVIHE NNVENMTRDL KLA
    Length:443
    Mass (Da):50,176
    Last modified:October 1, 1993 - v2
    Checksum:iC5CB313DB774F670
    GO

    Sequence cautioni

    The sequence CAA38501 differs from that shown. Reason: Frameshift at position 430. The resulting sequence is much longer and includes the sequence of yigZ.Curated

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    X54687 Genomic DNA Translation: CAA38501.1 Frameshift.
    M87049 Genomic DNA Translation: AAA67644.1
    U00096 Genomic DNA Translation: AAC76850.1
    AP009048 Genomic DNA Translation: BAE77456.1
    X52837 Genomic DNA No translation available.
    PIRiH65189
    RefSeqiNP_418289.1, NC_000913.3
    WP_000444561.1, NZ_LN832404.1

    Genome annotation databases

    EnsemblBacteriaiAAC76850; AAC76850; b3847
    BAE77456; BAE77456; BAE77456
    GeneIDi948335
    KEGGiecj:JW3823
    eco:b3847
    PATRICifig|1411691.4.peg.2863

    Similar proteinsi

    Entry informationi

    Entry nameiPEPQ_ECOLI
    AccessioniPrimary (citable) accession number: P21165
    Secondary accession number(s): P21176, Q2M8F0
    Entry historyiIntegrated into UniProtKB/Swiss-Prot: May 1, 1991
    Last sequence update: October 1, 1993
    Last modified: March 28, 2018
    This is version 153 of the entry and version 2 of the sequence. See 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

    We'd like to inform you that we have updated our Privacy Notice to comply with Europe’s new General Data Protection Regulation (GDPR) that applies since 25 May 2018.

    Do not show this banner again
    UniProt is an ELIXIR core data resource
    Main funding by: National Institutes of Health