ID A0A2A4KPU7_9ACTN Unreviewed; 245 AA.
AC A0A2A4KPU7;
DT 20-DEC-2017, integrated into UniProtKB/TrEMBL.
DT 20-DEC-2017, sequence version 1.
DT 27-MAR-2024, entry version 20.
DE RecName: Full=N-acetylmuramoyl-L-alanine amidase {ECO:0000256|ARBA:ARBA00011901};
DE EC=3.5.1.28 {ECO:0000256|ARBA:ARBA00011901};
GN ORFNames=CIB93_11395 {ECO:0000313|EMBL:PCG85904.1};
OS Streptomyces sp. WZ.A104.
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces.
OX NCBI_TaxID=2023771 {ECO:0000313|EMBL:PCG85904.1, ECO:0000313|Proteomes:UP000217525};
RN [1] {ECO:0000313|EMBL:PCG85904.1, ECO:0000313|Proteomes:UP000217525}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=WZ.A104 {ECO:0000313|EMBL:PCG85904.1,
RC ECO:0000313|Proteomes:UP000217525};
RA Xu L., He S., Yan X.;
RT "Isolation and Genomic Analysis of a Bioactive Actinomycete Associated with
RT Cyanobacterium Lyngbya cf. aestuarii.";
RL Submitted (SEP-2017) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Proteomes:UP000217525}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=WZ.A104 {ECO:0000313|Proteomes:UP000217525};
RA Jiao Y., Han B.;
RL Submitted (SEP-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 -!- SUBCELLULAR LOCATION: Secreted {ECO:0000256|ARBA:ARBA00004613}.
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:PCG85904.1}.
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DR EMBL; NWVL01000016; PCG85904.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2A4KPU7; -.
DR OrthoDB; 66275at2; -.
DR Proteomes; UP000217525; Unassembled WGS sequence.
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 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 SMART; SM00644; Ami_2; 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:UP000217525}.
FT DOMAIN 86..215
FT /note="N-acetylmuramoyl-L-alanine amidase"
FT /evidence="ECO:0000259|SMART:SM00644"
FT REGION 1..27
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 245 AA; 26951 MW; E63998794E49EA38 CRC64;
MGNNGSTRAP RKRSRTSSRK KPTSGVSRRA LLIGGGAAAA AGTAAVLTRD RLKRLWWQVP
GIEKPRKPGE LDYAAATWVA ASEGNWRRAD RPDDFRIDRV IIHVTQGSFA SAVKVFQDPA
HRAATHYIVG QDGRVVQMIR ELDVAYQAGD RAYNERSVGI EHEGFVDRPK DLTKAMYESS
ARLTASVCAR YDIPIDREHI IGHVEVPGTD HTDPGPHWDW DRYLELVRRA AAAPPSPTPS
AKAAG
//