GenomeNet

Database: UniProt
Entry: C2EJU4_9LACO
LinkDB: C2EJU4_9LACO
Original site: C2EJU4_9LACO 
ID   C2EJU4_9LACO            Unreviewed;       382 AA.
AC   C2EJU4;
DT   16-JUN-2009, integrated into UniProtKB/TrEMBL.
DT   16-JUN-2009, sequence version 1.
DT   27-MAR-2024, entry version 54.
DE   RecName: Full=Probable succinyl-diaminopimelate desuccinylase {ECO:0000256|ARBA:ARBA00016853};
DE            EC=3.5.1.18 {ECO:0000256|ARBA:ARBA00011921};
GN   ORFNames=HMPREF0545_1916 {ECO:0000313|EMBL:EEJ73245.1};
OS   Ligilactobacillus salivarius DSM 20555 = ATCC 11741.
OC   Bacteria; Bacillota; Bacilli; Lactobacillales; Lactobacillaceae;
OC   Ligilactobacillus.
OX   NCBI_TaxID=1423799 {ECO:0000313|EMBL:EEJ73245.1, ECO:0000313|Proteomes:UP000003531};
RN   [1] {ECO:0000313|EMBL:EEJ73245.1, ECO:0000313|Proteomes:UP000003531}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 11741 {ECO:0000313|EMBL:EEJ73245.1,
RC   ECO:0000313|Proteomes:UP000003531};
RA   Qin X., Bachman B., Battles P., Bell A., Bess C., Bickham C., Chaboub L.,
RA   Chen D., Coyle M., Deiros D.R., Dinh H., Forbes L., Fowler G.,
RA   Francisco L., Fu Q., Gubbala S., Hale W., Han Y., Hemphill L.,
RA   Highlander S.K., Hirani K., Hogues M., Jackson L., Jakkamsetti A.,
RA   Javaid M., Jiang H., Korchina V., Kovar C., Lara F., Lee S., Mata R.,
RA   Mathew T., Moen C., Morales K., Munidasa M., Nazareth L., Ngo R.,
RA   Nguyen L., Okwuonu G., Ongeri F., Patil S., Petrosino J., Pham C., Pham P.,
RA   Pu L.-L., Puazo M., Raj R., Reid J., Rouhana J., Saada N., Shang Y.,
RA   Simmons D., Thornton R., Warren J., Weissenberger G., Zhang J., Zhang L.,
RA   Zhou C., Zhu D., Muzny D., Worley K., Gibbs R.;
RL   Submitted (JAN-2009) to the EMBL/GenBank/DDBJ databases.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=H2O + N-succinyl-(2S,6S)-2,6-diaminoheptanedioate =
CC         (2S,6S)-2,6-diaminoheptanedioate + succinate; Xref=Rhea:RHEA:22608,
CC         ChEBI:CHEBI:15377, ChEBI:CHEBI:30031, ChEBI:CHEBI:57609,
CC         ChEBI:CHEBI:58087; EC=3.5.1.18;
CC         Evidence={ECO:0000256|ARBA:ARBA00001246};
CC   -!- COFACTOR:
CC       Name=Co(2+); Xref=ChEBI:CHEBI:48828;
CC         Evidence={ECO:0000256|ARBA:ARBA00001941};
CC   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC         Evidence={ECO:0000256|ARBA:ARBA00001947};
CC   -!- PATHWAY: Amino-acid biosynthesis; L-lysine biosynthesis via DAP
CC       pathway; LL-2,6-diaminopimelate from (S)-tetrahydrodipicolinate
CC       (succinylase route): step 3/3. {ECO:0000256|ARBA:ARBA00005130}.
CC   -!- SIMILARITY: Belongs to the peptidase M20A family.
CC       {ECO:0000256|ARBA:ARBA00006247}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:EEJ73245.1}.
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; ACGT01000044; EEJ73245.1; -; Genomic_DNA.
DR   RefSeq; WP_003700806.1; NZ_GG693224.1.
DR   AlphaFoldDB; C2EJU4; -.
DR   PATRIC; fig|1423799.3.peg.1830; -.
DR   HOGENOM; CLU_021802_2_2_9; -.
DR   UniPathway; UPA00034; UER00021.
DR   Proteomes; UP000003531; Unassembled WGS sequence.
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:UniProtKB-UniPathway.
DR   CDD; cd08659; M20_ArgE_DapE-like; 1.
DR   Gene3D; 3.30.70.360; -; 1.
DR   Gene3D; 3.40.630.10; Zn peptidases; 1.
DR   InterPro; IPR010182; ArgE/DapE.
DR   InterPro; IPR001261; ArgE/DapE_CS.
DR   InterPro; IPR036264; Bact_exopeptidase_dim_dom.
DR   InterPro; IPR002933; Peptidase_M20.
DR   InterPro; IPR011650; Peptidase_M20_dimer.
DR   NCBIfam; TIGR01910; DapE-ArgE; 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.
DR   PROSITE; PS00758; ARGE_DAPE_CPG2_1; 1.
DR   PROSITE; PS00759; ARGE_DAPE_CPG2_2; 1.
PE   3: Inferred from homology;
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000313|EMBL:EEJ73245.1};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Zinc {ECO:0000256|ARBA:ARBA00022833}.
FT   DOMAIN          169..274
FT                   /note="Peptidase M20 dimerisation"
FT                   /evidence="ECO:0000259|Pfam:PF07687"
SQ   SEQUENCE   382 AA;  41997 MW;  D0D2CADA90539E8D CRC64;
     MEEKEKIKIL QDLIQINSVN GNELEVAEYL HKLFAKSNLE SKVDEFGDRR ANLVLDVGQG
     EKVLGLTGHM DTVALGNEDK WSYPPLEAKI DGDRLYGRGA ADMKSGLAAL AIAIIELSDF
     GKIPGHIRFI ATAGEEYGTP GANRLRDLGV AKDLDALVVG EATNGDIIYA HSGSFNYRIV
     SHGKSVHSST PELGNNALDA LVDFAAIERT LFDDVPRDPY LGELKHSVTI LNVGEQVNTI
     PDEGELYGNI RPTSAFNNKQ IVERLKSAVD EVNDKNGAKL TFELIHDWYP VVSNPEDDFV
     QTALTVSQEV FSNYVEGKQP ELITMNGATD ASVFVKDNTN LPVIILGPGE SNVSHQIDEY
     TTISSYLALV EIYKQIILRY FE
//
DBGET integrated database retrieval system