ID A0A164DDV5_9MICO Unreviewed; 217 AA.
AC A0A164DDV5;
DT 06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT 06-JUL-2016, 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=AVP42_01401 {ECO:0000313|EMBL:KZE93784.1};
OS Agromyces sp. NDB4Y10.
OC Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Microbacteriaceae;
OC Agromyces.
OX NCBI_TaxID=1775951 {ECO:0000313|EMBL:KZE93784.1, ECO:0000313|Proteomes:UP000185889};
RN [1] {ECO:0000313|EMBL:KZE93784.1, ECO:0000313|Proteomes:UP000185889}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NDB4Y10 {ECO:0000313|EMBL:KZE93784.1,
RC ECO:0000313|Proteomes:UP000185889};
RA Adelskov J., Patel B.K.;
RT "Draft genome sequence of Agromyces sp. NDB4Y10 isolated from a newly
RT drilled coal seam bore well.";
RL Submitted (JAN-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:KZE93784.1}.
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DR EMBL; LQGY01000028; KZE93784.1; -; Genomic_DNA.
DR RefSeq; WP_067947500.1; NZ_LQGY01000028.1.
DR AlphaFoldDB; A0A164DDV5; -.
DR STRING; 1775951.AVP42_01401; -.
DR PATRIC; fig|1775951.3.peg.1441; -.
DR OrthoDB; 514320at2; -.
DR Proteomes; UP000185889; 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 InterPro; IPR006311; TAT_signal.
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.
DR PROSITE; PS51318; TAT; 1.
PE 3: Inferred from homology;
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Reference proteome {ECO:0000313|Proteomes:UP000185889};
KW Signal {ECO:0000256|SAM:SignalP}; Zinc {ECO:0000256|ARBA:ARBA00022833}.
FT SIGNAL 1..28
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 29..217
FT /note="N-acetylmuramoyl-L-alanine amidase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5038653369"
FT DOMAIN 39..194
FT /note="Peptidoglycan recognition protein family"
FT /evidence="ECO:0000259|SMART:SM00701"
SQ SEQUENCE 217 AA; 24024 MW; 192BAE9D017CA45E CRC64;
MTESTRLSRR LFLGGVAGLA AASLPFEAAT ARAADHRPPR IYSCREWGAR PPADPLTRID
ARPNKIIVHH TAYPNVQDFS LDYAFQNSRD IQNLHMDVNG WSDSGQHFTN SRGGFLTEGR
TGSLNALRSG RYMIQGAHCV GQNTQAIGIE NDGSYHLGEP VPQAQWDSLV AFCVYTCERY
RIAPTEIYGH MDFNATQCPG GLHERLPELR AAVRALL
//
