ID A0A0N1JZA6_9ACTN Unreviewed; 201 AA.
AC A0A0N1JZA6;
DT 09-DEC-2015, integrated into UniProtKB/TrEMBL.
DT 09-DEC-2015, sequence version 1.
DT 24-JAN-2024, entry version 21.
DE SubName: Full=Peptidoglycan-binding protein {ECO:0000313|EMBL:KPC65315.1};
GN ORFNames=ADL29_08175 {ECO:0000313|EMBL:KPC65315.1};
OS Streptomyces chattanoogensis.
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces.
OX NCBI_TaxID=66876 {ECO:0000313|EMBL:KPC65315.1, ECO:0000313|Proteomes:UP000037982};
RN [1] {ECO:0000313|Proteomes:UP000037982}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NRRL ISP-5002 {ECO:0000313|Proteomes:UP000037982};
RA Ju K.-S., Doroghazi J.R., Metcalf W.W.;
RL Submitted (JUL-2015) to the EMBL/GenBank/DDBJ databases.
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:KPC65315.1}.
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DR EMBL; LGKG01000046; KPC65315.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0N1JZA6; -.
DR PATRIC; fig|66876.3.peg.1793; -.
DR Proteomes; UP000037982; Unassembled WGS sequence.
DR GO; GO:0008745; F:N-acetylmuramoyl-L-alanine amidase activity; IEA:InterPro.
DR GO; GO:0009253; P:peptidoglycan catabolic process; IEA:InterPro.
DR Gene3D; 3.40.80.10; Peptidoglycan recognition protein-like; 1.
DR InterPro; IPR036505; Amidase/PGRP_sf.
DR InterPro; IPR002502; Amidase_domain.
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 Reference proteome {ECO:0000313|Proteomes:UP000037982}.
FT DOMAIN 27..180
FT /note="N-acetylmuramoyl-L-alanine amidase"
FT /evidence="ECO:0000259|SMART:SM00644"
SQ SEQUENCE 201 AA; 21992 MW; EC134198016BF5B0 CRC64;
MAAPMTADRM LTALRDEHLT VKEIRDWRHH NRNHKGPFSN VNGVMIHHTV TSGIEGTIKL
CYDGDSSLPG PRCHGVIGKD GVVYMVGNGR TNHAGKGDDD VLQAVIEERP LPPRNELNTD
GNARFYGFEC ENLGDGDDPW PEAQLEAIEK AAAAVCRVHG WHAASVIGHL EWQMGKIDPK
GFTMAGMRER VGRRLAGPPS G
//