Q0P9K4 (DAPE_CAMJE) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Succinyl-diaminopimelate desuccinylase
Short name=SDAP desuccinylase
EC=3.5.1.18

Alternative name(s):
N-succinyl-LL-2,6-diaminoheptanedioate amidohydrolase

Gene names

Name:	dapE
Ordered Locus Names:	Cj1048c

Organism

Campylobacter jejuni

Taxonomic identifier

197 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Epsilonproteobacteria › Campylobacterales › Campylobacteraceae › Campylobacter

Protein attributes

Sequence length	365 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Catalyzes the hydrolysis of N-succinyl-L,L-diaminopimelic acid (SDAP), forming succinate and LL-2,6-diaminoheptanedioate (DAP), an intermediate involved in the bacterial biosynthesis of lysine and meso-diaminopimelic acid, an essential component of bacterial cell walls By similarity. HAMAP MF_01690
Catalytic activity	N-succinyl-LL-2,6-diaminoheptanedioate + H2O = succinate + LL-2,6-diaminoheptanedioate. HAMAP MF_01690
Cofactor	Binds 1 Zn2+ ion per subunit By similarity. HAMAP MF_01690 Binds 1 Co2+ ion per subunit By similarity. HAMAP MF_01690
Pathway	Amino-acid biosynthesis; L-lysine biosynthesis via DAP pathway; LL-2,6-diaminopimelate from (S)-tetrahydrodipicolinate (succinylase route): step 3/3. HAMAP MF_01690
Subunit structure	Homodimer By similarity. HAMAP MF_01690
Sequence similarities	Belongs to the peptidase M20A family. DapE subfamily.

Ontologies

Keywords
Biological process	Amino-acid biosynthesis Diaminopimelate biosynthesis Lysine biosynthesis
Ligand	Cobalt Metal-binding Zinc
Molecular function	Hydrolase
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological process	diaminopimelate biosynthetic process Inferred from electronic annotation. Source: UniProtKB-KW proteolysis Inferred from electronic annotation. Source: InterPro
Molecular function	metal ion binding Inferred from electronic annotation. Source: UniProtKB-KW metallopeptidase activity Inferred from electronic annotation. Source: InterPro succinyl-diaminopimelate desuccinylase activity Inferred from electronic annotation. Source: EC
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
flaG	Q0PAW9	1	EBI-1194342,EBI-1191365
fliG	Q0PBJ0	1	EBI-1194342,EBI-1191336

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 365	365	Succinyl-diaminopimelate desuccinylase HAMAP MF_01690		PRO_0000375520
Sites
	Active site	67	1	By similarity
	Active site	126	1	Proton acceptor By similarity
	Metal binding	65	1	Cobalt or zinc 1 By similarity
	Metal binding	96	1	Cobalt or zinc 1 By similarity
	Metal binding	96	1	Cobalt or zinc 2 By similarity
	Metal binding	127	1	Cobalt or zinc 2 By similarity
	Metal binding	155	1	Cobalt or zinc 1 By similarity
	Metal binding	340	1	Cobalt or zinc 2 By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q0P9K4 [UniParc]. Last modified September 19, 2006. Version 1. Checksum: AE85159CDF09CB7E	FASTA	365	40,457
	10 20 30 40 50 60 MNAKEFLIEL LKFKSVTPND DGALNFIAME LSDFEAFFIE KEGIKNLLLT KKFKDEGEHL 70 80 90 100 110 120 AFGGHVDVVP AGEGWSNNAF APVEKEGFIY ARGAQDMKSG VAAFVDAAKN ADFKGARLSL 130 140 150 160 170 180 ILTSDEEGEA IYGTKAVLEW MQERDMLPDY AVVAEPTCVK KIGDSIKIGR RGSINGKLLI 190 200 210 220 230 240 RGKQGHVAYP EKCINPVHDF APVLKLLAGF DLDPGSAEFS PSKIVITDIR GGMGVCNVTP 250 260 270 280 290 300 NDLKLMFNVR NSPDTSLEDV KSYVEKICHG LNYELELKQS SEAFLTNIDN KIVQKMNESV 310 320 330 340 350 360 QKITHEVPEL NTKGGTSDAR YFAKYGVKVV EFGVCNDRIH AIDERVSIEE FEKLCLVFKD LIENF

References

[1]

"The genome sequence of the food-borne pathogen Campylobacter jejuni reveals hypervariable sequences." Parkhill J., Wren B.W., Mungall K.L., Ketley J.M., Churcher C.M., Basham D., Chillingworth T., Davies R.M., Feltwell T., Holroyd S., Jagels K., Karlyshev A.V., Moule S., Pallen M.J., Penn C.W., Quail M.A., Rajandream M.A., Rutherford K.M. , van Vliet A.H.M., Whitehead S., Barrell B.G. Nature 403:665-668(2000) [PubMed: 10688204] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: NCTC 11168 / Serotype O:2.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AL111168 Genomic DNA. Translation: CAL35166.1.
PIR	E81307.
RefSeq	YP_002344443.1. NC_002163.1.
3D structure databases
ProteinModelPortal	Q0P9K4.
ModBase	Search...
Protein-protein interaction databases
IntAct	Q0P9K4. 34 interactions.
Protein family/group databases
MEROPS	M20.010.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
GeneID	905340.
GenomeReviews	Gene locus Cj1048c in contig AL111168_GR.
KEGG	cje:Cj1048c.
PATRIC	20059054. VBICamJej33762_1030.
Phylogenomic databases
HOGENOM	HBG728841.
OMA	ARNPVHQ.
ProtClustDB	PRK13009.
Enzyme and pathway databases
BioCyc	CJEJ192222:CJ1048C-MONOMER.
Family and domain databases
HAMAP	MF_01690. DapE. [Tree]
InterPro	IPR001261. ArgE/DapE_CS. IPR005941. DapE_proteobac. IPR002933. Peptidase_M20. IPR011650. Peptidase_M20_dimer. [Graphical view]
KO	K01439.
Pfam	PF07687. M20_dimer. 1 hit. PF01546. Peptidase_M20. 1 hit. [Graphical view]
SUPFAM	SSF55031. Peptidase_M20_dimer. 1 hit.
TIGRFAMs	TIGR01246. DapE_proteo. 1 hit.
PROSITE	PS00758. ARGE_DAPE_CPG2_1. 1 hit. PS00759. ARGE_DAPE_CPG2_2. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

DAPE_CAMJE

Accession

Primary (citable) accession number: Q0P9K4

Entry history

Integrated into UniProtKB/Swiss-Prot:	May 26, 2009
Last sequence update:	September 19, 2006
Last modified:	January 25, 2012
This is version 41 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program