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Q9F2F0

- DEF_STRPN

UniProt

Q9F2F0 - DEF_STRPN

Protein

Peptide deformylase

Gene

def

Organism
Streptococcus pneumoniae serotype 4 (strain ATCC BAA-334 / TIGR4)
Status
Reviewed - Annotation score: 2 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 97 (01 Oct 2014)
      Sequence version 1 (01 Mar 2001)
      Previous versions | rss
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    Functioni

    Removes the formyl group from the N-terminal Met of newly synthesized proteins. Requires at least a dipeptide for an efficient rate of reaction. N-terminal L-methionine is a prerequisite for activity but the enzyme has broad specificity at other positions.UniRule annotation

    Catalytic activityi

    Formyl-L-methionyl peptide + H2O = formate + methionyl peptide.UniRule annotation

    Cofactori

    Binds 1 Fe2+ ion.UniRule annotation

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Metal bindingi130 – 1301IronUniRule annotation
    Metal bindingi173 – 1731IronUniRule annotation
    Active sitei174 – 1741UniRule annotation
    Metal bindingi177 – 1771IronUniRule annotation

    GO - Molecular functioni

    1. iron ion binding Source: InterPro
    2. peptide deformylase activity Source: UniProtKB-HAMAP

    GO - Biological processi

    1. translation Source: UniProtKB-HAMAP

    Keywords - Molecular functioni

    Hydrolase

    Keywords - Biological processi

    Protein biosynthesis

    Keywords - Ligandi

    Iron, Metal-binding

    Enzyme and pathway databases

    BioCyciSPNE170187:GHGN-1462-MONOMER.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Peptide deformylaseUniRule annotation (EC:3.5.1.88UniRule annotation)
    Short name:
    PDFUniRule annotation
    Alternative name(s):
    Polypeptide deformylaseUniRule annotation
    Gene namesi
    Name:defUniRule annotation
    Ordered Locus Names:SP_1456
    OrganismiStreptococcus pneumoniae serotype 4 (strain ATCC BAA-334 / TIGR4)
    Taxonomic identifieri170187 [NCBI]
    Taxonomic lineageiBacteriaFirmicutesBacilliLactobacillalesStreptococcaceaeStreptococcus
    ProteomesiUP000000585: Chromosome

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 203203Peptide deformylasePRO_0000082857Add
    BLAST

    Interactioni

    Protein-protein interaction databases

    STRINGi170187.SP_1456.

    Structurei

    Secondary structure

    1
    203
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Helixi3 – 75
    Helixi16 – 183
    Helixi25 – 284
    Helixi40 – 5617
    Helixi59 – 657
    Beta strandi71 – 744
    Helixi75 – 784
    Beta strandi82 – 898
    Beta strandi105 – 11713
    Beta strandi119 – 1246
    Beta strandi143 – 1453
    Beta strandi147 – 1526
    Beta strandi158 – 1636
    Helixi165 – 17814
    Helixi183 – 1864
    Beta strandi199 – 2024

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1LM6X-ray1.75A1-203[»]
    ProteinModelPortaliQ9F2F0.
    SMRiQ9F2F0. Positions 2-203.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiQ9F2F0.

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the polypeptide deformylase family.UniRule annotation

    Phylogenomic databases

    eggNOGiCOG0242.
    HOGENOMiHOG000243507.
    KOiK01462.
    OMAiHIDKENP.
    OrthoDBiEOG6PZXGQ.

    Family and domain databases

    Gene3Di3.90.45.10. 1 hit.
    HAMAPiMF_00163. Pep_deformylase.
    InterProiIPR000181. Fmet_deformylase.
    IPR023635. Peptide_deformylase.
    [Graphical view]
    PANTHERiPTHR10458. PTHR10458. 1 hit.
    PfamiPF01327. Pep_deformylase. 1 hit.
    [Graphical view]
    PIRSFiPIRSF004749. Pep_def. 1 hit.
    PRINTSiPR01576. PDEFORMYLASE.
    SUPFAMiSSF56420. SSF56420. 1 hit.
    TIGRFAMsiTIGR00079. pept_deformyl. 1 hit.

    Sequencei

    Sequence statusi: Complete.

    Q9F2F0-1 [UniParc]FASTAAdd to Basket

    « Hide

    MSAIERITKA AHLIDMNDII REGNPTLRAI AEEVTFPLSD QEIILGEKMM    50
    QFLKHSQDPV MAEKMGLRGG VGLAAPQLDI SKRIIAVLVP NIVEEGETPQ 100
    EAYDLEAIMY NPKIVSHSVQ DAALGEGEGC LSVDRNVPGY VVRHARVTVD 150
    YFDKDGEKHR IKLKGYNSIV VQHEIDHING IMFYDRINEK DPFAVKDGLL 200
    ILE 203
    Length:203
    Mass (Da):22,676
    Last modified:March 1, 2001 - v1
    Checksum:i192F91B42375F8CD
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AJ278785 Genomic DNA. Translation: CAC15392.1.
    AE005672 Genomic DNA. Translation: AAK75550.1.
    PIRiE95169.
    RefSeqiNP_345910.1. NC_003028.3.
    WP_001272941.1. NZ_AKVY01000001.1.

    Genome annotation databases

    EnsemblBacteriaiAAK75550; AAK75550; SP_1456.
    GeneIDi931384.
    KEGGispn:SP_1456.
    PATRICi19707331. VBIStrPne105772_1508.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AJ278785 Genomic DNA. Translation: CAC15392.1 .
    AE005672 Genomic DNA. Translation: AAK75550.1 .
    PIRi E95169.
    RefSeqi NP_345910.1. NC_003028.3.
    WP_001272941.1. NZ_AKVY01000001.1.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1LM6 X-ray 1.75 A 1-203 [» ]
    ProteinModelPortali Q9F2F0.
    SMRi Q9F2F0. Positions 2-203.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    STRINGi 170187.SP_1456.

    Chemistry

    ChEMBLi CHEMBL2029196.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblBacteriai AAK75550 ; AAK75550 ; SP_1456 .
    GeneIDi 931384.
    KEGGi spn:SP_1456.
    PATRICi 19707331. VBIStrPne105772_1508.

    Phylogenomic databases

    eggNOGi COG0242.
    HOGENOMi HOG000243507.
    KOi K01462.
    OMAi HIDKENP.
    OrthoDBi EOG6PZXGQ.

    Enzyme and pathway databases

    BioCyci SPNE170187:GHGN-1462-MONOMER.

    Miscellaneous databases

    EvolutionaryTracei Q9F2F0.

    Family and domain databases

    Gene3Di 3.90.45.10. 1 hit.
    HAMAPi MF_00163. Pep_deformylase.
    InterProi IPR000181. Fmet_deformylase.
    IPR023635. Peptide_deformylase.
    [Graphical view ]
    PANTHERi PTHR10458. PTHR10458. 1 hit.
    Pfami PF01327. Pep_deformylase. 1 hit.
    [Graphical view ]
    PIRSFi PIRSF004749. Pep_def. 1 hit.
    PRINTSi PR01576. PDEFORMYLASE.
    SUPFAMi SSF56420. SSF56420. 1 hit.
    TIGRFAMsi TIGR00079. pept_deformyl. 1 hit.
    ProtoNeti Search...

    Publicationsi

    1. "Peptide deformylase as an antibacterial drug target: target validation and resistance development."
      Apfel C.M., Locher H., Evers S., Takacs B., Hubschwerlen C., Pirson W., Page M.G., Keck W.
      Antimicrob. Agents Chemother. 45:1058-1064(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    2. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: ATCC BAA-334 / TIGR4.

    Entry informationi

    Entry nameiDEF_STRPN
    AccessioniPrimary (citable) accession number: Q9F2F0
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: December 5, 2001
    Last sequence update: March 1, 2001
    Last modified: October 1, 2014
    This is version 97 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programProkaryotic Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    3D-structure, Complete proteome

    Documents

    1. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    2. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3