ID A0A1B9ERJ7_9ACTN Unreviewed; 256 AA.
AC A0A1B9ERJ7;
DT 02-NOV-2016, integrated into UniProtKB/TrEMBL.
DT 02-NOV-2016, sequence version 1.
DT 27-MAR-2024, entry version 20.
DE RecName: Full=N-acetylmuramoyl-L-alanine amidase {ECO:0000256|ARBA:ARBA00011901};
DE EC=3.5.1.28 {ECO:0000256|ARBA:ARBA00011901};
GN ORFNames=A3Q37_04018 {ECO:0000313|EMBL:OCC10200.1};
OS Streptomyces sp. PTY087I2.
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces.
OX NCBI_TaxID=1819298 {ECO:0000313|EMBL:OCC10200.1, ECO:0000313|Proteomes:UP000093256};
RN [1] {ECO:0000313|EMBL:OCC10200.1, ECO:0000313|Proteomes:UP000093256}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PTY087I2 {ECO:0000313|EMBL:OCC10200.1,
RC ECO:0000313|Proteomes:UP000093256};
RA Kjaerup R.B., Dalgaard T.S., Juul-Madsen H.R.;
RL Submitted (JUN-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};
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}.
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:OCC10200.1}.
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DR EMBL; LZRD01000017; OCC10200.1; -; Genomic_DNA.
DR RefSeq; WP_065486480.1; NZ_LZRD01000017.1.
DR AlphaFoldDB; A0A1B9ERJ7; -.
DR PATRIC; fig|1819298.4.peg.4164; -.
DR Proteomes; UP000093256; 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:UP000093256};
KW Zinc {ECO:0000256|ARBA:ARBA00022833}.
FT DOMAIN 46..194
FT /note="Peptidoglycan recognition protein family"
FT /evidence="ECO:0000259|SMART:SM00701"
FT DOMAIN 60..222
FT /note="N-acetylmuramoyl-L-alanine amidase"
FT /evidence="ECO:0000259|SMART:SM00644"
FT REGION 28..48
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 256 AA; 27623 MW; 7E7A37391118777A CRC64;
MWSRRLVLGA LVLPLALLVF GDGPAFRTPG SEPATGPRPP RGLPQPAVVS RRDWHADEKL
VREGPHYTGA ARAVFVHHTG NPNDYDCADA PRLIRAVQRD HIRQDGWDDI GYNFLVDRCG
TIYEGRAGGV GRSVLGAHTK GFNADTVGIA AIGNFGEGAE VPEPMMDALV KLAAWKLRPG
ADPLGSVDLV STNDESRFDE GQVAHLHVIS GHRDSFETRC PGDALYALLP ELRERAARLR
AAVPGHSAAA RLRPSL
//
