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)

Q45495

- DEF2_BACSU

UniProt

Q45495 - DEF2_BACSU

Protein

Peptide deformylase 2

Gene

defB

Organism
Bacillus subtilis (strain 168)
Status
Reviewed - Annotation score: 3 out of 5- Experimental evidence at protein leveli
    • BLAST
    • Align
    • Format
    • Add to basket
    • History
      Entry version 105 (01 Oct 2014)
      Sequence version 1 (01 Nov 1996)
      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.

    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 bindingi110 – 1101IronBy similarity
    Metal bindingi153 – 1531IronBy similarity
    Active sitei154 – 1541By similarity
    Metal bindingi157 – 1571IronBy similarity

    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

    BioCyciBSUB:BSU14560-MONOMER.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Peptide deformylase 2 (EC:3.5.1.88)
    Short name:
    PDF 2
    Alternative name(s):
    Polypeptide deformylase 2
    Gene namesi
    Name:defB
    Synonyms:ykrB
    Ordered Locus Names:BSU14560
    OrganismiBacillus subtilis (strain 168)
    Taxonomic identifieri224308 [NCBI]
    Taxonomic lineageiBacteriaFirmicutesBacilliBacillalesBacillaceaeBacillus
    ProteomesiUP000001570: Chromosome

    Organism-specific databases

    GenoListiBSU14560. [Micado]

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 184184Peptide deformylase 2PRO_0000082740Add
    BLAST

    Proteomic databases

    PaxDbiQ45495.

    Interactioni

    Protein-protein interaction databases

    STRINGi224308.BSU14560.

    Structurei

    3D structure databases

    ProteinModelPortaliQ45495.
    SMRiQ45495. Positions 1-184.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the polypeptide deformylase family.Curated

    Phylogenomic databases

    eggNOGiCOG0242.
    HOGENOMiHOG000243507.
    KOiK01462.
    OMAiHIDKENP.
    OrthoDBiEOG6PZXGQ.
    PhylomeDBiQ45495.

    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.

    Q45495-1 [UniParc]FASTAAdd to Basket

    « Hide

    MITMENIVRD GHPALRETAE PVELPPTDAE KQQLADMIEF VKNSQNPELA    50
    EKYKLRPGVG LAAPQINIKK RMIAVHAEDA SGKLYSYALF NPKIVSHSVE 100
    KSYLTSGEGC LSVDEAIPGY VPRYARIRVK GTTLEGENID IRLKGFPAIV 150
    FQHEIDHLNG VMFYDHIDKE NPFKEPENAI AIER 184
    Length:184
    Mass (Da):20,656
    Last modified:November 1, 1996 - v1
    Checksum:i8641BF1932666C38
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF012285 Genomic DNA. Translation: AAC24930.1.
    AL009126 Genomic DNA. Translation: CAB13329.1.
    PIRiD69862.
    RefSeqiNP_389339.1. NC_000964.3.

    Genome annotation databases

    EnsemblBacteriaiCAB13329; CAB13329; BSU14560.
    GeneIDi939491.
    KEGGibsu:BSU14560.
    PATRICi18974703. VBIBacSub10457_1543.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF012285 Genomic DNA. Translation: AAC24930.1 .
    AL009126 Genomic DNA. Translation: CAB13329.1 .
    PIRi D69862.
    RefSeqi NP_389339.1. NC_000964.3.

    3D structure databases

    ProteinModelPortali Q45495.
    SMRi Q45495. Positions 1-184.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    STRINGi 224308.BSU14560.

    Proteomic databases

    PaxDbi Q45495.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblBacteriai CAB13329 ; CAB13329 ; BSU14560 .
    GeneIDi 939491.
    KEGGi bsu:BSU14560.
    PATRICi 18974703. VBIBacSub10457_1543.

    Organism-specific databases

    GenoListi BSU14560. [Micado ]

    Phylogenomic databases

    eggNOGi COG0242.
    HOGENOMi HOG000243507.
    KOi K01462.
    OMAi HIDKENP.
    OrthoDBi EOG6PZXGQ.
    PhylomeDBi Q45495.

    Enzyme and pathway databases

    BioCyci BSUB:BSU14560-MONOMER.

    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. "Sequence analysis of the mobA-ampS region of the Bacillus subtilis chromosome."
      Caldwell R.M., Ferrari E.
      Submitted (JUL-1997) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
      Strain: 168.
    2. "The complete genome sequence of the Gram-positive bacterium Bacillus subtilis."
      Kunst F., Ogasawara N., Moszer I., Albertini A.M., Alloni G., Azevedo V., Bertero M.G., Bessieres P., Bolotin A., Borchert S., Borriss R., Boursier L., Brans A., Braun M., Brignell S.C., Bron S., Brouillet S., Bruschi C.V.
      , Caldwell B., Capuano V., Carter N.M., Choi S.-K., Codani J.-J., Connerton I.F., Cummings N.J., Daniel R.A., Denizot F., Devine K.M., Duesterhoeft A., Ehrlich S.D., Emmerson P.T., Entian K.-D., Errington J., Fabret C., Ferrari E., Foulger D., Fritz C., Fujita M., Fujita Y., Fuma S., Galizzi A., Galleron N., Ghim S.-Y., Glaser P., Goffeau A., Golightly E.J., Grandi G., Guiseppi G., Guy B.J., Haga K., Haiech J., Harwood C.R., Henaut A., Hilbert H., Holsappel S., Hosono S., Hullo M.-F., Itaya M., Jones L.-M., Joris B., Karamata D., Kasahara Y., Klaerr-Blanchard M., Klein C., Kobayashi Y., Koetter P., Koningstein G., Krogh S., Kumano M., Kurita K., Lapidus A., Lardinois S., Lauber J., Lazarevic V., Lee S.-M., Levine A., Liu H., Masuda S., Mauel C., Medigue C., Medina N., Mellado R.P., Mizuno M., Moestl D., Nakai S., Noback M., Noone D., O'Reilly M., Ogawa K., Ogiwara A., Oudega B., Park S.-H., Parro V., Pohl T.M., Portetelle D., Porwollik S., Prescott A.M., Presecan E., Pujic P., Purnelle B., Rapoport G., Rey M., Reynolds S., Rieger M., Rivolta C., Rocha E., Roche B., Rose M., Sadaie Y., Sato T., Scanlan E., Schleich S., Schroeter R., Scoffone F., Sekiguchi J., Sekowska A., Seror S.J., Serror P., Shin B.-S., Soldo B., Sorokin A., Tacconi E., Takagi T., Takahashi H., Takemaru K., Takeuchi M., Tamakoshi A., Tanaka T., Terpstra P., Tognoni A., Tosato V., Uchiyama S., Vandenbol M., Vannier F., Vassarotti A., Viari A., Wambutt R., Wedler E., Wedler H., Weitzenegger T., Winters P., Wipat A., Yamamoto H., Yamane K., Yasumoto K., Yata K., Yoshida K., Yoshikawa H.-F., Zumstein E., Yoshikawa H., Danchin A.
      Nature 390:249-256(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: 168.
    3. "YkrB is the main peptide deformylase in Bacillus subtilis, a eubacterium containing two functional peptide deformylases."
      Haas M., Beyer D., Gahlmann R., Freiberg C.
      Microbiology 147:1783-1791(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: CHARACTERIZATION.

    Entry informationi

    Entry nameiDEF2_BACSU
    AccessioniPrimary (citable) accession number: Q45495
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: May 30, 2000
    Last sequence update: November 1, 1996
    Last modified: October 1, 2014
    This is version 105 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

    Complete proteome, Reference proteome

    Documents

    1. Bacillus subtilis
      Bacillus subtilis (strain 168): entries, gene names and cross-references to SubtiList
    2. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3