ID A0A069JYC2_9ACTN Unreviewed; 230 AA.
AC A0A069JYC2;
DT 01-OCT-2014, integrated into UniProtKB/TrEMBL.
DT 01-OCT-2014, sequence version 1.
DT 27-MAR-2024, entry version 26.
DE RecName: Full=N-acetylmuramoyl-L-alanine amidase {ECO:0000256|ARBA:ARBA00011901};
DE EC=3.5.1.28 {ECO:0000256|ARBA:ARBA00011901};
GN ORFNames=DT87_21395 {ECO:0000313|EMBL:KDQ69651.1};
OS Streptomyces sp. NTK 937.
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces.
OX NCBI_TaxID=1487711 {ECO:0000313|EMBL:KDQ69651.1, ECO:0000313|Proteomes:UP000027475};
RN [1] {ECO:0000313|EMBL:KDQ69651.1, ECO:0000313|Proteomes:UP000027475}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NTK 937 {ECO:0000313|EMBL:KDQ69651.1,
RC ECO:0000313|Proteomes:UP000027475};
RA Olano C., Cano-Prieto C., Losada A., Mendez C., Salas J.A.;
RT "Draft genome sequence of marine actinomycete Streptomyces sp. NTK 937,
RT producer of the benzoxazol antibiotic caboxamycin.";
RL Submitted (APR-2014) 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:KDQ69651.1}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; JJOB01000001; KDQ69651.1; -; Genomic_DNA.
DR RefSeq; WP_037879640.1; NZ_JJOB01000001.1.
DR AlphaFoldDB; A0A069JYC2; -.
DR OrthoDB; 66275at2; -.
DR Proteomes; UP000027475; 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 InterPro; IPR006311; TAT_signal.
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.
DR PROSITE; PS51318; TAT; 1.
PE 4: Predicted;
KW Cell wall biogenesis/degradation {ECO:0000256|ARBA:ARBA00023316};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801}.
FT DOMAIN 76..205
FT /note="N-acetylmuramoyl-L-alanine amidase"
FT /evidence="ECO:0000259|SMART:SM00644"
SQ SEQUENCE 230 AA; 25123 MW; 4B9379667954C23E CRC64;
MGTNRNAGSS GKGPAHGISR RSLLIGGGAA VVGGGALAAA EIRRLWWRVP GVHRPREPGE
LDYAGARWIA ASEANWRRAD RPDDYTVDRV IIHVTQGSYA SAVRVFQDPS HRAASHYIVG
QDGRVTQMIR ELDVAYHAGN RSFNERSVGI EHEGFVDRPQ DFTKEMYESS ARLAASICAR
HGIPVDREHV IGHMEVPGTD HTDPGPHWDW KRYMKLVRAA STGPSAGSAS
//
