ID A0A0M8YTR1_9ACTN Unreviewed; 421 AA.
AC A0A0M8YTR1;
DT 09-DEC-2015, integrated into UniProtKB/TrEMBL.
DT 09-DEC-2015, sequence version 1.
DT 27-MAR-2024, entry version 22.
DE RecName: Full=N-acetylmuramoyl-L-alanine amidase {ECO:0000256|ARBA:ARBA00011901};
DE EC=3.5.1.28 {ECO:0000256|ARBA:ARBA00011901};
GN ORFNames=ADL09_29160 {ECO:0000313|EMBL:KOX43044.1};
OS Streptomyces sp. NRRL F-7442.
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces.
OX NCBI_TaxID=1519498 {ECO:0000313|EMBL:KOX43044.1, ECO:0000313|Proteomes:UP000037772};
RN [1] {ECO:0000313|EMBL:KOX43044.1, ECO:0000313|Proteomes:UP000037772}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NRRL F-7442 {ECO:0000313|EMBL:KOX43044.1,
RC ECO:0000313|Proteomes:UP000037772};
RA Noorani M.;
RL Submitted (JUL-2015) 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:KOX43044.1}.
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DR EMBL; LGEH01000183; KOX43044.1; -; Genomic_DNA.
DR RefSeq; WP_053665719.1; NZ_LGEH01000183.1.
DR AlphaFoldDB; A0A0M8YTR1; -.
DR PATRIC; fig|1519498.3.peg.6073; -.
DR OrthoDB; 514320at2; -.
DR Proteomes; UP000037772; 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; 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 Signal {ECO:0000256|SAM:SignalP}; Zinc {ECO:0000256|ARBA:ARBA00022833}.
FT SIGNAL 1..31
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 32..421
FT /note="N-acetylmuramoyl-L-alanine amidase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5039492550"
FT DOMAIN 226..374
FT /note="Peptidoglycan recognition protein family"
FT /evidence="ECO:0000259|SMART:SM00701"
FT REGION 27..60
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 162..181
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 421 AA; 44550 MW; A44A7C99B6FFADEB CRC64;
MRGFGLLASS TGVTCAAALA LPLAPPAAAT ASSAPPGASS ATRPEVAAHA PGGTQSLPLT
SLAHDRAPGV AEQGLPRRDV QHFSLVGVVW DDPATELHGR VEVRTRATAT GTWSDWRELD
AHNRDHAADP GTTESTSGRV RGATAPLWVG DSDGVEVRVR AETAPEAART APARPRLPGG
LRLELVDPGE DVPPSANRAR AGSGEPAVLP ALANRRKAKP HTAPRPRITT RRGWGADEKL
RDKGFVYTKN IRTVFVHHSD TGNNYRCSQA PSVVRGIYRY HVNSLGWRDL GYNFLVDKCG
NIYEGRAGGV SKPVLGAHTL GFNSQSMGVA VLGTYSGRQP SSAALKAIAR LTAWKTGQYG
MNPRGKTYLK SGGGNLYPKG KKVRMNVVSG HRDGFATNCP GKKLYAKLGT VRAKAAAYQG
R
//
