ID W6SKE9_9CLOT Unreviewed; 418 AA.
AC W6SKE9;
DT 16-APR-2014, integrated into UniProtKB/TrEMBL.
DT 16-APR-2014, sequence version 1.
DT 27-MAR-2024, entry version 36.
DE RecName: Full=Lysozyme {ECO:0000256|ARBA:ARBA00012732, ECO:0000256|RuleBase:RU003788};
DE EC=3.2.1.17 {ECO:0000256|ARBA:ARBA00012732, ECO:0000256|RuleBase:RU003788};
GN ORFNames=CM240_3218 {ECO:0000313|EMBL:CDM70335.1};
OS Clostridium bornimense.
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Clostridiaceae;
OC Clostridium.
OX NCBI_TaxID=1216932 {ECO:0000313|EMBL:CDM70335.1, ECO:0000313|Proteomes:UP000019426};
RN [1] {ECO:0000313|EMBL:CDM70335.1, ECO:0000313|Proteomes:UP000019426}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=M2/40 {ECO:0000313|Proteomes:UP000019426};
RA Wibberg D., Puehler A., Schlueter A.;
RT "Complete genome sequence of Clostridum sp. M2/40.";
RL Submitted (NOV-2013) to the EMBL/GenBank/DDBJ databases.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Hydrolysis of (1->4)-beta-linkages between N-acetylmuramic
CC acid and N-acetyl-D-glucosamine residues in a peptidoglycan and
CC between N-acetyl-D-glucosamine residues in chitodextrins.;
CC EC=3.2.1.17; Evidence={ECO:0000256|ARBA:ARBA00000632,
CC ECO:0000256|RuleBase:RU003788};
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 24 family.
CC {ECO:0000256|RuleBase:RU003788}.
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DR EMBL; HG917869; CDM70335.1; -; Genomic_DNA.
DR RefSeq; WP_051483906.1; NZ_HG917869.1.
DR AlphaFoldDB; W6SKE9; -.
DR STRING; 1216932.CM240_3218; -.
DR KEGG; clt:CM240_3218; -.
DR PATRIC; fig|1216932.3.peg.3190; -.
DR eggNOG; COG3409; Bacteria.
DR eggNOG; COG3772; Bacteria.
DR HOGENOM; CLU_054349_0_0_9; -.
DR OrthoDB; 529831at2; -.
DR Proteomes; UP000019426; Chromosome 2.
DR GO; GO:0030430; C:host cell cytoplasm; IEA:UniProtKB-KW.
DR GO; GO:0003796; F:lysozyme activity; IEA:UniProtKB-EC.
DR GO; GO:0016998; P:cell wall macromolecule catabolic process; IEA:InterPro.
DR GO; GO:0042742; P:defense response to bacterium; IEA:UniProtKB-KW.
DR GO; GO:0031640; P:killing of cells of another organism; IEA:UniProtKB-KW.
DR GO; GO:0009253; P:peptidoglycan catabolic process; IEA:InterPro.
DR GO; GO:0046677; P:response to antibiotic; IEA:UniProtKB-KW.
DR CDD; cd00737; lyz_endolysin_autolysin; 1.
DR Gene3D; 1.10.530.40; -; 1.
DR Gene3D; 1.10.101.10; PGBD-like superfamily/PGBD; 4.
DR HAMAP; MF_04110; ENDOLYSIN_T4; 1.
DR InterPro; IPR033907; Endolysin_autolysin.
DR InterPro; IPR034690; Endolysin_T4_type.
DR InterPro; IPR002196; Glyco_hydro_24.
DR InterPro; IPR023346; Lysozyme-like_dom_sf.
DR InterPro; IPR023347; Lysozyme_dom_sf.
DR InterPro; IPR002477; Peptidoglycan-bd-like.
DR InterPro; IPR036365; PGBD-like_sf.
DR InterPro; IPR036366; PGBDSf.
DR PANTHER; PTHR38107; -; 1.
DR PANTHER; PTHR38107:SF3; LYSOZYME RRRD-RELATED; 1.
DR Pfam; PF01471; PG_binding_1; 4.
DR Pfam; PF00959; Phage_lysozyme; 1.
DR SUPFAM; SSF53955; Lysozyme-like; 1.
DR SUPFAM; SSF47090; PGBD-like; 4.
PE 3: Inferred from homology;
KW Antibiotic resistance {ECO:0000256|ARBA:ARBA00023251};
KW Antimicrobial {ECO:0000256|ARBA:ARBA00022529,
KW ECO:0000256|RuleBase:RU003788};
KW Bacteriolytic enzyme {ECO:0000256|ARBA:ARBA00022638,
KW ECO:0000256|RuleBase:RU003788};
KW Glycosidase {ECO:0000256|RuleBase:RU003788};
KW Host cytoplasm {ECO:0000256|ARBA:ARBA00023200};
KW Hydrolase {ECO:0000256|RuleBase:RU003788};
KW Reference proteome {ECO:0000313|Proteomes:UP000019426}.
FT DOMAIN 9..64
FT /note="Peptidoglycan binding-like"
FT /evidence="ECO:0000259|Pfam:PF01471"
FT DOMAIN 66..119
FT /note="Peptidoglycan binding-like"
FT /evidence="ECO:0000259|Pfam:PF01471"
FT DOMAIN 138..193
FT /note="Peptidoglycan binding-like"
FT /evidence="ECO:0000259|Pfam:PF01471"
FT DOMAIN 195..248
FT /note="Peptidoglycan binding-like"
FT /evidence="ECO:0000259|Pfam:PF01471"
SQ SEQUENCE 418 AA; 45273 MW; F3007EB876B8AA1E CRC64;
MLLKNGSSGK NVTYLQYGIK IMCCNPGTID GNFGDDTEKA VRKYQTMKGL DSDGKVGDGT
WKALKSDIEK IQQALKDKGY TITVDGIAGS ETYNTVLSFQ SNNGLTADGM AGSATWAALN
KTTTRSEGTS VLKVGSSGTY VKYLQYGLKI MCCNPGAIDG NFGDDTEKAV RKYQTMKGLE
DDGIVGDGTW SALKTDIKKV QQALNSRDYD LTVDGIAGEL TYNAVINFQS MNGLTADGMV
GDATWNALGK SNSNSNASSQ VASNGYVSNA LVEFVKAYEG FSSTPYYDSA GVKTIGYGST
SGWIINKSSV TKAEATQALM EDINVRAKTI NKDLKSKNVS LAQKEFDSLC SFAYNLGLSA
LLDTSNLYKK VCNGVRGETL RSEFQKWRYA GGKELQGLLN RRNEECDMFI YGDYNRNK
//
