ID E6WS56_PSEUU Unreviewed; 186 AA.
AC E6WS56;
DT 08-MAR-2011, integrated into UniProtKB/TrEMBL.
DT 08-MAR-2011, sequence version 1.
DT 27-MAR-2024, entry version 52.
DE RecName: Full=N-acetylmuramoyl-L-alanine amidase {ECO:0000256|ARBA:ARBA00011901};
DE EC=3.5.1.28 {ECO:0000256|ARBA:ARBA00011901};
GN OrderedLocusNames=Psesu_1155 {ECO:0000313|EMBL:ADV27005.1};
OS Pseudoxanthomonas suwonensis (strain 11-1).
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Xanthomonadales;
OC Xanthomonadaceae; Pseudoxanthomonas.
OX NCBI_TaxID=743721 {ECO:0000313|EMBL:ADV27005.1, ECO:0000313|Proteomes:UP000008632};
RN [1] {ECO:0000313|EMBL:ADV27005.1, ECO:0000313|Proteomes:UP000008632}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=11-1 {ECO:0000313|Proteomes:UP000008632};
RG US DOE Joint Genome Institute;
RA Lucas S., Copeland A., Lapidus A., Cheng J.-F., Goodwin L., Pitluck S.,
RA Teshima H., Detter J.C., Han C., Tapia R., Land M., Hauser L., Kyrpides N.,
RA Ivanova N., Ovchinnikova G., Siebers A.K., Allgaier M., Thelen M.P.,
RA Hugenholtz P., Gladden J., Woyke T.;
RT "Complete sequence of Pseudoxanthomonas suwonensis 11-1.";
RL Submitted (JAN-2011) 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};
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DR EMBL; CP002446; ADV27005.1; -; Genomic_DNA.
DR RefSeq; WP_013534834.1; NC_014924.1.
DR AlphaFoldDB; E6WS56; -.
DR STRING; 743721.Psesu_1155; -.
DR KEGG; psu:Psesu_1155; -.
DR eggNOG; COG0860; Bacteria.
DR HOGENOM; CLU_094099_0_0_6; -.
DR OrthoDB; 7051801at2; -.
DR Proteomes; UP000008632; Chromosome.
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; 3.40.630.40; Zn-dependent exopeptidases; 1.
DR InterPro; IPR002508; MurNAc-LAA_cat.
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 SMART; SM00646; Ami_3; 1.
DR SUPFAM; SSF53187; Zn-dependent exopeptidases; 1.
PE 4: Predicted;
KW Hydrolase {ECO:0000313|EMBL:ADV27005.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000008632}.
FT DOMAIN 74..178
FT /note="MurNAc-LAA"
FT /evidence="ECO:0000259|SMART:SM00646"
SQ SEQUENCE 186 AA; 19543 MW; 03C50C86F8735F75 CRC64;
MRSIYVSAGH SGTDPGAVAN GRREADIAVE FRNLVRFYLD RHNEELAGGA PRTHKDAIHV
GTDGAGTENL PLRQAAADAR KFDVAVEFHC NAATSPAATG CEVLAGPKDM ALAARISAAL
SGALGIRDRG AKPENAGQHQ RLAFVQAGGL IVELFFITNP SDLAAYDARK WLAARAVARV
LTEAAA
//
