ID A0A0D6DTY5_9LACT Unreviewed; 526 AA.
AC A0A0D6DTY5;
DT 27-MAY-2015, integrated into UniProtKB/TrEMBL.
DT 27-MAY-2015, sequence version 1.
DT 27-MAR-2024, entry version 32.
DE RecName: Full=N-acetylmuramoyl-L-alanine amidase {ECO:0000256|ARBA:ARBA00011901};
DE EC=3.5.1.28 {ECO:0000256|ARBA:ARBA00011901};
GN ORFNames=LACPI_0102 {ECO:0000313|EMBL:CEN27302.1};
OS Lactococcus piscium MKFS47.
OC Bacteria; Bacillota; Bacilli; Lactobacillales; Streptococcaceae;
OC Lactococcus.
OX NCBI_TaxID=297352 {ECO:0000313|EMBL:CEN27302.1, ECO:0000313|Proteomes:UP000033166};
RN [1] {ECO:0000313|Proteomes:UP000033166}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MKFS47 {ECO:0000313|Proteomes:UP000033166};
RA Andreevskaya M.;
RL Submitted (JAN-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};
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DR EMBL; LN774769; CEN27302.1; -; Genomic_DNA.
DR RefSeq; WP_050702927.1; NZ_LN774769.1.
DR AlphaFoldDB; A0A0D6DTY5; -.
DR STRING; 1364.LP2241_10095; -.
DR KEGG; lpk:LACPI_0102; -.
DR HOGENOM; CLU_528724_0_0_9; -.
DR Proteomes; UP000033166; Chromosome I.
DR GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
DR GO; GO:0071555; P:cell wall organization; IEA:UniProtKB-KW.
DR CDD; cd00118; LysM; 3.
DR Gene3D; 1.10.530.10; -; 1.
DR Gene3D; 3.90.1720.10; endopeptidase domain like (from Nostoc punctiforme); 1.
DR Gene3D; 3.10.350.10; LysM domain; 3.
DR InterPro; IPR007921; CHAP_dom.
DR InterPro; IPR018392; LysM_dom.
DR InterPro; IPR036779; LysM_dom_sf.
DR InterPro; IPR023346; Lysozyme-like_dom_sf.
DR InterPro; IPR038765; Papain-like_cys_pep_sf.
DR InterPro; IPR041219; Phage_lysozyme2.
DR PANTHER; PTHR33734:SF35; LYSM DOMAIN-CONTAINING GPI-ANCHORED PROTEIN 1; 1.
DR PANTHER; PTHR33734; LYSM DOMAIN-CONTAINING GPI-ANCHORED PROTEIN 2; 1.
DR Pfam; PF05257; CHAP; 1.
DR Pfam; PF01476; LysM; 3.
DR Pfam; PF18013; Phage_lysozyme2; 1.
DR SMART; SM00257; LysM; 3.
DR SUPFAM; SSF54001; Cysteine proteinases; 1.
DR SUPFAM; SSF54106; LysM domain; 3.
DR SUPFAM; SSF53955; Lysozyme-like; 1.
DR PROSITE; PS50911; CHAP; 1.
DR PROSITE; PS51782; LYSM; 3.
PE 4: Predicted;
KW Antimicrobial {ECO:0000256|ARBA:ARBA00022529};
KW Bacteriolytic enzyme {ECO:0000256|ARBA:ARBA00022638};
KW Cell wall biogenesis/degradation {ECO:0000256|ARBA:ARBA00023316};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000313|EMBL:CEN27302.1};
KW Signal {ECO:0000256|ARBA:ARBA00022729}.
FT DOMAIN 40..84
FT /note="LysM"
FT /evidence="ECO:0000259|PROSITE:PS51782"
FT DOMAIN 114..158
FT /note="LysM"
FT /evidence="ECO:0000259|PROSITE:PS51782"
FT DOMAIN 176..220
FT /note="LysM"
FT /evidence="ECO:0000259|PROSITE:PS51782"
FT DOMAIN 399..523
FT /note="Peptidase C51"
FT /evidence="ECO:0000259|PROSITE:PS50911"
SQ SEQUENCE 526 AA; 55561 MW; 6ED48710FA5A3821 CRC64;
MGKHDQPSLI YTKKNAVKLA LSTGTIAGAF ALTTVTAAAD TYIVKAGDTL SGIAAKYDTS
VSALSKLNNI QDIHHISINQ RIETSQVAQV EPSKPSEQAA TVNSESIGTS TPAVTYIVKA
GDTLGAISSK QGVSVAEIVK QSKLKDANLI YVGQTLIIKP EVKAKPRIVP KVIPAVTYKV
KAGESLWQIA NAEKVTIAEI VNHSGIHNAN LIYVGQELII KPAVTIYVGG GALSISATDL
AKQAGLSETA AQNAIDIANH LMGQEGFTVQ GAAGTLAVAQ RESGFNPEAI NPSGGVAGIF
QWSGWSNNIN GNRWGRASEK TLSMPVQLEL VSTELNSNFK NVKTLVGNAT DPKQASLDWT
VYYEGVALSD PQTKEKALLA NAEKWYDLLK DHVTGTEADA VDVPFDVTKG AYSSTGNTYA
SGQCTWYVKD IFKARMGDYW GNAKDWAASA KREGVPVDHN PIANQTIAVF QPGSAGADAT
YGHVAVVIGV NGDSITIKEM NGAAGIGKTN TRVIPKSAAT YIHMTY
//
