ID   A0A158G7G6_9BURK        Unreviewed;       511 AA.
AC   A0A158G7G6;
DT   27-SEP-2017, integrated into UniProtKB/TrEMBL.
DT   27-SEP-2017, sequence version 1.
DT   27-MAR-2024, entry version 19.
DE   RecName: Full=N-acetylmuramoyl-L-alanine amidase {ECO:0000256|ARBA:ARBA00011901};
DE            EC=3.5.1.28 {ECO:0000256|ARBA:ARBA00011901};
GN   ORFNames=AWB68_01326 {ECO:0000313|EMBL:SAL27803.1};
OS   Caballeronia choica.
OC   Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC   Burkholderiaceae; Caballeronia.
OX   NCBI_TaxID=326476 {ECO:0000313|EMBL:SAL27803.1, ECO:0000313|Proteomes:UP000054770};
RN   [1] {ECO:0000313|Proteomes:UP000054770}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Peeters C.;
RL   Submitted (JAN-2016) 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};
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DR   EMBL; FCON02000010; SAL27803.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A158G7G6; -.
DR   OrthoDB; 9806267at2; -.
DR   Proteomes; UP000054770; Unassembled WGS sequence.
DR   GO; GO:0008745; F:N-acetylmuramoyl-L-alanine amidase activity; IEA:UniProtKB-EC.
DR   GO; GO:0009253; P:peptidoglycan catabolic process; IEA:InterPro.
DR   CDD; cd02696; MurNAc-LAA; 1.
DR   Gene3D; 2.60.40.3500; -; 1.
DR   Gene3D; 3.40.630.40; Zn-dependent exopeptidases; 1.
DR   InterPro; IPR021731; AMIN_dom.
DR   InterPro; IPR002508; MurNAc-LAA_cat.
DR   PANTHER; PTHR30404; N-ACETYLMURAMOYL-L-ALANINE AMIDASE; 1.
DR   PANTHER; PTHR30404:SF0; N-ACETYLMURAMOYL-L-ALANINE AMIDASE AMIC; 1.
DR   Pfam; PF01520; Amidase_3; 1.
DR   Pfam; PF11741; AMIN; 1.
DR   SMART; SM00646; Ami_3; 1.
DR   SUPFAM; SSF53187; Zn-dependent exopeptidases; 1.
PE   4: Predicted;
FT   DOMAIN          341..496
FT                   /note="MurNAc-LAA"
FT                   /evidence="ECO:0000259|SMART:SM00646"
FT   REGION          174..274
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        184..204
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        226..248
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   511 AA;  55873 MW;  94EA35E388B55B9A CRC64;
     MSRKMLIKPF HSIESTATAS HNWRRRQVLR AGVSTIALAL VAPRLAHASS VLGVRVWPAR
     DYTRVTIESD QPLQNTQQLL QGPDRLVVDL SGLDLDQELK DLVSKITPND PQIQSVRIGQ
     YQPHVVRMVF DLKGSVKPQV FTLTPIGSYK YRLVFDLYPA VAPDPLMELL AQSERKQEAF
     DQSNPNPTPP PATLSGPATP PKPLAPDNTD EFFQKYADNS DLPRAPVAPL PMPAPRPSVK
     PPVPLAPPLA KKNEDDDDGD NYAFSAPKQN NKPGTTRLLT VAIDPGHGGE DPGAIGGAGT
     YEKHIALDIA KKLRTKIDAQ PNMRAMMTRD ADFFVPLNVR VQKARRVGAD LFVSIHADAF
     TTPDARGSSV FALSDHGASS AAARWLANKE NESDSIGGIN VRTQDVSVNR ALFDMSTTAQ
     IRDSMRYGNF VLNEIGGINK LHKGSVEQAG FAVLKAPDIP SILVETAFIS NPDEETRLND
     DAYRDKMANA IMKGIKRYFA ANPPLAKSRM T
//