ID A1WIK9_VEREI Unreviewed; 471 AA.
AC A1WIK9;
DT 06-FEB-2007, integrated into UniProtKB/TrEMBL.
DT 06-FEB-2007, sequence version 1.
DT 27-MAR-2024, entry version 75.
DE RecName: Full=N-acetylmuramoyl-L-alanine amidase {ECO:0000256|ARBA:ARBA00011901};
DE EC=3.5.1.28 {ECO:0000256|ARBA:ARBA00011901};
GN OrderedLocusNames=Veis_1711 {ECO:0000313|EMBL:ABM57466.1};
OS Verminephrobacter eiseniae (strain EF01-2).
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Comamonadaceae; Verminephrobacter.
OX NCBI_TaxID=391735 {ECO:0000313|EMBL:ABM57466.1, ECO:0000313|Proteomes:UP000000374};
RN [1] {ECO:0000313|Proteomes:UP000000374}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=EF01-2 {ECO:0000313|Proteomes:UP000000374};
RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA Glavina del Rio T., Dalin E., Tice H., Pitluck S., Chertkov O., Brettin T.,
RA Bruce D., Han C., Tapia R., Gilna P., Schmutz J., Larimer F., Land M.,
RA Hauser L., Kyrpides N., Kim E., Stahl D., Richardson P.;
RT "Complete sequence of chromosome 1 of Verminephrobacter eiseniae EF01-2.";
RL Submitted (DEC-2006) 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; CP000542; ABM57466.1; -; Genomic_DNA.
DR AlphaFoldDB; A1WIK9; -.
DR STRING; 391735.Veis_1711; -.
DR KEGG; vei:Veis_1711; -.
DR eggNOG; COG0860; Bacteria.
DR HOGENOM; CLU_014322_2_2_4; -.
DR Proteomes; UP000000374; 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; 2.60.40.3500; -; 1.
DR Gene3D; 3.40.630.40; Zn-dependent exopeptidases; 1.
DR InterPro; IPR021731; AMIN_dom.
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 Pfam; PF11741; AMIN; 1.
DR SMART; SM00646; Ami_3; 1.
DR SUPFAM; SSF53187; Zn-dependent exopeptidases; 1.
PE 4: Predicted;
KW Hydrolase {ECO:0000313|EMBL:ABM57466.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000000374}.
FT DOMAIN 299..456
FT /note="MurNAc-LAA"
FT /evidence="ECO:0000259|SMART:SM00646"
FT REGION 132..162
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 135..160
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 471 AA; 49674 MW; BE605BE27A656161 CRC64;
MAHGAGIVAV RIWPAPEYSR VTIESDEALS AKPFFVATPP RLAVDIEGAD LSPALRELVA
KVRFDDPNIA GIRVGQNAPG VVRLVIDLKQ AALPQVFTLP PVAAYRHRLV LDLYPAAPMD
PLQALIAERL RDAPPPPATA APAPAPATTA QTPAPPAAPD PLDALIAQHS NHRSPPPAET
APPTLAAAPI STAPAAPAPP LPAVPAAPAP PIVPAVPARP GNRATATPTD RLIIVALDPG
HGGEDPGAIG PAGTREKDVV LRVAQLLRQR INATTVAGNP MRAYLTRDGD YFVPLGTRVQ
KARDVQADLF VSIHADAFTT PAARGASVFA LSQSGASSAA ARWMANKENQ SDLVGGINAQ
RQAQDRYVQF TKLDMSITAQ IKDSLQLGRV LLGEIGQLGQ LHKPQVEQAG FAVLKAPDIP
SVLVETAFIS NPEEEKRLRS SAYQEQLANA LMRGITRYFA KNPPLARSRS I
//
