Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Basket 0
(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

P68826

- DEF_STAAU

UniProt

P68826 - DEF_STAAU

Protein

Peptide deformylase

Gene

def

Organism
Staphylococcus aureus
Status
Reviewed - Annotation score: 3 out of 5- Experimental evidence at protein leveli
    • BLAST
    • Align
    • Format
    • Add to basket
    • History
      Entry version 52 (01 Oct 2014)
      Sequence version 1 (21 Dec 2004)
      Previous versions | rss
    • Help video
    • Feedback
    • Comment

    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 By similarity.By similarity

    Catalytic activityi

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

    Cofactori

    Binds 1 Fe2+ ion.By similarity

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Metal bindingi111 – 1111Iron
    Metal bindingi154 – 1541Iron
    Active sitei155 – 1551By similarity
    Metal bindingi158 – 1581Iron

    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

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Peptide deformylase (EC:3.5.1.88)
    Short name:
    PDF
    Alternative name(s):
    Polypeptide deformylase
    Gene namesi
    Name:def
    Synonyms:def1, pdf1
    OrganismiStaphylococcus aureus
    Taxonomic identifieri1280 [NCBI]
    Taxonomic lineageiBacteriaFirmicutesBacilliBacillalesStaphylococcus

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 183183Peptide deformylasePRO_0000082843Add
    BLAST

    Proteomic databases

    PRIDEiP68826.

    Interactioni

    Structurei

    Secondary structure

    1
    183
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Helixi4 – 63
    Helixi13 – 164
    Helixi28 – 4518
    Helixi47 – 537
    Beta strandi58 – 625
    Helixi63 – 664
    Beta strandi70 – 778
    Beta strandi81 – 833
    Beta strandi86 – 9813
    Beta strandi100 – 1045
    Beta strandi124 – 13310
    Beta strandi139 – 1457
    Helixi146 – 15914
    Helixi164 – 1674
    Beta strandi170 – 1723

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1LM4X-ray1.45A/B1-183[»]
    1LMHX-ray1.90A1-183[»]
    1LQWX-ray1.87A/B1-183[»]
    1Q1YX-ray1.90A1-183[»]
    2AI9X-ray2.50A/B1-183[»]
    ProteinModelPortaliP68826.
    SMRiP68826. Positions 1-183.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP68826.

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the polypeptide deformylase family.Curated

    Phylogenomic databases

    eggNOGiCOG0242.

    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.

    P68826-1 [UniParc]FASTAAdd to Basket

    « Hide

    MLTMKDIIRD GHPTLRQKAA ELELPLTKEE KETLIAMREF LVNSQDEEIA    50
    KRYGLRSGVG LAAPQINISK RMIAVLIPDD GSGKSYDYML VNPKIVSHSV 100
    QEAYLPTGEG CLSVDDNVAG LVHRHNRITI KAKDIEGNDI QLRLKGYPAI 150
    VFQHEIDHLN GVMFYDHIDK NHPLQPHTDA VEV 183
    Length:183
    Mass (Da):20,559
    Last modified:December 21, 2004 - v1
    Checksum:i32A64066A6FEAB0E
    GO

    Mass spectrometryi

    Molecular mass is 20600 Da from positions 1 - 183. Determined by MALDI. 1 Publication

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AY007227 Genomic DNA. Translation: AAG02249.1.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AY007227 Genomic DNA. Translation: AAG02249.1 .

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1LM4 X-ray 1.45 A/B 1-183 [» ]
    1LMH X-ray 1.90 A 1-183 [» ]
    1LQW X-ray 1.87 A/B 1-183 [» ]
    1Q1Y X-ray 1.90 A 1-183 [» ]
    2AI9 X-ray 2.50 A/B 1-183 [» ]
    ProteinModelPortali P68826.
    SMRi P68826. Positions 1-183.
    ModBasei Search...
    MobiDBi Search...

    Chemistry

    BindingDBi P68826.
    ChEMBLi CHEMBL2010635.

    Proteomic databases

    PRIDEi P68826.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Phylogenomic databases

    eggNOGi COG0242.

    Miscellaneous databases

    EvolutionaryTracei P68826.

    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. "Staphylococcus aureus deformylase 1 encoding DNA."
      Lonetto M.A., Sylvester D.R., Warren R.L.
      Submitted (AUG-2000) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
      Strain: WCUH29 / NCIMB 40771.
    2. "Identification of Staphylococcus aureus proteins recognized by the antibody-mediated immune response to a biofilm infection."
      Brady R.A., Leid J.G., Camper A.K., Costerton J.W., Shirtliff M.E.
      Infect. Immun. 74:3415-3426(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: MASS SPECTROMETRY.
      Strain: MRSA-M2.
    3. "Structure analysis of peptide deformylases from Streptococcus pneumoniae, Staphylococcus aureus, Thermotoga maritima and Pseudomonas aeruginosa: snapshots of the oxygen sensitivity of peptide deformylase."
      Kreusch A., Spraggon G., Lee C.C., Klock H., McMullan D., Ng K., Shin T., Vincent J., Warner I., Ericson C., Lesley S.A.
      J. Mol. Biol. 330:309-321(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (1.45 ANGSTROMS).

    Entry informationi

    Entry nameiDEF_STAAU
    AccessioniPrimary (citable) accession number: P68826
    Secondary accession number(s): Q9F4L4
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: December 21, 2004
    Last sequence update: December 21, 2004
    Last modified: October 1, 2014
    This is version 52 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

    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