ID   A7GI54_CLOBL            Unreviewed;       300 AA.
AC   A7GI54;
DT   11-SEP-2007, integrated into UniProtKB/TrEMBL.
DT   11-SEP-2007, sequence version 1.
DT   27-MAR-2024, entry version 65.
DE   RecName: Full=N-acetylmuramoyl-L-alanine amidase {ECO:0000256|ARBA:ARBA00011901};
DE            EC=3.5.1.28 {ECO:0000256|ARBA:ARBA00011901};
GN   OrderedLocusNames=CLI_3252 {ECO:0000313|EMBL:ABS41559.1};
OS   Clostridium botulinum (strain Langeland / NCTC 10281 / Type F).
OC   Bacteria; Bacillota; Clostridia; Eubacteriales; Clostridiaceae;
OC   Clostridium.
OX   NCBI_TaxID=441772 {ECO:0000313|EMBL:ABS41559.1, ECO:0000313|Proteomes:UP000002410};
RN   [1] {ECO:0000313|Proteomes:UP000002410}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Langeland / NCTC 10281 / Type F
RC   {ECO:0000313|Proteomes:UP000002410};
RA   Brinkac L.M., Daugherty S., Dodson R.J., Madupu R., Brown J.L., Bruce D.,
RA   Detter C., Munk C., Smith L.A., Smith T.J., White O., Brettin T.S.;
RL   Submitted (JUN-2007) 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   -!- SIMILARITY: Belongs to the N-acetylmuramoyl-L-alanine amidase 2 family.
CC       {ECO:0000256|ARBA:ARBA00007553}.
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DR   EMBL; CP000728; ABS41559.1; -; Genomic_DNA.
DR   RefSeq; WP_012100880.1; NC_009699.1.
DR   AlphaFoldDB; A7GI54; -.
DR   KEGG; cbf:CLI_3252; -.
DR   HOGENOM; CLU_079366_0_1_9; -.
DR   Proteomes; UP000002410; Chromosome.
DR   GO; GO:0008745; F:N-acetylmuramoyl-L-alanine amidase activity; IEA:InterPro.
DR   GO; GO:0008270; F:zinc ion binding; 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   Gene3D; 2.30.30.40; SH3 Domains; 2.
DR   InterPro; IPR036505; Amidase/PGRP_sf.
DR   InterPro; IPR002502; Amidase_domain.
DR   InterPro; IPR015510; PGRP.
DR   InterPro; IPR006619; PGRP_domain_met/bac.
DR   InterPro; IPR003646; SH3-like_bac-type.
DR   PANTHER; PTHR11022; PEPTIDOGLYCAN RECOGNITION PROTEIN; 1.
DR   PANTHER; PTHR11022:SF41; PEPTIDOGLYCAN-RECOGNITION PROTEIN SC1A-RELATED; 1.
DR   Pfam; PF01510; Amidase_2; 1.
DR   Pfam; PF08239; SH3_3; 1.
DR   SMART; SM00644; Ami_2; 1.
DR   SMART; SM00701; PGRP; 1.
DR   SMART; SM00287; SH3b; 2.
DR   SUPFAM; SSF55846; N-acetylmuramoyl-L-alanine amidase-like; 1.
DR   PROSITE; PS51781; SH3B; 1.
PE   3: Inferred from homology;
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Zinc {ECO:0000256|ARBA:ARBA00022833}.
FT   DOMAIN          239..300
FT                   /note="SH3b"
FT                   /evidence="ECO:0000259|PROSITE:PS51781"
SQ   SEQUENCE   300 AA;  32872 MW;  501407D7908421DF CRC64;
     MNIRNANLSF GSMSYGNNPQ ELDLHHAEAS VCSVLDVHSW HKGNGWAGIG YHYFVRKNGE
     IWKGRPDSAI GAHVAGHNTN TLGICAEGSY MSEDMPQAQK NAIIELCKYL CNKYGINKIY
     GHREVGSSNC PGTKYPLAEI KNAVLNGGSS NNPGPVVNDN VRDKVGIITG SGVNVRLDPN
     GKILGSVNKG DKVKLYRLEG DWYHCYSLYS GYNRCYIYKN YVSIQGSSNG SSSGTNLDGK
     TGVINTPSGV NVRADKSTSS KILGTLSNGS KVQLYRKEGD WMHIYYPKQG GYVYAKYIRY
//