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Database: UniProt
Entry: C2ES15_9LACO
LinkDB: C2ES15_9LACO
Original site: C2ES15_9LACO 
ID   C2ES15_9LACO            Unreviewed;       378 AA.
AC   C2ES15;
DT   16-JUN-2009, integrated into UniProtKB/TrEMBL.
DT   16-JUN-2009, sequence version 1.
DT   27-MAR-2024, entry version 63.
DE   RecName: Full=Probable succinyl-diaminopimelate desuccinylase {ECO:0000256|ARBA:ARBA00016853};
DE            EC=3.5.1.18 {ECO:0000256|ARBA:ARBA00011921};
GN   ORFNames=HMPREF0549_0251 {ECO:0000313|EMBL:EEJ41375.1};
OS   Limosilactobacillus vaginalis DSM 5837 = ATCC 49540.
OC   Bacteria; Bacillota; Bacilli; Lactobacillales; Lactobacillaceae;
OC   Limosilactobacillus.
OX   NCBI_TaxID=1423814 {ECO:0000313|EMBL:EEJ41375.1, ECO:0000313|Proteomes:UP000004483};
RN   [1] {ECO:0000313|EMBL:EEJ41375.1, ECO:0000313|Proteomes:UP000004483}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 49540 {ECO:0000313|EMBL:EEJ41375.1,
RC   ECO:0000313|Proteomes:UP000004483};
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:EEJ41375.1}.
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DR   EMBL; ACGV01000018; EEJ41375.1; -; Genomic_DNA.
DR   RefSeq; WP_003716896.1; NZ_GG693413.1.
DR   AlphaFoldDB; C2ES15; -.
DR   STRING; 1423814.HMPREF0549_0251; -.
DR   PATRIC; fig|1423814.6.peg.1762; -.
DR   eggNOG; COG0624; Bacteria.
DR   HOGENOM; CLU_021802_2_2_9; -.
DR   OrthoDB; 9792335at2; -.
DR   UniPathway; UPA00034; UER00021.
DR   Proteomes; UP000004483; 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:EEJ41375.1};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Zinc {ECO:0000256|ARBA:ARBA00022833}.
FT   DOMAIN          171..278
FT                   /note="Peptidase M20 dimerisation"
FT                   /evidence="ECO:0000259|Pfam:PF07687"
SQ   SEQUENCE   378 AA;  41191 MW;  8F7211ED426BC569 CRC64;
     MDDQAKIALL QKVIQFNTVN GNEQPLAEYL KEVLAQHHID SQLVKFADNR TCLVAEIGNQ
     PGKVLAFAGH MDTVATGDPA KWKYPPFSGE IVNGNIYGRG SVDMKGGLTA MVISLIQMKE
     AGLPKHGKVR LLLSVDEEVG GQGSMLLTQK GYADDLDAMV MGEASSNQLE YAHCGSFDYE
     IESFGKTAHS SRPDLGINAV ANLARFIDGE RTAFADAQPS PVLGKVIHSV TVFHGGEQLN
     SIPDYAYLKG NVRTVPECDN EETQARLQKI IDQLNKQGAQ LRLKVVASFA PVVTDPHDPF
     INLVSDAVAA TKGSKPKVIV SHGATDASRY SLAERPFSFV EYGPGDDRQS HQINEHLLVD
     DFLQAPMIYQ KIAEKFLI
//
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