ID A0A0U3P4L9_9ACTN Unreviewed; 620 AA.
AC A0A0U3P4L9;
DT 16-MAR-2016, integrated into UniProtKB/TrEMBL.
DT 16-MAR-2016, 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=AS200_24470 {ECO:0000313|EMBL:ALV38747.1};
OS Streptomyces sp. CdTB01.
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces.
OX NCBI_TaxID=1725411 {ECO:0000313|EMBL:ALV38747.1, ECO:0000313|Proteomes:UP000068029};
RN [1] {ECO:0000313|EMBL:ALV38747.1, ECO:0000313|Proteomes:UP000068029}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CdTB01 {ECO:0000313|EMBL:ALV38747.1,
RC ECO:0000313|Proteomes:UP000068029};
RA Tian Y., Zhou G., Yang H., Lu X.;
RT "Complete genome sequence of the Streptomyces sp. strain CdTB01, a
RT bacterium tolerant to cadmium.";
RL Submitted (DEC-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 -!- SUBCELLULAR LOCATION: Secreted {ECO:0000256|ARBA:ARBA00004613}.
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DR EMBL; CP013743; ALV38747.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0U3P4L9; -.
DR STRING; 1725411.AS200_24470; -.
DR KEGG; scx:AS200_24470; -.
DR Proteomes; UP000068029; 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; 1.10.530.10; -; 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; IPR023346; Lysozyme-like_dom_sf.
DR InterPro; IPR008258; Transglycosylase_SLT_dom_1.
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; PF01464; SLT; 1.
DR SMART; SM00644; Ami_2; 1.
DR SUPFAM; SSF53955; Lysozyme-like; 1.
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:UP000068029};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..21
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 22..620
FT /note="N-acetylmuramoyl-L-alanine amidase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5006842739"
FT DOMAIN 245..383
FT /note="N-acetylmuramoyl-L-alanine amidase"
FT /evidence="ECO:0000259|SMART:SM00644"
SQ SEQUENCE 620 AA; 63949 MW; AAC3DECFF6BA2021 CRC64;
MAAVAALAAA GATTVPVTAA AADASGRPAP SLERAFTAAA DAYHVPRQVL LAVSYQESAW
DTHPGQHSTD GGYGPMHLTD VTPAMLASGP AGAAGRGDLA QLAADPALHT LQAAAKLTGL
SATKLRTDPA ANIRGGAALL ASYQKKVTGG TSADPGNWYG AVARYSQSTQ RRGAAAFADR
VFASLRKGAA RTTSDGRRMS LAADSGIRPA TGQLAGLHLK SAAATDVECP ATLDCTFVPA
AASNGQVSNR PANGIKIDTI VIHDTESSYD AAIKTAQAAG GAAAHYVMRS ADGAVTQMVP
TKDLAFHAGN YTANMHSIGI EHEGYAAHGA TWYTEAQYEA TAELVAYLAA RYDIPLDRQH
IIGHDNVAGP KSSLVSGMHW DPGPSWDWNH FMNLLGVHSG PHGVGPVGSA VTIAPRFANN
LQTVQICPAD DPTGATTACT ETQQPSNFVY LRTEPSDTAP LFGDQAVHPG AAGTDRINDW
GSTAVAGQQF VVADRDGDWT AIWYSGAKVW FYNPHGCNTA PAYGVQVISA AGASPVAVYG
SAYPDAAEYP SGLSPSTQAP LSMYSVPAGQ AYVATEPPAP TQDFFPSGGT VVTGAKSMYT
IQYNHRVALV YAGDVTAAAQ
//
