ID   A0A2W7N8N7_9BACI        Unreviewed;       468 AA.
AC   A0A2W7N8N7;
DT   12-SEP-2018, integrated into UniProtKB/TrEMBL.
DT   12-SEP-2018, sequence version 1.
DT   27-MAR-2024, entry version 18.
DE   SubName: Full=Succinyl-diaminopimelate desuccinylase {ECO:0000313|EMBL:PZX06909.1};
GN   ORFNames=C7437_1019 {ECO:0000313|EMBL:PZX06909.1};
OS   Psychrobacillus insolitus.
OC   Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Psychrobacillus.
OX   NCBI_TaxID=1461 {ECO:0000313|EMBL:PZX06909.1, ECO:0000313|Proteomes:UP000248646};
RN   [1] {ECO:0000313|EMBL:PZX06909.1, ECO:0000313|Proteomes:UP000248646}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 5 {ECO:0000313|EMBL:PZX06909.1,
RC   ECO:0000313|Proteomes:UP000248646};
RA   Goeker M.;
RT   "Genomic Encyclopedia of Type Strains, Phase IV (KMG-IV): sequencing the
RT   most valuable type-strain genomes for metagenomic binning, comparative
RT   biology and taxonomic classification.";
RL   Submitted (JUN-2018) to the EMBL/GenBank/DDBJ databases.
CC   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC         Evidence={ECO:0000256|ARBA:ARBA00001947};
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:PZX06909.1}.
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; QKZI01000001; PZX06909.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A2W7N8N7; -.
DR   OrthoDB; 9761532at2; -.
DR   Proteomes; UP000248646; Unassembled WGS sequence.
DR   GO; GO:0016805; F:dipeptidase activity; IEA:UniProtKB-KW.
DR   GO; GO:0008237; F:metallopeptidase activity; IEA:UniProtKB-KW.
DR   GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR   CDD; cd03888; M20_PepV; 1.
DR   Gene3D; 3.30.70.360; -; 2.
DR   Gene3D; 3.40.630.10; Zn peptidases; 1.
DR   InterPro; IPR036264; Bact_exopeptidase_dim_dom.
DR   InterPro; IPR010964; M20A_pepV-rel.
DR   InterPro; IPR002933; Peptidase_M20.
DR   InterPro; IPR011650; Peptidase_M20_dimer.
DR   NCBIfam; TIGR01887; dipeptidaselike; 1.
DR   PANTHER; PTHR43808; ACETYLORNITHINE DEACETYLASE; 1.
DR   PANTHER; PTHR43808:SF33; DIPEPTIDASE SAOUHSC_01868-RELATED; 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   Dipeptidase {ECO:0000256|ARBA:ARBA00022997};
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022997};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Protease {ECO:0000256|ARBA:ARBA00022997};
KW   Reference proteome {ECO:0000313|Proteomes:UP000248646}.
FT   DOMAIN          254..362
FT                   /note="Peptidase M20 dimerisation"
FT                   /evidence="ECO:0000259|Pfam:PF07687"
SQ   SEQUENCE   468 AA;  51315 MW;  F171D2BAED00C274 CRC64;
     MNWLELAEQK RTEIVADLQK LIQIPSVLDE KAVTAEMPFG PKPLEALNFM LNEGQKAGFL
     TKNIDNMAGH IEMGEGDETL GILCHVDVVP EGNGWTYPPF EGIEADGKVY GRGAIDDKGP
     TIAAWMAMKL VKESGIELNK KVRMIIGTDE ESGFRCVTRY FEKEAMPEIG FAPDADFPII
     NAEKGIASLI FTQTGSTDTE TIQFFQSGKR TNMVPEEAFA LIFGGLHSIK QKFNAFSNEH
     GFTGEVTQEG PMVKILTHGK SAHAMEPNDG VNAAILLAKF LQTVPLTAHS KAFVHFLVQS
     FGEDSRGHAL ALQFTDEVSG DTTLNPGVIH YAPAQGSCTQ VSMRYSVTYP FEEKLAACRE
     ILKETGITLD LGTNSQPHYV DKEDELIKTL QKVYERQTGE EAKLLSIGGG TYARVLKKGV
     AFGMLFPGRK DLAHQVDEYV DIDDLVKATA IYADAIVELA TKLTREGV
//