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P68771

- DEF_STRP1

UniProt

P68771 - DEF_STRP1

Protein

Peptide deformylase

Gene

def

Organism
Streptococcus pyogenes serotype M1
Status
Reviewed - Annotation score: 2 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 69 (01 Oct 2014)
      Sequence version 1 (21 Dec 2004)
      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 bindingi131 – 1311IronUniRule annotation
    Metal bindingi174 – 1741IronUniRule annotation
    Active sitei175 – 1751UniRule annotation
    Metal bindingi178 – 1781IronUniRule 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

    BioCyciSPYO160490:GJ81-1613-MONOMER.
    SPYO293653:GHFC-1748-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:SPy_1958, M5005_Spy1669
    OrganismiStreptococcus pyogenes serotype M1
    Taxonomic identifieri301447 [NCBI]
    Taxonomic lineageiBacteriaFirmicutesBacilliLactobacillalesStreptococcaceaeStreptococcus
    ProteomesiUP000000750: Chromosome, UP000002702: Chromosome

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 204204Peptide deformylasePRO_0000082859Add
    BLAST

    Proteomic databases

    PaxDbiP68771.

    Interactioni

    Protein-protein interaction databases

    STRINGi160490.SPy_1958.

    Structurei

    Secondary structure

    1
    204
    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 – 909
    Beta strandi101 – 11818
    Beta strandi120 – 1256
    Beta strandi144 – 15310
    Beta strandi159 – 1646
    Helixi166 – 17813
    Turni179 – 1813
    Helixi184 – 1874
    Beta strandi200 – 2034

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    2OS3X-ray2.26A2-204[»]
    ProteinModelPortaliP68771.
    SMRiP68771. Positions 2-204.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP68771.

    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.

    P68771-1 [UniParc]FASTAAdd to Basket

    « Hide

    MSAQDKLIKP SHLITMDDII REGNPTLRAV AKEVSLPLCD EDILLGEKMM    50
    QFLKHSQDPV MAEKLGLRAG VGLAAPQIDV SKRIIAVLVP NLPDKEGNPP 100
    KEAYSWQEVL YNPKIVSHSV QDAALSDGEG CLSVDRVVEG YVVRHARVTV 150
    DYYDKEGQQH RIKLKGYNAI VVQHEIDHIN GVLFYDRINA KNPFETKEEL 200
    LILD 204
    Length:204
    Mass (Da):22,862
    Last modified:December 21, 2004 - v1
    Checksum:i89F8EDE94D94DC05
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AE004092 Genomic DNA. Translation: AAK34651.1.
    CP000017 Genomic DNA. Translation: AAZ52287.1.
    RefSeqiNP_269930.1. NC_002737.1.
    YP_283032.1. NC_007297.1.

    Genome annotation databases

    EnsemblBacteriaiAAK34651; AAK34651; SPy_1958.
    AAZ52287; AAZ52287; M5005_Spy1669.
    GeneIDi3571223.
    901633.
    KEGGispy:SPy_1958.
    spz:M5005_Spy_1669.
    PATRICi19717319. VBIStrPyo79812_1705.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AE004092 Genomic DNA. Translation: AAK34651.1 .
    CP000017 Genomic DNA. Translation: AAZ52287.1 .
    RefSeqi NP_269930.1. NC_002737.1.
    YP_283032.1. NC_007297.1.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    2OS3 X-ray 2.26 A 2-204 [» ]
    ProteinModelPortali P68771.
    SMRi P68771. Positions 2-204.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    STRINGi 160490.SPy_1958.

    Proteomic databases

    PaxDbi P68771.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblBacteriai AAK34651 ; AAK34651 ; SPy_1958 .
    AAZ52287 ; AAZ52287 ; M5005_Spy1669 .
    GeneIDi 3571223.
    901633.
    KEGGi spy:SPy_1958.
    spz:M5005_Spy_1669.
    PATRICi 19717319. VBIStrPyo79812_1705.

    Phylogenomic databases

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

    Enzyme and pathway databases

    BioCyci SPYO160490:GJ81-1613-MONOMER.
    SPYO293653:GHFC-1748-MONOMER.

    Miscellaneous databases

    EvolutionaryTracei P68771.

    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. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: ATCC 700294 / SF370 / Serotype M1.
    2. "Evolutionary origin and emergence of a highly successful clone of serotype M1 group A Streptococcus involved multiple horizontal gene transfer events."
      Sumby P., Porcella S.F., Madrigal A.G., Barbian K.D., Virtaneva K., Ricklefs S.M., Sturdevant D.E., Graham M.R., Vuopio-Varkila J., Hoe N.P., Musser J.M.
      J. Infect. Dis. 192:771-782(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: ATCC BAA-947 / MGAS5005 / Serotype M1.

    Entry informationi

    Entry nameiDEF_STRP1
    AccessioniPrimary (citable) accession number: P68771
    Secondary accession number(s): P82590, Q48WI8, Q99XY7
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: December 21, 2004
    Last sequence update: December 21, 2004
    Last modified: October 1, 2014
    This is version 69 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, Reference 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