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Database: UniProt
Entry: U5EJT3_NOCAS
LinkDB: U5EJT3_NOCAS
Original site: U5EJT3_NOCAS 
ID   U5EJT3_NOCAS            Unreviewed;       255 AA.
AC   U5EJT3;
DT   11-DEC-2013, integrated into UniProtKB/TrEMBL.
DT   11-DEC-2013, sequence version 1.
DT   24-JAN-2024, entry version 31.
DE   RecName: Full=N-acetylmuramoyl-L-alanine amidase {ECO:0000256|ARBA:ARBA00011901};
DE            EC=3.5.1.28 {ECO:0000256|ARBA:ARBA00011901};
GN   ORFNames=NCAST_31_00880 {ECO:0000313|EMBL:GAD85394.1};
OS   Nocardia asteroides NBRC 15531.
OC   Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Nocardiaceae;
OC   Nocardia.
OX   NCBI_TaxID=1110697 {ECO:0000313|EMBL:GAD85394.1, ECO:0000313|Proteomes:UP000017048};
RN   [1] {ECO:0000313|EMBL:GAD85394.1, ECO:0000313|Proteomes:UP000017048}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NBRC 15531 {ECO:0000313|EMBL:GAD85394.1,
RC   ECO:0000313|Proteomes:UP000017048};
RX   PubMed=24884595; DOI=10.1186/1471-2164-15-323;
RA   Komaki H., Ichikawa N., Hosoyama A., Takahashi-Nakaguchi A., Matsuzawa T.,
RA   Suzuki K., Fujita N., Gonoi T.;
RT   "Genome based analysis of type-I polyketide synthase and nonribosomal
RT   peptide synthetase gene clusters in seven strains of five representative
RT   Nocardia species.";
RL   BMC Genomics 15:323-323(2014).
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   -!- 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:GAD85394.1}.
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DR   EMBL; BAFO02000031; GAD85394.1; -; Genomic_DNA.
DR   AlphaFoldDB; U5EJT3; -.
DR   STRING; 1824.SAMN05444423_101604; -.
DR   eggNOG; COG3023; Bacteria.
DR   OrthoDB; 5178799at2; -.
DR   Proteomes; UP000017048; 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   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:UP000017048}.
FT   DOMAIN          26..162
FT                   /note="N-acetylmuramoyl-L-alanine amidase"
FT                   /evidence="ECO:0000259|SMART:SM00644"
SQ   SEQUENCE   255 AA;  27792 MW;  5CACE6090D09FFBE CRC64;
     MSWTGDPVWL ADVLRAAGLN VIEHDGWRDR GHGDFRDLRG VLCHHTAGGG ANDWRIVQNG
     RADLPGPLAQ LVLERDGTYR VVAAGVCWHA GRGSWPGWPT DNANYHVIGI EAVSRGDGTD
     WTPEQIDAYQ RGCAAILARI GRSAEDCVAH REYSHEGKID PAGIDMDEFR RAVQAFIDGE
     DAPMSASEVT QIQDFITAFC GPIGSDVKDI REQLCGSRQR DAGMYGGWDQ LDGMTVVDAL
     ADILDRLKAL ETPPA
//
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