ID   A0A4U8YYQ7_METTU        Unreviewed;       246 AA.
AC   A0A4U8YYQ7;
DT   31-JUL-2019, integrated into UniProtKB/TrEMBL.
DT   31-JUL-2019, sequence version 1.
DT   28-JAN-2026, entry version 21.
DE   RecName: Full=N-acetylmuramoyl-L-alanine amidase {ECO:0000256|ARBA:ARBA00011901};
DE            EC=3.5.1.28 {ECO:0000256|ARBA:ARBA00011901};
GN   ORFNames=MTUNDRAET4_1743 {ECO:0000313|EMBL:VFU08636.1};
OS   Methylocella tundrae.
OC   Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
OC   Hyphomicrobiales; Beijerinckiaceae; Methylocella.
OX   NCBI_TaxID=227605 {ECO:0000313|EMBL:VFU08636.1, ECO:0000313|Proteomes:UP000294360};
RN   [1] {ECO:0000313|EMBL:VFU08636.1, ECO:0000313|Proteomes:UP000294360}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MTUNDRAET4 annotated genome {ECO:0000313|EMBL:VFU08636.1};
RA   Kox A.R. M.;
RL   Submitted (MAR-2019) 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   -!- SIMILARITY: Belongs to the N-acetylmuramoyl-L-alanine amidase 2 family.
CC       {ECO:0000256|ARBA:ARBA00007553}.
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DR   EMBL; LR536450; VFU08636.1; -; Genomic_DNA.
DR   RefSeq; WP_244605754.1; NZ_CP139089.1.
DR   AlphaFoldDB; A0A4U8YYQ7; -.
DR   KEGG; mtun:MTUNDRAET4_1743; -.
DR   Proteomes; UP000294360; Chromosome.
DR   GO; GO:0019867; C:outer membrane; IEA:TreeGrafter.
DR   GO; GO:0008745; F:N-acetylmuramoyl-L-alanine amidase activity; IEA:UniProtKB-EC.
DR   GO; GO:0071555; P:cell wall organization; IEA:UniProtKB-KW.
DR   GO; GO:0009253; P:peptidoglycan catabolic process; IEA:InterPro.
DR   GO; GO:0009254; P:peptidoglycan turnover; IEA:TreeGrafter.
DR   CDD; cd06583; PGRP; 1.
DR   Gene3D; 3.40.80.10; Peptidoglycan recognition protein-like; 1.
DR   Gene3D; 1.10.101.10; PGBD-like superfamily/PGBD; 1.
DR   InterPro; IPR036505; Amidase/PGRP_sf.
DR   InterPro; IPR002502; Amidase_domain.
DR   InterPro; IPR051206; NAMLAA_amidase_2.
DR   InterPro; IPR002477; Peptidoglycan-bd-like.
DR   InterPro; IPR036365; PGBD-like_sf.
DR   InterPro; IPR036366; PGBDSf.
DR   PANTHER; PTHR30417; N-ACETYLMURAMOYL-L-ALANINE AMIDASE AMID; 1.
DR   PANTHER; PTHR30417:SF1; N-ACETYLMURAMOYL-L-ALANINE AMIDASE AMID; 1.
DR   Pfam; PF01510; Amidase_2; 1.
DR   Pfam; PF01471; PG_binding_1; 1.
DR   SMART; SM00644; Ami_2; 1.
DR   SUPFAM; SSF55846; N-acetylmuramoyl-L-alanine amidase-like; 1.
DR   SUPFAM; SSF47090; PGBD-like; 1.
PE   3: Inferred from homology;
KW   Cell wall biogenesis/degradation {ECO:0000256|ARBA:ARBA00023316};
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801}.
FT   DOMAIN          8..147
FT                   /note="N-acetylmuramoyl-L-alanine amidase"
FT                   /evidence="ECO:0000259|SMART:SM00644"
SQ   SEQUENCE   246 AA;  26533 MW;  6386A75FC80DF0D0 CRC64;
     MPAAFCSSPN HGERKGGRTP DSLILHYTGV ATGEAAVRLL CDPATQVSAH YVVMPDGALW
     QLVPETRRAW HAGKGSWAGE TDMNDISIGV EIAHPGHKDG AAAFPYPEAQ IATVTALCLD
     IVGRWRITPQ RVLAHSDIAP DRKIDPGEFF PWAQLAKAGV GHYVAPCPIA DGPRLEQDAS
     GADVEELQSL LARYGYGIDF SGVYDKKTQL VVRAFQRHFR PGLVDGTADF STVVTLRKLL
     AARPQG
//