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B0BC67 (DAPF_CHLTB) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 45. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Diaminopimelate epimerase

Short name=DAP epimerase
EC=5.1.1.7
Gene names
Name:dapF
Ordered Locus Names:CTLon_0685
OrganismChlamydia trachomatis serovar L2b (strain UCH-1/proctitis) [Complete proteome] [HAMAP]
Taxonomic identifier471473 [NCBI]
Taxonomic lineageBacteriaChlamydiaeChlamydialesChlamydiaceaeChlamydia/Chlamydophila groupChlamydia

Protein attributes

Sequence length275 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Catalyzes the stereoinversion of LL-2,6-diaminoheptanedioate (L,L-DAP) to meso-diaminoheptanedioate (meso-DAP), a precursor of L-lysine and an essential component of the bacterial peptidoglycan By similarity. HAMAP-Rule MF_00197

Catalytic activity

LL-2,6-diaminoheptanedioate = meso-diaminoheptanedioate. HAMAP-Rule MF_00197

Pathway

Amino-acid biosynthesis; L-lysine biosynthesis via DAP pathway; DL-2,6-diaminopimelate from LL-2,6-diaminopimelate: step 1/1. HAMAP-Rule MF_00197

Subcellular location

Cytoplasm By similarity HAMAP-Rule MF_00197.

Sequence similarities

Belongs to the diaminopimelate epimerase family.

Ontologies

Keywords
   Biological processAmino-acid biosynthesis
Lysine biosynthesis
   Cellular componentCytoplasm
   Molecular functionIsomerase
   PTMDisulfide bond
   Technical termComplete proteome
Gene Ontology (GO)
   Biological_processlysine biosynthetic process via diaminopimelate

Inferred from electronic annotation. Source: UniProtKB-HAMAP

   Cellular_componentcytoplasm

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular_functiondiaminopimelate epimerase activity

Inferred from electronic annotation. Source: UniProtKB-HAMAP

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 275275Diaminopimelate epimerase HAMAP-Rule MF_00197
PRO_1000099227

Regions

Region72 – 743Substrate binding By similarity
Region197 – 1982Substrate binding By similarity
Region208 – 2092Substrate binding By similarity

Sites

Active site721Proton donor/acceptor By similarity
Active site2071Proton donor/acceptor By similarity
Binding site201Substrate By similarity
Binding site451Substrate By similarity
Binding site631Substrate By similarity
Binding site1791Substrate By similarity
Site1471Important for catalytic activity By similarity
Site1971Important for catalytic activity By similarity

Amino acid modifications

Disulfide bond72 ↔ 207 HAMAP-Rule MF_00197

Sequences

Sequence LengthMass (Da)Tools
B0BC67 [UniParc].

Last modified February 26, 2008. Version 1.
Checksum: 38882BBA95327335

FASTA27530,576
        10         20         30         40         50         60 
MGFSSLLTTC RYLLYSGAGN SFILGESMPS LEDVLFLCQE EMVDGFLCVE SSEIADAKLT 

        70         80         90        100        110        120 
VFNSDGSIAS MCGNGLRCAM AHVAQCFGLE DVSIETERGV YQGKFFSMNR VLVDMTLPDW 

       130        140        150        160        170        180 
KKAERKLTHV LPGMPEQVFF IDTGVPHVVV FVSDLSKVPV QEWGSFLRYH EDFAPEGVNV 

       190        200        210        220        230        240 
DFVQRKKDDL LLVYTYERGC ERETLSCGTG MLASALVAAD IFSLGQDFSI AVCSRSRNLI 

       250        260        270 
KIFSEKGKVF LEGPVSLLNR SENFGWLEPK SRRFG 

« Hide

References

[1]"Chlamydia trachomatis: genome sequence analysis of lymphogranuloma venereum isolates."
Thomson N.R., Holden M.T.G., Carder C., Lennard N., Lockey S.J., Marsh P., Skipp P., O'Connor C.D., Goodhead I., Norbertzcak H., Harris B., Ormond D., Rance R., Quail M.A., Parkhill J., Stephens R.S., Clarke I.N.
Genome Res. 18:161-171(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: UCH-1/proctitis.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AM884177 Genomic DNA. Translation: CAP07082.1.
RefSeqYP_001653773.1. NC_010280.2.

3D structure databases

ProteinModelPortalB0BC67.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING471473.CTLon_0685.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaCAP07082; CAP07082; CTLon_0685.
GeneID5858994.
KEGGctl:CTLon_0685.
PATRIC20383033. VBIChlTra68089_0742.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0253.
HOGENOMHOG000220466.
KOK01778.
OMANGLRCVI.
OrthoDBEOG6ND0M5.
ProtClustDBPRK00450.

Enzyme and pathway databases

BioCycCTRA471473:GHJK-719-MONOMER.
UniPathwayUPA00034; UER00025.

Family and domain databases

HAMAPMF_00197. DAP_epimerase.
InterProIPR018510. DAP_epimerase_AS.
IPR001653. DAP_epimerase_DapF.
[Graphical view]
PANTHERPTHR31689:SF0. PTHR31689:SF0. 1 hit.
PfamPF01678. DAP_epimerase. 2 hits.
[Graphical view]
TIGRFAMsTIGR00652. DapF. 1 hit.
PROSITEPS01326. DAP_EPIMERASE. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameDAPF_CHLTB
AccessionPrimary (citable) accession number: B0BC67
Entry history
Integrated into UniProtKB/Swiss-Prot: March 24, 2009
Last sequence update: February 26, 2008
Last modified: February 19, 2014
This is version 45 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PATHWAY comments

Index of metabolic and biosynthesis pathways