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UniProtKB/Swiss-Prot entry Q45495


[Entry info] [Name and origin] [References] [Comments] [Cross-references] [Keywords] [Features] [Sequence] [Tools]

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Entry information
Entry name DEF2_BACSU
Primary accession number Q45495
Secondary accession numbers None
Integrated into Swiss-Prot on May 30, 2000
Sequence was last modified on November 1, 1996 (Sequence version 1)
Annotations were last modified on    July 22, 2008 (Entry version 65)
Name and origin of the protein
Protein name Peptide deformylase 2
Synonyms PDF 2
EC 3.5.1.88
Polypeptide deformylase 2
Gene name
Name: defB
Synonyms: ykrB
OrderedLocusNames: BSU14560
From
Bacillus subtilis [TaxID: 1423] [HAMAP proteome]
Taxonomy Bacteria; Firmicutes; Bacillales; Bacillaceae; Bacillus.
Protein existence 1: Evidence at protein level;
References
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
STRAIN=168;
Caldwell R.M., Ferrari E.;
"Sequence analysis of the mobA-ampS region of the Bacillus subtilis chromosome.";
Submitted (JUL-1997) to the EMBL/GenBank/DDBJ databases.
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=168;
DOI=10.1038/36786; PubMed=9384377 [NCBI, ExPASy, EBI, Israel, Japan]
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.;
"The complete genome sequence of the Gram-positive bacterium Bacillus subtilis.";
Nature 390:249-256(1997).
[3]
CHARACTERIZATION.
PubMed=11429456 [NCBI, ExPASy, EBI, Israel, Japan]
Haas M., Beyer D., Gahlmann R., Freiberg C.;
"YkrB is the main peptide deformylase in Bacillus subtilis, a eubacterium containing two functional peptide deformylases.";
Microbiology 147:1783-1791(2001).
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.
  • CATALYTIC ACTIVITY: Formyl-L-methionyl peptide + H2O = formate + methionyl peptide.
  • COFACTOR: Binds 1 Fe(2+) ion (By similarity).
  • SIMILARITY: Belongs to the polypeptide deformylase family.
Copyright
Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.
Cross-references
Sequence databases
EMBL
AF012285; AAC24930.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
Z99111; CAB13329.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
PIR D69862; D69862.
RefSeq NP_389339.1; -.
3D structure databases
HSSP O31410; 1LQY. [HSSP ENTRY / PDB]
ModBase Q45495.
Enzyme and pathway databases
BioCyc BSUB224308:BSU1458-MON; -.
Organism-specific databases
SubtiList BG11815; defB. [Micado]
Ontologies
GO
GO:0042586; Molecular function: peptide deformylase activity (inferred from electronic annotation from HAMAP).
GO:0006412; Biological process: translation (inferred from electronic annotation from HAMAP).
QuickGo view.
Family and domain databases
HAMAP MF_00163; -; 1.
PBIL [Tree]
InterPro IPR000181; Fmet_deformylase.
Graphical view of domain structure.
Gene3D G3DSA:3.90.45.10; Fmet_deformylase; 1.
PANTHER PTHR10458; Fmet_deformylase; 1.
Pfam PF01327; Pep_deformylase; 1.
Pfam graphical view of domain structure.
PIRSF PIRSF004749; Pep_def; 1.
PRINTS PR01576; PDEFORMYLASE.
ProDom PD003844; Fmet_deformylase; 1.
[Domain structure / List of seq. sharing at least 1 domain]
TIGRFAMs TIGR00079; pept_deformyl; 1.
BLOCKS Q45495.
Genome annotation databases
GeneID 939491; -.
GenomeReviews AL009126_GR; BSU14560.
KEGG bsu:BSU14560; -.
NMPDR fig|224308.1.peg.1458; -.
Phylogenomic databases
HOGENOM Q45495; -.
Genome annotation databases
CMR Q45495; BSU14560.
Other
ProtoNet Q45495.
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
Complete proteome; Hydrolase; Iron; Metal-binding; Protein biosynthesis.
Features
SEVIEWER logo Feature table viewer
KeyFrom   To Length Description FTId
CHAIN   1   184  184     Peptide deformylase 2. PRO_0000082740
ACT_SITE   154   154        By similarity. 
METAL   110   110        Iron (By similarity). 
METAL   153   153        Iron (By similarity). 
METAL   157   157        Iron (By similarity). 
Sequence information
Length: 184 AA [This is the length of the unprocessed precursor] Molecular weight: 20656 Da [This is the MW of the unprocessed precursor] CRC64: 8641BF1932666C38 [This is a checksum on the sequence]
        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 

Q45495 in FASTA format

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