ID A0A0R1U3C4_9LACO Unreviewed; 381 AA.
AC A0A0R1U3C4;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 27-MAR-2024, entry version 30.
DE SubName: Full=Succinyl-diaminopimelate desuccinylase {ECO:0000313|EMBL:KRL87108.1};
GN ORFNames=FC32_GL000401 {ECO:0000313|EMBL:KRL87108.1};
OS Ligilactobacillus apodemi DSM 16634 = JCM 16172.
OC Bacteria; Bacillota; Bacilli; Lactobacillales; Lactobacillaceae;
OC Ligilactobacillus.
OX NCBI_TaxID=1423724 {ECO:0000313|EMBL:KRL87108.1, ECO:0000313|Proteomes:UP000051324};
RN [1] {ECO:0000313|EMBL:KRL87108.1, ECO:0000313|Proteomes:UP000051324}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 16634 {ECO:0000313|EMBL:KRL87108.1,
RC ECO:0000313|Proteomes:UP000051324};
RX PubMed=26415554; DOI=10.1038/ncomms9322;
RA Sun Z., Harris H.M., McCann A., Guo C., Argimon S., Zhang W., Yang X.,
RA Jeffery I.B., Cooney J.C., Kagawa T.F., Liu W., Song Y., Salvetti E.,
RA Wrobel A., Rasinkangas P., Parkhill J., Rea M.C., O'Sullivan O., Ritari J.,
RA Douillard F.P., Paul Ross R., Yang R., Briner A.E., Felis G.E.,
RA de Vos W.M., Barrangou R., Klaenhammer T.R., Caufield P.W., Cui Y.,
RA Zhang H., O'Toole P.W.;
RT "Expanding the biotechnology potential of lactobacilli through comparative
RT genomics of 213 strains and associated genera.";
RL Nat. Commun. 6:8322-8322(2015).
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 -!- 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:KRL87108.1}.
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DR EMBL; AZFT01000009; KRL87108.1; -; Genomic_DNA.
DR RefSeq; WP_025087606.1; NZ_BAMM01000014.1.
DR AlphaFoldDB; A0A0R1U3C4; -.
DR STRING; 1423724.FC32_GL000401; -.
DR PATRIC; fig|1423724.4.peg.420; -.
DR eggNOG; COG0624; Bacteria.
DR OrthoDB; 9792335at2; -.
DR Proteomes; UP000051324; Unassembled WGS sequence.
DR GO; GO:0016787; F:hydrolase activity; IEA:InterPro.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
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; 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.
PE 3: Inferred from homology;
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Reference proteome {ECO:0000313|Proteomes:UP000051324}.
FT DOMAIN 171..276
FT /note="Peptidase M20 dimerisation"
FT /evidence="ECO:0000259|Pfam:PF07687"
SQ SEQUENCE 381 AA; 41808 MW; FEBBFCA079E2DD17 CRC64;
MALSETQKIE LLAQLVAIKS VNGDEEKVAQ FLQRYLADYW IKAQLVPVAK GRSCLVAKIG
HGHPCLAVSG HLDIVLAEPA EWYSDPFTLT AKKDRLYGRG ASDMKAGVAA LVSALIALKQ
ANEPKHGSLK LLLTVAEEVG QEGSRVLLEQ GYLTDVDALL IAEPTNLELA YAHKGSMDIK
VTSRGKSAHS SMPEEGYNAL EPLIDFLYQT KQAFEKINQA DELLGLASFN ATVIKAGKQV
NSLPAFAEAK INVRTTPLVD NQKVREILHL WKTKLNHTGA QLDLAIYLDQ HPVKLASDST
LLKLACDLGK QYFHQEIKVI GLAPVTDASN LTQGKPTDFP LIIFGPGNKS VHQANEYVDK
SQYLTFCELY PQLFTTYLAK N
//
