Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

Succinyl-diaminopimelate desuccinylase

Gene

dapE

Organism
Escherichia coli O157:H7 (strain TW14359 / EHEC)
Status
Unreviewed-Annotation score: Annotation score: 3 out of 5-Protein inferred from homologyi

Functioni

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.UniRule annotationSAAS annotation

Catalytic activityi

N-succinyl-LL-2,6-diaminoheptanedioate + H2O = succinate + LL-2,6-diaminoheptanedioate.UniRule annotationSAAS annotation

Cofactori

Protein has several cofactor binding sites:
  • Co2+UniRule annotationNote: Binds 1 Co2+ ion per subunit.UniRule annotation
  • Zn2+UniRule annotationNote: Binds 1 Zn2+ ion per subunit.UniRule annotation

Pathwayi

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi66 – 661Cobalt or zinc 1UniRule annotation
Active sitei68 – 681UniRule annotation
Metal bindingi99 – 991Cobalt or zinc 1UniRule annotation
Metal bindingi99 – 991Cobalt or zinc 2UniRule annotation
Active sitei133 – 1331Proton acceptorUniRule annotation
Metal bindingi134 – 1341Cobalt or zinc 2UniRule annotation
Metal bindingi162 – 1621Cobalt or zinc 1UniRule annotation
Metal bindingi348 – 3481Cobalt or zinc 2UniRule annotation

GO - Molecular functioni

  1. cobalt ion binding Source: UniProtKB-HAMAP
  2. metallopeptidase activity Source: InterPro
  3. succinyl-diaminopimelate desuccinylase activity Source: UniProtKB-HAMAP
  4. zinc ion binding Source: UniProtKB-HAMAP

GO - Biological processi

  1. diaminopimelate biosynthetic process Source: UniProtKB-HAMAP
  2. lysine biosynthetic process via diaminopimelate Source: UniProtKB-HAMAP
Complete GO annotation...

Keywords - Molecular functioni

HydrolaseUniRule annotationSAAS annotation

Keywords - Biological processi

Amino-acid biosynthesis, Diaminopimelate biosynthesisUniRule annotationSAAS annotation, Lysine biosynthesisUniRule annotationSAAS annotation

Keywords - Ligandi

CobaltUniRule annotationSAAS annotation, Metal-bindingUniRule annotationSAAS annotation, ZincUniRule annotationSAAS annotation

Enzyme and pathway databases

BioCyciECOL544404:GKCX-3406-MONOMER.
UniPathwayiUPA00034; UER00021.

Names & Taxonomyi

Protein namesi
Recommended name:
Succinyl-diaminopimelate desuccinylaseUniRule annotationSAAS annotation (EC:3.5.1.18UniRule annotationSAAS annotation)
Short name:
SDAP desuccinylaseUniRule annotation
Alternative name(s):
N-succinyl-LL-2,6-diaminoheptanedioate amidohydrolaseUniRule annotation
Gene namesi
Name:dapEUniRule annotationImported
Ordered Locus Names:ECSP_3410Imported
OrganismiEscherichia coli O157:H7 (strain TW14359 / EHEC)Imported
Taxonomic identifieri544404 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia
ProteomesiUP000002056: Chromosome

Interactioni

Subunit structurei

Homodimer.UniRule annotationSAAS annotation

Protein-protein interaction databases

STRINGi544404.ECSP_3410.

Structurei

3D structure databases

ProteinModelPortaliC6UQ52.
SMRiC6UQ52. Positions 2-374.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the peptidase M20A family. DapE subfamily.UniRule annotation

Phylogenomic databases

eggNOGiCOG0624.
HOGENOMiHOG000243770.
KOiK01439.
OMAiPNDRIHA.
OrthoDBiEOG60651W.

Family and domain databases

Gene3Di3.30.70.360. 1 hit.
HAMAPiMF_01690. DapE.
InterProiIPR001261. ArgE/DapE_CS.
IPR005941. DapE_proteobac.
IPR002933. Peptidase_M20.
IPR011650. Peptidase_M20_dimer.
[Graphical view]
PfamiPF07687. M20_dimer. 1 hit.
PF01546. Peptidase_M20. 1 hit.
[Graphical view]
SUPFAMiSSF55031. SSF55031. 1 hit.
TIGRFAMsiTIGR01246. dapE_proteo. 1 hit.
PROSITEiPS00758. ARGE_DAPE_CPG2_1. 1 hit.
PS00759. ARGE_DAPE_CPG2_2. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

C6UQ52-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MSCPVIELTQ QLIRRPSLSP DDAGCQALLI ERLQAIGFTV ERMDFADTQN
60 70 80 90 100
FWAWRGQGET LAFAGHTDVV PPGDADRWIN PPFEPTIRDG MLFGRGAADM
110 120 130 140 150
KGSLAAMVVA AERFVAQHPN HTGRLAFLIT SDEEASAHNG TVKAVEALMA
160 170 180 190 200
RNERLDYCLV GEPSSIEVVG DVVKNGRRGS LTCNLTIHGV QGHVAYPHLA
210 220 230 240 250
DNPVHRAAPF LNELVAIEWD QGNEFFPATS MQIANIQAGT GSNNVIPGEL
260 270 280 290 300
FVQFNFRFST ELTDEMIKAQ VLALLEKHQL RYTVDWWLSG QPFLTARGKL
310 320 330 340 350
VDAVVNAVEH YNEIKPQLLT TGGTSDGRFI ARMGAQVVEL GPVNATIHKI
360 370
NECVNAADLQ LLARMYQRIM EQLVA
Length:375
Mass (Da):41,241
Last modified:September 22, 2009 - v1
Checksum:iB249E6B09D84F2CA
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CP001368 Genomic DNA. Translation: ACT73177.1.
RefSeqiYP_003079253.1. NC_013008.1.

Genome annotation databases

EnsemblBacteriaiACT73177; ACT73177; ECSP_3410.
GeneIDi8217976.
KEGGietw:ECSP_3410.
PATRICi18390894. VBIEscCol9396_3464.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CP001368 Genomic DNA. Translation: ACT73177.1.
RefSeqiYP_003079253.1. NC_013008.1.

3D structure databases

ProteinModelPortaliC6UQ52.
SMRiC6UQ52. Positions 2-374.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi544404.ECSP_3410.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiACT73177; ACT73177; ECSP_3410.
GeneIDi8217976.
KEGGietw:ECSP_3410.
PATRICi18390894. VBIEscCol9396_3464.

Phylogenomic databases

eggNOGiCOG0624.
HOGENOMiHOG000243770.
KOiK01439.
OMAiPNDRIHA.
OrthoDBiEOG60651W.

Enzyme and pathway databases

UniPathwayiUPA00034; UER00021.
BioCyciECOL544404:GKCX-3406-MONOMER.

Family and domain databases

Gene3Di3.30.70.360. 1 hit.
HAMAPiMF_01690. DapE.
InterProiIPR001261. ArgE/DapE_CS.
IPR005941. DapE_proteobac.
IPR002933. Peptidase_M20.
IPR011650. Peptidase_M20_dimer.
[Graphical view]
PfamiPF07687. M20_dimer. 1 hit.
PF01546. Peptidase_M20. 1 hit.
[Graphical view]
SUPFAMiSSF55031. SSF55031. 1 hit.
TIGRFAMsiTIGR01246. dapE_proteo. 1 hit.
PROSITEiPS00758. ARGE_DAPE_CPG2_1. 1 hit.
PS00759. ARGE_DAPE_CPG2_2. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

  1. "Analysis of the genome of the Escherichia coli O157:H7 2006 spinach-associated outbreak isolate indicates candidate genes that may enhance virulence."
    Kulasekara B.R., Jacobs M., Zhou Y., Wu Z., Sims E., Saenphimmachak C., Rohmer L., Ritchie J.M., Radey M., McKevitt M., Freeman T.L., Hayden H., Haugen E., Gillett W., Fong C., Chang J., Beskhlebnaya V., Waldor M.K.
    , Samadpour M., Whittam T.S., Kaul R., Brittnacher M., Miller S.I.
    Infect. Immun. 77:3713-3721(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: TW14359 / EHECImported.

Entry informationi

Entry nameiC6UQ52_ECO5T
AccessioniPrimary (citable) accession number: C6UQ52
Entry historyi
Integrated into UniProtKB/TrEMBL: September 22, 2009
Last sequence update: September 22, 2009
Last modified: February 4, 2015
This is version 40 of the entry and version 1 of the sequence. [Complete history]
Entry statusiUnreviewed (UniProtKB/TrEMBL)

Miscellaneousi

Keywords - Technical termi

Complete proteomeImported

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.