ID A0A0G3GV05_9CORY Unreviewed; 393 AA.
AC A0A0G3GV05;
DT 16-SEP-2015, integrated into UniProtKB/TrEMBL.
DT 16-SEP-2015, sequence version 1.
DT 08-OCT-2025, entry version 26.
DE SubName: Full=N-acetylmuramoyl-L-alanine amidase {ECO:0000313|EMBL:AKK04355.1};
DE EC=3.5.1.28 {ECO:0000313|EMBL:AKK04355.1};
GN Name=cwlM {ECO:0000313|EMBL:AKK04355.1};
GN ORFNames=CEPID_12665 {ECO:0000313|EMBL:AKK04355.1};
OS Corynebacterium epidermidicanis.
OC Bacteria; Bacillati; Actinomycetota; Actinomycetes; Mycobacteriales;
OC Corynebacteriaceae; Corynebacterium.
OX NCBI_TaxID=1050174 {ECO:0000313|EMBL:AKK04355.1, ECO:0000313|Proteomes:UP000035368};
RN [1] {ECO:0000313|EMBL:AKK04355.1, ECO:0000313|Proteomes:UP000035368}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 45586 {ECO:0000313|EMBL:AKK04355.1,
RC ECO:0000313|Proteomes:UP000035368};
RA Ruckert C., Albersmeier A., Winkler A., Tauch A.;
RT "Complete genome sequence of Corynebacterium epidermidicanis DSM 45586,
RT isolated from the skin of a dog suffering from pruritus.";
RL Submitted (MAY-2015) to the EMBL/GenBank/DDBJ databases.
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; CP011541; AKK04355.1; -; Genomic_DNA.
DR RefSeq; WP_047241203.1; NZ_CP011541.1.
DR AlphaFoldDB; A0A0G3GV05; -.
DR STRING; 1050174.CEPID_12665; -.
DR KEGG; cei:CEPID_12665; -.
DR PATRIC; fig|1050174.4.peg.2557; -.
DR OrthoDB; 9810670at2; -.
DR Proteomes; UP000035368; Chromosome.
DR GO; GO:0030288; C:outer membrane-bounded periplasmic space; IEA:TreeGrafter.
DR GO; GO:0008745; F:N-acetylmuramoyl-L-alanine amidase activity; IEA:UniProtKB-EC.
DR GO; GO:0009253; P:peptidoglycan catabolic process; IEA:InterPro.
DR CDD; cd02696; MurNAc-LAA; 1.
DR Gene3D; 1.10.101.10; PGBD-like superfamily/PGBD; 2.
DR Gene3D; 3.40.630.40; Zn-dependent exopeptidases; 1.
DR InterPro; IPR002508; MurNAc-LAA_cat.
DR InterPro; IPR050695; N-acetylmuramoyl_amidase_3.
DR InterPro; IPR002477; Peptidoglycan-bd-like.
DR InterPro; IPR036365; PGBD-like_sf.
DR InterPro; IPR036366; PGBDSf.
DR PANTHER; PTHR30404; N-ACETYLMURAMOYL-L-ALANINE AMIDASE; 1.
DR PANTHER; PTHR30404:SF0; N-ACETYLMURAMOYL-L-ALANINE AMIDASE AMIC; 1.
DR Pfam; PF01520; Amidase_3; 1.
DR Pfam; PF01471; PG_binding_1; 2.
DR SMART; SM00646; Ami_3; 1.
DR SUPFAM; SSF47090; PGBD-like; 2.
DR SUPFAM; SSF53187; Zn-dependent exopeptidases; 1.
PE 4: Predicted;
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000313|EMBL:AKK04355.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000035368}.
FT DOMAIN 252..367
FT /note="MurNAc-LAA"
FT /evidence="ECO:0000259|SMART:SM00646"
SQ SEQUENCE 393 AA; 43199 MW; 41A46C03B0100002 CRC64;
MAELLRVGDK SPRVAEVRAA LVRLGLMSGH EGSLAPGSSR QFAEKDTVFD EDLAEALRAF
QQSRGIRADG VIGEKLLRTL REASYTLGAR VLVYQPGNIM VGDDVAQLQL QLQELGFYAE
RVDGHYDETT FKAVKNYQLN YGLNEDGITG PNTVRALGLL GRRITGGSRQ AIREREQVRK
AGPKLAGKRV VIDPSLGGAN KGMRVQGKYG EVAEEELLWD LATRLEGRMI AAGMEAILSR
PRLDDPSIKQ RAEIANAFGA DLLINLSMDH YPNEKANGVA TFYFGSEKGA TSLTGEMLSG
YVQREVVART GLGDCRNHAR TWDVLRMTKM PTIELVCGYL TNPRDVAILT DPRERDAIAE
AVVVAVKRLY LLDDDDQPTG TFKFTELLEA EAQ
//
