ID   D9XYX4_9ACTN            Unreviewed;       233 AA.
AC   D9XYX4;
DT   05-OCT-2010, integrated into UniProtKB/TrEMBL.
DT   05-OCT-2010, sequence version 1.
DT   27-MAR-2024, entry version 45.
DE   RecName: Full=N-acetylmuramoyl-L-alanine amidase {ECO:0000256|ARBA:ARBA00011901};
DE            EC=3.5.1.28 {ECO:0000256|ARBA:ARBA00011901};
GN   ORFNames=SSRG_01756 {ECO:0000313|EMBL:EFL38952.1};
OS   Streptomyces griseoflavus Tu4000.
OC   Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC   Streptomycetaceae; Streptomyces.
OX   NCBI_TaxID=467200 {ECO:0000313|EMBL:EFL38952.1, ECO:0000313|Proteomes:UP000002968};
RN   [1] {ECO:0000313|EMBL:EFL38952.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Tu4000 {ECO:0000313|EMBL:EFL38952.1};
RG   The Broad Institute Genome Sequencing Platform;
RG   Broad Institute Microbial Sequencing Center;
RA   Fischbach M., Godfrey P., Ward D., Young S., Zeng Q., Koehrsen M.,
RA   Alvarado L., Berlin A.M., Bochicchio J., Borenstein D., Chapman S.B.,
RA   Chen Z., Engels R., Freedman E., Gellesch M., Goldberg J., Griggs A.,
RA   Gujja S., Heilman E.R., Heiman D.I., Hepburn T.A., Howarth C., Jen D.,
RA   Larson L., Lewis B., Mehta T., Park D., Pearson M., Richards J.,
RA   Roberts A., Saif S., Shea T.D., Shenoy N., Sisk P., Stolte C., Sykes S.N.,
RA   Thomson T., Walk T., White J., Yandava C., Straight P., Clardy J., Hung D.,
RA   Kolter R., Mekalanos J., Walker S., Walsh C.T., Wieland-Brown L.C.,
RA   Haas B., Nusbaum C., Birren B.;
RT   "Annotation of Streptomyces griseoflavus strain Tu4000.";
RL   Submitted (FEB-2009) 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; GG657758; EFL38952.1; -; Genomic_DNA.
DR   RefSeq; WP_004925138.1; NZ_GG657758.1.
DR   AlphaFoldDB; D9XYX4; -.
DR   STRING; 467200.SSRG_01756; -.
DR   eggNOG; COG3023; Bacteria.
DR   HOGENOM; CLU_087616_0_0_11; -.
DR   OrthoDB; 66275at2; -.
DR   Proteomes; UP000002968; 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}.
FT   DOMAIN          72..201
FT                   /note="N-acetylmuramoyl-L-alanine amidase"
FT                   /evidence="ECO:0000259|SMART:SM00644"
SQ   SEQUENCE   233 AA;  25894 MW;  E09A11447B947EDE CRC64;
     MGENRASADG DRRIGRRALI VGGIAAATGT AVLARDELAR LWWRMPGVEK PREQGVVDYA
     GARWVAASDA NWRRADRPDD YHVDMVIVHV TQGSFDSAVQ AFQDPGHKAA AHYIVGQDGR
     VTQMIRELDV AYHAGNRDYN ERSIGIEHAG FVDRPEDFTD EMYEASARLT ARICARYDLP
     VDRKHILGHV EVPGTDHTDP GPHWDWDRYL KLVRRARTAP TPTPSTSPSS TAG
//