ID A0A1W7D177_9ACTN Unreviewed; 297 AA.
AC A0A1W7D177;
DT 05-JUL-2017, integrated into UniProtKB/TrEMBL.
DT 05-JUL-2017, sequence version 1.
DT 27-MAR-2024, 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=CAG99_20000 {ECO:0000313|EMBL:ARQ70818.1};
OS Streptomyces marincola.
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces.
OX NCBI_TaxID=2878388 {ECO:0000313|EMBL:ARQ70818.1, ECO:0000313|Proteomes:UP000194218};
RN [1] {ECO:0000313|EMBL:ARQ70818.1, ECO:0000313|Proteomes:UP000194218}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SCSIO 03032 {ECO:0000313|EMBL:ARQ70818.1,
RC ECO:0000313|Proteomes:UP000194218};
RA Ma L., Zhu Y., Zhang W., Zhang G., Tian X., Zhang S., Zhang C.;
RT "Complete genome sequence of Streptomyces sp. SCSIO 03032 revealed the
RT diverse biosynthetic pathways for its bioactive secondary metabolites.";
RL Submitted (MAY-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; CP021121; ARQ70818.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1W7D177; -.
DR KEGG; smao:CAG99_20000; -.
DR OrthoDB; 514320at2; -.
DR Proteomes; UP000194218; 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 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:UP000194218};
KW Zinc {ECO:0000256|ARBA:ARBA00022833}.
FT DOMAIN 118..273
FT /note="Peptidoglycan recognition protein family"
FT /evidence="ECO:0000259|SMART:SM00701"
FT DOMAIN 130..279
FT /note="N-acetylmuramoyl-L-alanine amidase"
FT /evidence="ECO:0000259|SMART:SM00644"
FT REGION 1..69
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..20
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 21..41
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 297 AA; 31170 MW; C084A9D1EF5A50A4 CRC64;
MWTATSSTAR GTACSPSPTT RPDPRATPVA PATPPPGRPG RGAGGPGSTT PRETPTLAAE
PAHGGRLRPV LEGAPVVRDL SIRPVRRRTL LAAVTGTAAA AAAVAVPGPA RAAQPVEPDI
DGTAQWNARP PDGTISVLRH RPSMIIVHHT VSDNAQDFSR DRAHAHAHWV QDLHMDDNGW
VDTGYHFLVS RGGWITEGRH RSLETLLGGT GFVLGSHTSG QNNRGIGIAT EGAYHDGATP
PDAQWEVLVA LCAFVCAQYG IPSAEIYGHK DFGSTLCPGV LHDMLPRLRD EVAGALA
//
