ID I1XLL6_METNJ Unreviewed; 461 AA.
AC I1XLL6;
DT 11-JUL-2012, integrated into UniProtKB/TrEMBL.
DT 11-JUL-2012, sequence version 1.
DT 27-MAR-2024, entry version 59.
DE RecName: Full=N-acetylmuramoyl-L-alanine amidase {ECO:0000256|ARBA:ARBA00011901};
DE EC=3.5.1.28 {ECO:0000256|ARBA:ARBA00011901};
GN OrderedLocusNames=Q7A_2485 {ECO:0000313|EMBL:AFI85285.1};
GN ORFNames=CDW43_14895 {ECO:0000313|EMBL:AUZ85770.1};
OS Methylophaga nitratireducenticrescens.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Thiotrichales;
OC Piscirickettsiaceae; Methylophaga.
OX NCBI_TaxID=754476 {ECO:0000313|EMBL:AFI85285.1, ECO:0000313|Proteomes:UP000009144};
RN [1] {ECO:0000313|EMBL:AFI85285.1, ECO:0000313|Proteomes:UP000009144}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JAM1 {ECO:0000313|EMBL:AFI85285.1,
RC ECO:0000313|Proteomes:UP000009144};
RX PubMed=22815445; DOI=10.1128/JB.00726-12;
RA Villeneuve C., Martineau C., Mauffrey F., Villemur R.;
RT "Complete genome sequences of Methylophaga sp. strain JAM1 and Methylophaga
RT sp. strain JAM7.";
RL J. Bacteriol. 194:4126-4127(2012).
RN [2] {ECO:0000313|EMBL:AFI85285.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=JAM1 {ECO:0000313|EMBL:AFI85285.1};
RX PubMed=23148104; DOI=10.1099/ijs.0.044545-0;
RA Villeneuve C., Martineau C., Mauffrey F., Villemur R.;
RT "Methylophaga nitratireducenticrescens sp. nov. and Methylophaga frappieri
RT sp. nov., isolated from the biofilm of the methanol-fed denitrification
RT system treating the seawater at the Montreal Biodome.";
RL Int. J. Syst. Evol. Microbiol. 63:2216-2222(2013).
RN [3] {ECO:0000313|EMBL:AFI85285.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=JAM1 {ECO:0000313|EMBL:AFI85285.1};
RA Villeneuve C., Villemur R.;
RL Submitted (JUN-2015) to the EMBL/GenBank/DDBJ databases.
RN [4] {ECO:0000313|EMBL:AUZ85770.1, ECO:0000313|Proteomes:UP000238402}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=GP59 {ECO:0000313|EMBL:AUZ85770.1,
RC ECO:0000313|Proteomes:UP000238402};
RA Villemur R.;
RT "The sequence of the genome of Methylophaga nitratireducenticrescens GP59
RT and its two plasmids.";
RL Submitted (JUN-2017) 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; CP003390; AFI85285.1; -; Genomic_DNA.
DR EMBL; CP021973; AUZ85770.1; -; Genomic_DNA.
DR RefSeq; WP_014707649.1; NZ_CP021973.1.
DR AlphaFoldDB; I1XLL6; -.
DR STRING; 754476.Q7A_2485; -.
DR KEGG; mej:Q7A_2485; -.
DR PATRIC; fig|754476.3.peg.2447; -.
DR eggNOG; COG0860; Bacteria.
DR eggNOG; COG1388; Bacteria.
DR HOGENOM; CLU_014322_2_3_6; -.
DR OrthoDB; 9806267at2; -.
DR Proteomes; UP000009144; Chromosome.
DR Proteomes; UP000238402; 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; cd00118; LysM; 1.
DR CDD; cd02696; MurNAc-LAA; 1.
DR Gene3D; 2.60.40.3500; -; 1.
DR Gene3D; 3.10.350.10; LysM domain; 1.
DR Gene3D; 3.40.630.40; Zn-dependent exopeptidases; 1.
DR InterPro; IPR021731; AMIN_dom.
DR InterPro; IPR018392; LysM_dom.
DR InterPro; IPR036779; LysM_dom_sf.
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 Pfam; PF01476; LysM; 1.
DR SMART; SM00646; Ami_3; 1.
DR SMART; SM00257; LysM; 1.
DR SUPFAM; SSF54106; LysM domain; 1.
DR SUPFAM; SSF53187; Zn-dependent exopeptidases; 1.
DR PROSITE; PS51782; LYSM; 1.
PE 4: Predicted;
KW Hydrolase {ECO:0000313|EMBL:AFI85285.1}; Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..19
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 20..461
FT /note="N-acetylmuramoyl-L-alanine amidase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5015093917"
FT DOMAIN 417..460
FT /note="LysM"
FT /evidence="ECO:0000259|PROSITE:PS51782"
FT REGION 132..175
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 140..154
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 157..175
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 461 AA; 50731 MW; F65B1E6161D9CF32 CRC64;
MSRLLLGLII LMFTVDAHAA SVENIRISQN TNLTRVVLDL DTALEYSSFT LTNPHRLVVD
LKAAKVNKKL IAPTFNSAVV EKIRHAQHDQ ETYRLVFDLK QETDYEIQTL APEGEYSHRL
LVDLKHGPAT ALATNKSSKS PEKATDKAEE KASAQITKAD TPPSPQQTAT NTTVRNRPML
PRRDIVIAID PGHGGRDPGA IGRKGTREKD VVLAISRRLA KLVDNEPGMR AFMTRERDEF
ITLRQRIQRA KKNGADMFIS IHADAFQRTS AKGSSVYVLS QRGASSEAAQ ILADRENAAD
LAGGISLEDK DDLLASVLLD LSQTASLEAS LEVGNSVLSG LKRVGPVHKK RVESAAFVVL
KSPDIPSVLV ETAFISNPEE ERKLNDVNHQ NKLAQAMLAG IRSYFQRNPI TQQVKPQQHI
VSSGDTLSTI AQRYRVNMSE LKSTNNLQTS KLMVGDVLKI P
//
