ID   A0A0J8VCD3_9GAMM        Unreviewed;       188 AA.
AC   A0A0J8VCD3;
DT   14-OCT-2015, integrated into UniProtKB/TrEMBL.
DT   14-OCT-2015, sequence version 1.
DT   27-MAR-2024, entry version 28.
DE   RecName: Full=1,6-anhydro-N-acetylmuramyl-L-alanine amidase AmpD {ECO:0000256|ARBA:ARBA00039257};
DE            EC=3.5.1.28 {ECO:0000256|ARBA:ARBA00011901};
DE   AltName: Full=N-acetylmuramoyl-L-alanine amidase {ECO:0000256|ARBA:ARBA00042615};
GN   ORFNames=C9I94_19325 {ECO:0000313|EMBL:PSW22607.1};
OS   Photobacterium swingsii.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC   Photobacterium.
OX   NCBI_TaxID=680026 {ECO:0000313|EMBL:PSW22607.1, ECO:0000313|Proteomes:UP000240481};
RN   [1] {ECO:0000313|EMBL:PSW22607.1, ECO:0000313|Proteomes:UP000240481}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 24669 {ECO:0000313|EMBL:PSW22607.1,
RC   ECO:0000313|Proteomes:UP000240481};
RA   Butler K.;
RT   "Whole genome sequencing of Histamine producing bacteria.";
RL   Submitted (JAN-2018) to the EMBL/GenBank/DDBJ databases.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=Hydrolyzes the link between N-acetylmuramoyl residues and L-
CC         amino acid residues in certain cell-wall glycopeptides.; EC=3.5.1.28;
CC         Evidence={ECO:0000256|ARBA:ARBA00001561};
CC   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC         Evidence={ECO:0000256|ARBA:ARBA00001947};
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}.
CC   -!- SIMILARITY: Belongs to the N-acetylmuramoyl-L-alanine amidase 2 family.
CC       {ECO:0000256|ARBA:ARBA00007553}.
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:PSW22607.1}.
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DR   EMBL; PYLZ01000012; PSW22607.1; -; Genomic_DNA.
DR   RefSeq; WP_048899247.1; NZ_PYLZ01000012.1.
DR   AlphaFoldDB; A0A0J8VCD3; -.
DR   STRING; 680026.AB733_13590; -.
DR   OrthoDB; 9794842at2; -.
DR   Proteomes; UP000240481; Unassembled WGS sequence.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0008745; F:N-acetylmuramoyl-L-alanine amidase activity; IEA:InterPro.
DR   GO; GO:0009253; P:peptidoglycan catabolic process; IEA:InterPro.
DR   CDD; cd06583; PGRP; 1.
DR   Gene3D; 3.40.80.10; Peptidoglycan recognition protein-like; 1.
DR   InterPro; IPR036505; Amidase/PGRP_sf.
DR   InterPro; IPR002502; Amidase_domain.
DR   PANTHER; PTHR30417:SF4; 1,6-ANHYDRO-N-ACETYLMURAMYL-L-ALANINE AMIDASE AMPD; 1.
DR   PANTHER; PTHR30417; N-ACETYLMURAMOYL-L-ALANINE AMIDASE AMID; 1.
DR   Pfam; PF01510; Amidase_2; 1.
DR   SMART; SM00644; Ami_2; 1.
DR   SUPFAM; SSF55846; N-acetylmuramoyl-L-alanine amidase-like; 1.
PE   3: Inferred from homology;
KW   Cytoplasm {ECO:0000256|ARBA:ARBA00022490}.
FT   DOMAIN          20..171
FT                   /note="N-acetylmuramoyl-L-alanine amidase"
FT                   /evidence="ECO:0000259|SMART:SM00644"
SQ   SEQUENCE   188 AA;  21359 MW;  758FBD8AD92E55C7 CRC64;
     MKTLTIQTDH WLSGVKHVPS PFYDLRPQGE VVSLLVVHNI SLPPGQFGGP YIEQLFTGKL
     NPDEHPYFEL ISEFRVSAHC LIRRNGDIIQ FVPLDCRAWH AGVSQFAERE RCNDFSIGIE
     LEGTDTLPYT QAQYASLTEL SRVLMDYYPH IDTSRITGHE FIAPGRKTDP GLAFDWYAFK
     TTLADDKS
//