ID   B2GKP7_KOCRD            Unreviewed;       368 AA.
AC   B2GKP7;
DT   10-JUN-2008, integrated into UniProtKB/TrEMBL.
DT   10-JUN-2008, sequence version 1.
DT   27-MAR-2024, entry version 77.
DE   SubName: Full=Succinyl-diaminopimelate desuccinylase {ECO:0000313|EMBL:BAG29176.1};
DE            EC=3.5.1.18 {ECO:0000313|EMBL:BAG29176.1};
GN   Name=dapE {ECO:0000313|EMBL:BAG29176.1};
GN   OrderedLocusNames=KRH_08290 {ECO:0000313|EMBL:BAG29176.1};
OS   Kocuria rhizophila (strain ATCC 9341 / DSM 348 / NBRC 103217 / DC2201).
OC   Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Micrococcaceae;
OC   Kocuria.
OX   NCBI_TaxID=378753 {ECO:0000313|EMBL:BAG29176.1, ECO:0000313|Proteomes:UP000008838};
RN   [1] {ECO:0000313|EMBL:BAG29176.1, ECO:0000313|Proteomes:UP000008838}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 9341 / DSM 348 / NBRC 103217 / DC2201
RC   {ECO:0000313|Proteomes:UP000008838};
RX   PubMed=18408034; DOI=10.1128/JB.01853-07;
RA   Takarada H., Sekine M., Kosugi H., Matsuo Y., Fujisawa T., Omata S.,
RA   Kishi E., Shimizu A., Tsukatani N., Tanikawa S., Fujita N., Harayama S.;
RT   "Complete genome sequence of the soil actinomycete Kocuria rhizophila.";
RL   J. Bacteriol. 190:4139-4146(2008).
CC   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC         Evidence={ECO:0000256|ARBA:ARBA00001947};
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; AP009152; BAG29176.1; -; Genomic_DNA.
DR   AlphaFoldDB; B2GKP7; -.
DR   STRING; 378753.KRH_08290; -.
DR   KEGG; krh:KRH_08290; -.
DR   eggNOG; COG0624; Bacteria.
DR   HOGENOM; CLU_021802_1_0_11; -.
DR   Proteomes; UP000008838; Chromosome.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0009014; F:succinyl-diaminopimelate desuccinylase activity; IEA:UniProtKB-EC.
DR   GO; GO:0009089; P:lysine biosynthetic process via diaminopimelate; IEA:InterPro.
DR   Gene3D; 3.30.70.360; -; 1.
DR   Gene3D; 3.40.630.10; Zn peptidases; 1.
DR   InterPro; IPR036264; Bact_exopeptidase_dim_dom.
DR   InterPro; IPR002933; Peptidase_M20.
DR   InterPro; IPR011650; Peptidase_M20_dimer.
DR   InterPro; IPR010174; Succinyl-DAP_deSuclase_DapE.
DR   NCBIfam; TIGR01900; dapE-gram_pos; 1.
DR   PANTHER; PTHR43808; ACETYLORNITHINE DEACETYLASE; 1.
DR   PANTHER; PTHR43808:SF8; M20_DIMER DOMAIN-CONTAINING PROTEIN; 1.
DR   Pfam; PF07687; M20_dimer; 1.
DR   Pfam; PF01546; Peptidase_M20; 1.
DR   SUPFAM; SSF55031; Bacterial exopeptidase dimerisation domain; 1.
DR   SUPFAM; SSF53187; Zn-dependent exopeptidases; 1.
PE   4: Predicted;
KW   Hydrolase {ECO:0000313|EMBL:BAG29176.1};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Reference proteome {ECO:0000313|Proteomes:UP000008838}.
FT   DOMAIN          183..281
FT                   /note="Peptidase M20 dimerisation"
FT                   /evidence="ECO:0000259|Pfam:PF07687"
SQ   SEQUENCE   368 AA;  39973 MW;  CD06195FD356E84D CRC64;
     MASDQQTPVL DLTMDPADLT AALVDVESVS DHEGPLADAV EAALRELPHL TVHRDGDTVV
     ARTELGRDER VILAGHLDTV PLPTVEGALG AVPSVRRREG DRDVIYGRGT TDMKGGVAVQ
     LALVQQLREP NRDVTYVFYD HEEVSSDASG LGRVMRNGPE LLEADFAVLL EPTNGTVEGG
     CNGTMRFRIT THGKASHSGR AWIGDNAIHK QAELLERLAR YEPRTVTVEG LDYREGLNAI
     RIGGGVAGNV IPDTAWVEVN YRFAPDKTLQ QAQQHVREVF EGYEIEWQDL SPAARPGLDR
     PAAAQFVAAV GQEPMPKYGW TDVARFSEAG VPAVNFGPGD ALLAHTDDEH VVDDAVRACH
     RALSQWLS
//