ID A0A126T7U5_9GAMM Unreviewed; 521 AA.
AC A0A126T7U5;
DT 11-MAY-2016, integrated into UniProtKB/TrEMBL.
DT 11-MAY-2016, sequence version 1.
DT 27-MAR-2024, entry version 27.
DE RecName: Full=N-acetylmuramoyl-L-alanine amidase {ECO:0000256|ARBA:ARBA00011901};
DE EC=3.5.1.28 {ECO:0000256|ARBA:ARBA00011901};
GN ORFNames=JT25_017025 {ECO:0000313|EMBL:AMK78165.1};
OS Methylomonas denitrificans.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Methylococcales;
OC Methylococcaceae; Methylomonas.
OX NCBI_TaxID=1538553 {ECO:0000313|EMBL:AMK78165.1, ECO:0000313|Proteomes:UP000030512};
RN [1] {ECO:0000313|EMBL:AMK78165.1, ECO:0000313|Proteomes:UP000030512}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=FJG1 {ECO:0000313|EMBL:AMK78165.1,
RC ECO:0000313|Proteomes:UP000030512};
RX PubMed=25580993; DOI=10.1111/1462-2920.12772;
RA Kits K.D., Klotz M.G., Stein L.Y.;
RT "Methane oxidation coupled to nitrate reduction under hypoxia by the
RT Gammaproteobacterium Methylomonas denitrificans, sp. nov. type strain
RT FJG1.";
RL Environ. Microbiol. 17:3219-3232(2015).
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; CP014476; AMK78165.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A126T7U5; -.
DR STRING; 1538553.JT25_017025; -.
DR KEGG; mdn:JT25_017025; -.
DR OrthoDB; 9806267at2; -.
DR Proteomes; UP000030512; 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:AMK78165.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000030512};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..25
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 26..521
FT /note="N-acetylmuramoyl-L-alanine amidase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5007274553"
FT DOMAIN 474..517
FT /note="LysM"
FT /evidence="ECO:0000259|PROSITE:PS51782"
SQ SEQUENCE 521 AA; 55289 MW; 0BD2EDAC430902C5 CRC64;
MWGTQQMFRI FWIWGLLLPT FSAFAAQTEL GAVSYSLANQ LLVNLPSTVK HHAFVLRSPN
RLVVDFVDAK MTQGLNQPAA DHPLFGFARS AMRNNKDLRI VVELKADADA KVAMVGKNLQ
IDLAAKDQPA QPQLAAKPAE KAFTPVAAVK TEKPAAAPAV AVAEKADKSS KKSEITAKPV
AVKSVAKAKG RNIIVAIDAG HGGKDIGAQG ANGTQEKDVV FAIAKSLQGM VNSQPGMKAV
MIRDGDYFVK LNERRRIARS AKADLFVSIH ADAFSDSQAH GASVYTLASN GASSAGAGWL
AASENAVDGG AGEDRDDTLT SVLMDLSNKA AKEASQNVGN KVLRSVKSVG HLHRSAVQKA
GFVVLKSAEI PSILVETAFI SNPEEERRLN TKAYQNKMAS AVFSGIVGHF KQYAPADTMM
AQLNRSGKSK AVQLAALAVD DNESVAKAKP EQKPVLAARE LDAGPTVVAS NSGTHHVINR
GETLSGIAQQ YGISMRALRM ANAMNDGNVR IGQVLQIPRD S
//
