Reviewed, UniProtKB/Swiss-Prot P0AED7 (DAPE_ECOLI)

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
Synonyms:	msgB
Ordered Locus Names:	b2472, JW2456

Organism

Escherichia coli (strain K12) [Complete proteome] [HAMAP]

Taxonomic identifier

83333 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Gammaproteobacteria › Enterobacteriales › Enterobacteriaceae › Escherichia

Protein attributes

Sequence length	375 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
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.
Catalytic activity	N-succinyl-LL-2,6-diaminoheptanedioate + H2O = succinate + LL-2,6-diaminoheptanedioate.
Cofactor	Binds 1 Zn2+ ion per subunit. Binds 1 Co2+ ion per subunit.
Pathway	Amino-acid biosynthesis; L-lysine biosynthesis via DAP pathway; LL-diaminopimelate from tetrahydrodipicolinate (succinylase route): step 3/3.
Subunit structure	Homodimer.
Miscellaneous	DapE/msgB is a multicopy suppressor of a temperature-sensitive allele of the heat shock gene grpE.
Sequence similarities	Belongs to the peptidase M20A family. DapE subfamily.
Biophysicochemical properties	Kinetic parameters: KM=0.41 mM for L,L-SDAP (in the presence of Zn2+ at pH 7.0)

Ontologies

Keywords
Biological process	Amino-acid biosynthesis Diaminopimelate biosynthesis Lysine biosynthesis
Ligand	Cobalt Metal-binding Zinc
Molecular function	Hydrolase
Technical term	Complete 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	cobalt ion binding Inferred from electronic annotation. Source: UniProtKB-KW metallopeptidase activity Inferred from electronic annotation. Source: InterPro protein dimerization activity Inferred from electronic annotation. Source: InterPro succinyl-diaminopimelate desuccinylase activity Inferred from electronic annotation. Source: EC zinc ion binding Inferred from electronic annotation. Source: UniProtKB-KW
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
groL	P0A6F5	1	EBI-1129009,EBI-543750
hemX	P09127	1	EBI-1129009,EBI-1128342

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 375	375	Succinyl-diaminopimelate desuccinylase		PRO_0000185261
Sites
	Active site	68	1	By similarity
	Active site	133	1	Proton acceptor By similarity
	Metal binding	66	1	Cobalt or zinc 1 By similarity
	Metal binding	99	1	Cobalt or zinc 1 By similarity
	Metal binding	99	1	Cobalt or zinc 2 By similarity
	Metal binding	134	1	Cobalt or zinc 2 By similarity
	Metal binding	162	1	Cobalt or zinc 1 By similarity
	Metal binding	348	1	Cobalt or zinc 2 By similarity

Sequences

	Sequence		Length	Mass (Da)
	P0AED7-1 [UniParc]. Last modified December 6, 2005. Version 1. Checksum: 181F43D05E88C20E	FASTA	375	41,269
	10 20 30 40 50 60 MSCPVIELTQ QLIRRPSLSP DDAGCQALLI ERLQAIGFTV ERMDFADTQN FWAWRGQGET 70 80 90 100 110 120 LAFAGHTDVV PPGDADRWIN PPFEPTIRDG MLFGRGAADM KGSLAAMVVA AERFVAQHPN 130 140 150 160 170 180 HTGRLAFLIT SDEEASAHNG TVKVVEALMA RNERLDYCLV GEPSSIEVVG DVVKNGRRGS 190 200 210 220 230 240 LTCNLTIHGV QGHVAYPHLA DNPVHRAAPF LNELVAIEWD QGNEFFPATS MQIANIQAGT 250 260 270 280 290 300 GSNNVIPGEL FVQFNFRFST ELTDEMIKAQ VLALLEKHQL RYTVDWWLSG QPFLTARGKL 310 320 330 340 350 360 VDAVVNAVEH YNEIKPQLLT TGGTSDGRFI ARMGAQVVEL GPVNATIHKI NECVNAADLQ 370 LLARMYQRIM EQLVA

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Cloning, characterization, and expression of the dapE gene of Escherichia coli." Bouvier J., Richaud C., Higgins W., Bogler O., Stragier S. J. Bacteriol. 174:5265-5271(1992) [PubMed: 1644752] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: K12.
[2]	"The essential Escherichia coli msgB gene, a multicopy suppressor of a temperature-sensitive allele of the heat shock gene grpE, is identical to dapE." Wu B., Georgopoulos C., Ang D. J. Bacteriol. 174:5258-5264(1992) [PubMed: 1644751] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[3]	"Construction of a contiguous 874-kb sequence of the Escherichia coli-K12 genome corresponding to 50.0-68.8 min on the linkage map and analysis of its sequence features." Yamamoto Y., Aiba H., Baba T., Hayashi K., Inada T., Isono K., Itoh T., Kimura S., Kitagawa M., Makino K., Miki T., Mitsuhashi N., Mizobuchi K., Mori H., Nakade S., Nakamura Y., Nashimoto H., Oshima T. , Oyama S., Saito N., Sampei G., Satoh Y., Sivasundaram S., Tagami H., Takahashi H., Takeda J., Takemoto K., Uehara K., Wada C., Yamagata S., Horiuchi T. DNA Res. 4:91-113(1997) [PubMed: 9205837] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
[4]	"The complete genome sequence of Escherichia coli K-12." Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V., Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F., Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B., Shao Y. Science 277:1453-1474(1997) [PubMed: 9278503] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: K12 / MG1655 / ATCC 47076.
[5]	"Highly accurate genome sequences of Escherichia coli K-12 strains MG1655 and W3110." Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S., Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T. Mol. Syst. Biol. 2:E1-E5(2006) [PubMed: 16738553] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
[6]	"Bacterial N-succinyl-L-diaminopimelic acid desuccinylase. Purification, partial characterization, and substrate specificity." Lin Y.K., Myhrman R., Schrag M.L., Gelb M.H. J. Biol. Chem. 263:1622-1627(1988) [PubMed: 3276674] [Abstract] Cited for: FUNCTION, SUBUNIT, COFACTOR, BIOPHYSICOCHEMICAL PROPERTIES.

Cross-references

Sequence databases
EMBLGenBankDDBJ	S41760 Genomic DNA. Translation: AAB22798.1. X57403 Genomic DNA. Translation: CAA40665.1. U00096 Genomic DNA. Translation: AAC75525.1. AP009048 Genomic DNA. Translation: BAA16346.1.
PIR	A42959.
RefSeq	AP_003057.1. NP_416967.1.
3D structure databases
ModBase	Search...
Protein-protein interaction databases
IntAct	P0AED7. 3 interactions.
Protein family/group databases
MEROPS	M20.010.
Genome annotation databases
GeneID	948313.
GenomeReviews	Gene locus JW2456 in contig AP009048_GR. Gene locus b2472 in contig U00096_GR.
KEGG	ecj:JW2456. eco:b2472.
Organism-specific databases
EchoBASE	EB0204.
EcoGene	EG10208. dapE.
CMR	Search...
Phylogenomic databases
HOGENOM	P0AED7.
OMA	P0AED7. PDHQGSI.
Enzyme and pathway databases
BioCyc	EcoCyc:MON0-1981. MetaCyc:MON0-1981.
Family and domain databases
HAMAP	MF_01690. [Tree]
InterPro	IPR001261. ArgE/DapE_CS. IPR005941. DapE_proteobac. IPR002933. Peptidase_M20. IPR011650. Peptidase_M20_dimer. [Graphical view]
Pfam	PF07687. M20_dimer. 1 hit. PF01546. Peptidase_M20. 1 hit. [Graphical view]
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_ECOLI

Accession

Primary (citable) accession number: P0AED7
Secondary accession number(s): P24176

Entry history

Integrated into UniProtKB/Swiss-Prot:	December 6, 2005
Last sequence update:	December 6, 2005
Last modified:	June 16, 2009
This is version 32 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HAMAP (High-quality Automated and Manual Annotation of microbial Proteomes)