ID A0A239AMU8_9ACTN Unreviewed; 511 AA.
AC A0A239AMU8;
DT 25-OCT-2017, integrated into UniProtKB/TrEMBL.
DT 25-OCT-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=SAMN05216252_10222 {ECO:0000313|EMBL:SNR96384.1};
OS Actinacidiphila glaucinigra.
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Actinacidiphila.
OX NCBI_TaxID=235986 {ECO:0000313|EMBL:SNR96384.1, ECO:0000313|Proteomes:UP000198280};
RN [1] {ECO:0000313|EMBL:SNR96384.1, ECO:0000313|Proteomes:UP000198280}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CGMCC 4.1858 {ECO:0000313|EMBL:SNR96384.1,
RC ECO:0000313|Proteomes:UP000198280};
RA Kim H.J., Triplett B.A.;
RL Submitted (JUN-2017) 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; FZOF01000002; SNR96384.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A239AMU8; -.
DR Proteomes; UP000198280; Unassembled WGS sequence.
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 InterPro; IPR036505; Amidase/PGRP_sf.
DR InterPro; IPR002502; Amidase_domain.
DR InterPro; IPR015510; PGRP.
DR InterPro; IPR006619; PGRP_domain_met/bac.
DR PANTHER; PTHR11022; PEPTIDOGLYCAN RECOGNITION PROTEIN; 1.
DR PANTHER; PTHR11022:SF41; PEPTIDOGLYCAN-RECOGNITION PROTEIN SC1A-RELATED; 1.
DR Pfam; PF01510; Amidase_2; 1.
DR SMART; SM00644; Ami_2; 1.
DR SMART; SM00701; PGRP; 1.
DR SUPFAM; SSF55846; N-acetylmuramoyl-L-alanine amidase-like; 1.
PE 3: Inferred from homology;
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Reference proteome {ECO:0000313|Proteomes:UP000198280};
KW Signal {ECO:0000256|SAM:SignalP}; Zinc {ECO:0000256|ARBA:ARBA00022833}.
FT SIGNAL 1..16
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 17..511
FT /note="N-acetylmuramoyl-L-alanine amidase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5039428452"
FT DOMAIN 316..464
FT /note="Peptidoglycan recognition protein family"
FT /evidence="ECO:0000259|SMART:SM00701"
FT DOMAIN 332..491
FT /note="N-acetylmuramoyl-L-alanine amidase"
FT /evidence="ECO:0000259|SMART:SM00644"
FT REGION 100..312
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 271..285
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 295..309
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 511 AA; 52301 MW; B606C038A1D64963 CRC64;
MAALALPLAF PSGATATVHT PVRAAGPDTS PGATRTLPLA PLATSGRVIG TPLSQGLPAR
AVRPFSMVGI TWDDVGTDLR GTVQVRTRAT GTGTWSKWRT VEAHSDDAPD AGSSEGSASA
VRGSTSPLWV GRSDGIEVRV VPEAPAGSRR GVQPGLPKGL RLEMVDPGDE PGDGLGDGSG
DLGGSYLDPD AALDPGPAGP GGGIQRGDGT ADGPAGDGAF PGEPSGGGEP AESDGPSGGA
DPSGGDPSDS GDPFDGVGPS EGGYPLGGGR QDGTTTDNAA DPADTSGTPV ESPFVPALSR
SQTEALTGQR FTGGRPRIVT RFGWGADEQL RNEDSDFTDA ISAVFVHHTA TGNDYECSDS
PSVIRGIYRY HVKSSGWRDI GYNFLVDKCG NIYEGRSGGV SKAVFGAHTL GFNEHTMGIA
VLGDYSEDEP SREALSAVAG LAAWKLGIYG HNPEGMTYLV SGGSNRYPKG TRVRMNVISG
HRDGFNTQCP GTELYDDLGI IRRTAAGLQG R
//
