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Database: UniProt
Entry: A0A368XIR2_9BACI
LinkDB: A0A368XIR2_9BACI
Original site: A0A368XIR2_9BACI 
ID   A0A368XIR2_9BACI        Unreviewed;       396 AA.
AC   A0A368XIR2;
DT   07-NOV-2018, integrated into UniProtKB/TrEMBL.
DT   07-NOV-2018, sequence version 1.
DT   27-MAR-2024, entry version 12.
DE   SubName: Full=G-D-glutamyl-meso-diaminopimelate peptidase {ECO:0000313|EMBL:RCW65894.1};
GN   ORFNames=DFR57_110112 {ECO:0000313|EMBL:RCW65894.1};
OS   Saliterribacillus persicus.
OC   Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Saliterribacillus.
OX   NCBI_TaxID=930114 {ECO:0000313|EMBL:RCW65894.1, ECO:0000313|Proteomes:UP000252585};
RN   [1] {ECO:0000313|EMBL:RCW65894.1, ECO:0000313|Proteomes:UP000252585}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 27696 {ECO:0000313|EMBL:RCW65894.1,
RC   ECO:0000313|Proteomes:UP000252585};
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 (JUL-2018) to the EMBL/GenBank/DDBJ databases.
CC   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC         Evidence={ECO:0000256|ARBA:ARBA00001947};
CC   -!- SIMILARITY: Belongs to the peptidase M14 family.
CC       {ECO:0000256|ARBA:ARBA00005988}.
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:RCW65894.1}.
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DR   EMBL; QPJJ01000010; RCW65894.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A368XIR2; -.
DR   OrthoDB; 9802862at2; -.
DR   Proteomes; UP000252585; Unassembled WGS sequence.
DR   GO; GO:0004181; F:metallocarboxypeptidase activity; IEA:InterPro.
DR   GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR   GO; GO:0006508; P:proteolysis; IEA:InterPro.
DR   CDD; cd00118; LysM; 2.
DR   CDD; cd06229; M14_Endopeptidase_I; 1.
DR   Gene3D; 3.10.350.10; LysM domain; 2.
DR   Gene3D; 3.40.630.10; Zn peptidases; 1.
DR   InterPro; IPR034274; ENP1_M14_CPD.
DR   InterPro; IPR018392; LysM_dom.
DR   InterPro; IPR036779; LysM_dom_sf.
DR   InterPro; IPR000834; Peptidase_M14.
DR   PANTHER; PTHR11705:SF91; CARBOXYPEPTIDASE A1 (PANCREATIC)-RELATED; 1.
DR   PANTHER; PTHR11705; PROTEASE FAMILY M14 CARBOXYPEPTIDASE A,B; 1.
DR   Pfam; PF01476; LysM; 2.
DR   Pfam; PF00246; Peptidase_M14; 1.
DR   SMART; SM00257; LysM; 2.
DR   SMART; SM00631; Zn_pept; 1.
DR   SUPFAM; SSF54106; LysM domain; 2.
DR   SUPFAM; SSF53187; Zn-dependent exopeptidases; 1.
DR   PROSITE; PS51782; LYSM; 2.
PE   3: Inferred from homology;
KW   Reference proteome {ECO:0000313|Proteomes:UP000252585}.
FT   DOMAIN          1..45
FT                   /note="LysM"
FT                   /evidence="ECO:0000259|PROSITE:PS51782"
FT   DOMAIN          51..95
FT                   /note="LysM"
FT                   /evidence="ECO:0000259|PROSITE:PS51782"
SQ   SEQUENCE   396 AA;  44601 MW;  3B6F0A319851AD94 CRC64;
     MKVSVRQGDS LWYFSQLFQI PLPLIQASNP QLNPNLLMIG QDVDIPGFVL QSYSIKANDT
     LWRIAQTSVL PVDALLLLNP TIQPTQLQIG QTLLLPRRVT NLVFSNANNY SYQKMLEDIQ
     QLVTIYPFIR QQIIGKSILE KDIIELQIGA GNRQKHINGS FHANEWITTP VIMRFINEYA
     LALTNNASIR GLNLLPFFET NTLSLVPMVN PDGVDLVLNG AEAAGNLRDS VLTLNDGSTD
     FSGWKANING VDLNNQYPAL WDTEAARKPT SPQPRDFPGY QPLTEPEAIA MAQLAQQRPF
     EIMNAFHTQG EVIYWGFQGL EPPQSQTIVE EFSRISGYQP IQYVDSFAGY KDWFIQEFQR
     PGYTVELGMG VNPLPISQFE EIYQESLGIM LATLYL
//
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