ID A0A0J1JDL2_9GAMM Unreviewed; 575 AA.
AC A0A0J1JDL2;
DT 14-OCT-2015, integrated into UniProtKB/TrEMBL.
DT 14-OCT-2015, sequence version 1.
DT 27-MAR-2024, entry version 25.
DE RecName: Full=N-acetylmuramoyl-L-alanine amidase {ECO:0000256|ARBA:ARBA00011901};
DE EC=3.5.1.28 {ECO:0000256|ARBA:ARBA00011901};
GN ORFNames=ABT58_15855 {ECO:0000313|EMBL:KLU99716.1};
OS Photobacterium aphoticum.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC Photobacterium.
OX NCBI_TaxID=754436 {ECO:0000313|EMBL:KLU99716.1, ECO:0000313|Proteomes:UP000036426};
RN [1] {ECO:0000313|EMBL:KLU99716.1, ECO:0000313|Proteomes:UP000036426}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 25995 {ECO:0000313|EMBL:KLU99716.1,
RC ECO:0000313|Proteomes:UP000036426};
RA Machado H., Gram L.;
RT "Photobacterium galathea sp. nov.";
RL Submitted (MAY-2015) 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};
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:KLU99716.1}.
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DR EMBL; LDOV01000028; KLU99716.1; -; Genomic_DNA.
DR RefSeq; WP_047875417.1; NZ_PYMF01000164.1.
DR AlphaFoldDB; A0A0J1JDL2; -.
DR PATRIC; fig|754436.4.peg.3363; -.
DR OrthoDB; 9806267at2; -.
DR Proteomes; UP000036426; Unassembled WGS sequence.
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; 3.
DR CDD; cd02696; MurNAc-LAA; 1.
DR Gene3D; 2.60.40.3500; -; 1.
DR Gene3D; 3.10.350.10; LysM domain; 3.
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; 3.
DR SMART; SM00646; Ami_3; 1.
DR SMART; SM00257; LysM; 3.
DR SUPFAM; SSF54106; LysM domain; 3.
DR SUPFAM; SSF53187; Zn-dependent exopeptidases; 1.
DR PROSITE; PS51782; LYSM; 3.
PE 4: Predicted;
KW Reference proteome {ECO:0000313|Proteomes:UP000036426}.
FT DOMAIN 404..447
FT /note="LysM"
FT /evidence="ECO:0000259|PROSITE:PS51782"
FT DOMAIN 478..521
FT /note="LysM"
FT /evidence="ECO:0000259|PROSITE:PS51782"
FT DOMAIN 529..572
FT /note="LysM"
FT /evidence="ECO:0000259|PROSITE:PS51782"
SQ SEQUENCE 575 AA; 62735 MW; 53238A15FE7EF0CB CRC64;
MSLRTFFHAV IISAGVFSSL AMANELRGIR AWPAPDETRV VLDMQEKAEY SYFTLTKPDR
LVLDLKDTTL KTKLPMAVKD SAVLKTIRSS GAPEKGTYRL VFEIKTGTTP KLFTLSPTPD
GHYSHRLVLD LPHKTAPVKQ ASKPVSSKPV ANDKAILPYG NDDIIVAIDP GHGGEDPGSI
GPSRKYEKNV TLTIAKKVMA RINATPGMKA VLTRQGDYFV NLNKRSEIAR KNKAHLLVSI
HADGFTSPKP RGASVWVLNT RRANTEIGRW LEQHEKQSEL LGGGDVLSGD NEDQYLSMAV
LDLQFSHSQK EGYDVASRVL KELKGVTTLH KSKPAHASLA VLKSPDIPSL LVETGFITNP
TEERLLNATS HQNKLADAVY RGILSYFNEK PPEGTLFASR QHGIKHKVAS GQSLSVIANK
YGTSVSALKQ ANNLKSNTVR IGQVLMIPGK TPAVSHTSST AQKSSSTPSR TVVVKKTVTH
TVKRGEFLGK IANQYGVSVS SIRSANRLRS DELAVGQKLK IDVSQRRAVQ HTVKRGEFLG
KIAAHYGVSI DSLRRANKLR SDQLAVGQKL TIPSS
//
