ID A0A1D9MLD5_9ACTO Unreviewed; 255 AA.
AC A0A1D9MLD5;
DT 15-FEB-2017, integrated into UniProtKB/TrEMBL.
DT 15-FEB-2017, sequence version 1.
DT 27-MAR-2024, entry version 25.
DE RecName: Full=N-acetylmuramoyl-L-alanine amidase {ECO:0000256|ARBA:ARBA00011901};
DE EC=3.5.1.28 {ECO:0000256|ARBA:ARBA00011901};
GN ORFNames=BK816_07050 {ECO:0000313|EMBL:AOZ73075.1};
OS Boudabousia tangfeifanii.
OC Bacteria; Actinomycetota; Actinomycetes; Actinomycetales; Actinomycetaceae;
OC Boudabousia.
OX NCBI_TaxID=1912795 {ECO:0000313|EMBL:AOZ73075.1, ECO:0000313|Proteomes:UP000176288};
RN [1] {ECO:0000313|EMBL:AOZ73075.1, ECO:0000313|Proteomes:UP000176288}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=VUL4_3 {ECO:0000313|EMBL:AOZ73075.1,
RC ECO:0000313|Proteomes:UP000176288};
RA Wang Y.;
RT "Actinomyces aegypiusis sp. nov., isolated from the Aegypius monachus in
RT Qinghai Tibet Plateau China.";
RL Submitted (OCT-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 -!- SUBCELLULAR LOCATION: Secreted {ECO:0000256|ARBA:ARBA00004613}.
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DR EMBL; CP017812; AOZ73075.1; -; Genomic_DNA.
DR RefSeq; WP_071164539.1; NZ_CP017812.1.
DR AlphaFoldDB; A0A1D9MLD5; -.
DR STRING; 1912795.BK816_07050; -.
DR KEGG; avu:BK816_07050; -.
DR OrthoDB; 9758772at2; -.
DR Proteomes; UP000176288; Chromosome.
DR GO; GO:0008745; F:N-acetylmuramoyl-L-alanine amidase activity; IEA:InterPro.
DR GO; GO:0071555; P:cell wall organization; IEA:UniProtKB-KW.
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; IPR013168; Cpl_7_lyso_C.
DR PANTHER; PTHR30417; N-ACETYLMURAMOYL-L-ALANINE AMIDASE AMID; 1.
DR PANTHER; PTHR30417:SF1; N-ACETYLMURAMOYL-L-ALANINE AMIDASE BLYA; 1.
DR Pfam; PF01510; Amidase_2; 1.
DR Pfam; PF08230; CW_7; 2.
DR SMART; SM00644; Ami_2; 1.
DR SMART; SM01095; Cpl-7; 2.
DR SUPFAM; SSF55846; N-acetylmuramoyl-L-alanine amidase-like; 1.
PE 4: Predicted;
KW Cell wall biogenesis/degradation {ECO:0000256|ARBA:ARBA00023316};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Reference proteome {ECO:0000313|Proteomes:UP000176288}.
FT DOMAIN 11..133
FT /note="N-acetylmuramoyl-L-alanine amidase"
FT /evidence="ECO:0000259|SMART:SM00644"
FT DOMAIN 166..204
FT /note="Cpl-7 lysozyme C-terminal"
FT /evidence="ECO:0000259|SMART:SM01095"
FT DOMAIN 216..254
FT /note="Cpl-7 lysozyme C-terminal"
FT /evidence="ECO:0000259|SMART:SM01095"
SQ SEQUENCE 255 AA; 27527 MW; 90F8117C9934BE8C CRC64;
MSYTIDHSHD ATAFTTGRQG HRIKYIVVHH WDDPAKHPTF EGTIRWFERG GNNTSAHYVA
EAGRVAQLVA DGDTAYHAGN WVKNLESIGI ECNPRCSDAD KATVAELIRD LQAKHGPLTI
LGHKDCTSTD CPGRYYPPTR VLAPWLSGGS GNAKPATTAT APSGDLNALA DAVLRGDYGN
GEERKRRLGS KYSAVQAIVN QRLGYGTAPA STGPNLNALA DAVIRGDYGN GDERKRRLGA
NYKAVQALVN RKLGY
//
