Skip Header

 
Contribute Send feedback

Reviewed, UniProtKB/Swiss-Prot Q45495 (DEF2_BACSU)

Last modified November 25, 2008. Version 66. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

Hide | Top

Names and origin

Protein namesRecommended name:
    Peptide deformylase 2
      Short name=PDF 2
    EC=3.5.1.88
Alternative name(s):
    Polypeptide deformylase 2
Gene names
Name: defB
Synonyms: ykrB
Ordered Locus Names: BSU14560
OrganismBacillus subtilis [Complete proteome] [HAMAP]
Taxonomic identifier1423 [NCBI]
Taxonomic lineageBacteria › Firmicutes › Bacillales › Bacillaceae › Bacillus

Hide | Top

Protein attributes

Sequence length184 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is not processed.
Protein existenceEvidence at protein level.

Hide | Top

General annotation (Comments)

Function

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. HAMAP MF_00163

Catalytic activity

Formyl-L-methionyl peptide + H(2)O = formate + methionyl peptide. HAMAP MF_00163

Cofactor

Binds 1 Fe(2+) ion By similarity.

Sequence similarities

Belongs to the polypeptide deformylase family.

Hide | Top

Ontologies

Keywords

   Biological processProtein biosynthesis
   LigandIron
Metal-binding
   Molecular functionHydrolase
   Technical termComplete proteome

Gene Ontology (GO)

   Biological processtranslation

Inferred from electronic annotation. Source: HAMAP

   Molecular functioniron ion binding

Inferred from electronic annotation. Source: InterPro

peptide deformylase activity

Inferred from electronic annotation. Source: HAMAP

Complete GO annotation...

Hide | Top

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 184184Peptide deformylase 2 HAMAP MF_00163
PRO_0000082740

Sites

Active site1541 By similarity
Metal binding1101Iron By similarity
Metal binding1531Iron By similarity
Metal binding1571Iron By similarity

Hide | Top

Sequences

Sequence LengthMass (Da)Tools
Q45495-1 [UniParc].

Last modified November 1, 1996. Version 1.
Checksum: 8641BF1932666C38

FASTA18420,656
        10         20         30         40         50         60 
MITMENIVRD GHPALRETAE PVELPPTDAE KQQLADMIEF VKNSQNPELA EKYKLRPGVG 

        70         80         90        100        110        120 
LAAPQINIKK RMIAVHAEDA SGKLYSYALF NPKIVSHSVE KSYLTSGEGC LSVDEAIPGY 

       130        140        150        160        170        180 
VPRYARIRVK GTTLEGENID IRLKGFPAIV FQHEIDHLNG VMFYDHIDKE NPFKEPENAI 


AIER

« Hide

Hide | Top

References

« Hide 'large scale' references
[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. expand/collapse author list , 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: 9384377] [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: 11429456] [Abstract]
Cited for: CHARACTERIZATION.

Hide | Top

Cross-references

Sequence databases

AF012285 Genomic DNA. Translation: AAC24930.1.
Z99111 Genomic DNA. Translation: CAB13329.1.
PIRD69862.
RefSeqNP_389339.1.

3D structure databases

HSSPHSSP built from PDB template 1LQY based on UniProtKB O31410.
ModBaseSearch...

Genome annotation databases

GeneID939491.
GenomeReviewsGene locus BSU14560 in contig AL009126_GR.
KEGGbsu:BSU14560.
NMPDRfig|224308.1.peg.1458.

Organism-specific databases

SubtiListBG11815. defB. [Micado]
CMRSearch...

Phylogenomic databases

HOGENOMQ45495.

Enzyme and pathway databases

BioCycBSUB224308:BSU1458-MON.

Family and domain databases

HAMAPMF_00163.
[Tree]
InterProIPR000181. Fmet_deformylase.
[Graphical view]
Gene3DG3DSA:3.90.45.10. Fmet_deformylase. 1 hit.
PANTHERPTHR10458. Fmet_deformylase. 1 hit.
PfamPF01327. Pep_deformylase. 1 hit.
[Graphical view]
PIRSFPIRSF004749. Pep_def. 1 hit.
PRINTSPR01576. PDEFORMYLASE.
ProDomPD003844. Fmet_deformylase. 1 hit.
[Graphical view] [Entries sharing at least one domain]
TIGRFAMsTIGR00079. pept_deformyl. 1 hit.
ProtoNetSearch...

Hide | Top

Entry information

Entry nameDEF2_BACSU
AccessionPrimary (citable) accession number: Q45495
Entry history
Integrated into UniProtKB/Swiss-Prot: May 30, 2000
Last sequence update: November 1, 1996
Last modified: November 25, 2008
This is version 66 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHAMAP (High-quality Automated and Manual Annotation of microbial Proteomes)

Hide | Top

Relevant documents

Bacillus subtilis

Bacillus subtilis (strain 168): entries, gene names and cross-references to SubtiList

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents