ID A0A0W0TIN7_9GAMM Unreviewed; 455 AA.
AC A0A0W0TIN7;
DT 16-MAR-2016, integrated into UniProtKB/TrEMBL.
DT 16-MAR-2016, sequence version 1.
DT 27-MAR-2024, entry version 33.
DE RecName: Full=N-acetylmuramoyl-L-alanine amidase {ECO:0000256|ARBA:ARBA00011901};
DE EC=3.5.1.28 {ECO:0000256|ARBA:ARBA00011901};
GN Name=amiB {ECO:0000313|EMBL:KTC95045.1};
GN ORFNames=Lfee_2709 {ECO:0000313|EMBL:KTC95045.1}, NCTC12022_02486
GN {ECO:0000313|EMBL:SPX61737.1};
OS Legionella feeleii.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Legionellales;
OC Legionellaceae; Legionella.
OX NCBI_TaxID=453 {ECO:0000313|EMBL:KTC95045.1, ECO:0000313|Proteomes:UP000054698};
RN [1] {ECO:0000313|EMBL:KTC95045.1, ECO:0000313|Proteomes:UP000054698}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=WO-44C {ECO:0000313|EMBL:KTC95045.1,
RC ECO:0000313|Proteomes:UP000054698};
RA Burstein D., Amaro F., Zusman T., Lifshitz Z., Cohen O., Gilbert J.A.,
RA Pupko T., Shuman H.A., Segal G.;
RT "Genomic analysis of 38 Legionella species identifies large and diverse
RT effector repertoires.";
RL Submitted (NOV-2015) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:SPX61737.1, ECO:0000313|Proteomes:UP000251942}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NCTC12022 {ECO:0000313|EMBL:SPX61737.1,
RC ECO:0000313|Proteomes:UP000251942};
RG Pathogen Informatics;
RA Doyle S.;
RL Submitted (JUN-2018) 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; LNYB01000085; KTC95045.1; -; Genomic_DNA.
DR EMBL; UASS01000022; SPX61737.1; -; Genomic_DNA.
DR RefSeq; WP_058447539.1; NZ_CAAAHT010000006.1.
DR AlphaFoldDB; A0A0W0TIN7; -.
DR STRING; 453.Lfee_2709; -.
DR PATRIC; fig|453.4.peg.2966; -.
DR Proteomes; UP000054698; Unassembled WGS sequence.
DR Proteomes; UP000251942; 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; 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:SPX61737.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000054698}.
FT DOMAIN 408..451
FT /note="LysM"
FT /evidence="ECO:0000259|PROSITE:PS51782"
FT REGION 136..159
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 136..152
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 455 AA; 50107 MW; 4420300B2417771E CRC64;
MKIRIASICL LIVWCSTLMA AKLLSIEIKQ QSGNPSVLFT LDEAVAHRVF TLTNPNRVVI
DFESTDLAVN LNRVNLGRQL IKYIRSGRPN PQTLRLVFEV SQAVMTRTNP MHRSAASKHG
FSLDLSTNGN LPSRAISSTV PVNRSGATNT AKVPVSARHE PGKTLRDVVV VLDPGHGGKD
PGASGPRRTM EKDVTLRIAQ KLKQIIDRQP GMRAVLTRNG DYYIGLRERL TIARKYNADV
FVSIHADAFI NQQSNGASVF ALSQSGATSE AARWLAEKEN YSELGGVNLS ELDDQSGLVR
TVLIDLSQTA TIGASLHMGE RVLRDLDRIT NLHNHKVEQA RFMVLKSPDI PSILIETGFI
SNPREESNLT NPAYQTHLTQ AIFQGLKRYF WDYPPHGTRI EALAGNSKIH IVRSGESLPR
IAAQYHMSVA VLQAANHLSN SQLKIGQKLV IPALT
//
