ID B1BNS7_CLOPF Unreviewed; 342 AA.
AC B1BNS7;
DT 29-APR-2008, integrated into UniProtKB/TrEMBL.
DT 29-APR-2008, sequence version 1.
DT 24-JAN-2024, entry version 43.
DE RecName: Full=Lysozyme {ECO:0000256|RuleBase:RU361176};
DE EC=3.2.1.17 {ECO:0000256|RuleBase:RU361176};
GN ORFNames=AC3_0502 {ECO:0000313|EMBL:EDT16603.1};
OS Clostridium perfringens E str. JGS1987.
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Clostridiaceae;
OC Clostridium.
OX NCBI_TaxID=451755 {ECO:0000313|EMBL:EDT16603.1, ECO:0000313|Proteomes:UP000005337};
RN [1] {ECO:0000313|EMBL:EDT16603.1, ECO:0000313|Proteomes:UP000005337}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=E str. JGS1987 {ECO:0000313|Proteomes:UP000005337};
RA Paulsen I., Sebastian Y.;
RT "Annotation of Clostridium perfringens E str. JGS1987.";
RL Submitted (JUL-2007) 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|RuleBase:RU361176};
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 25 family.
CC {ECO:0000256|ARBA:ARBA00010646, ECO:0000256|RuleBase:RU361176}.
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:EDT16603.1}.
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DR EMBL; ABDW01000001; EDT16603.1; -; Genomic_DNA.
DR RefSeq; WP_003461014.1; NZ_ABDW01000001.1.
DR AlphaFoldDB; B1BNS7; -.
DR Proteomes; UP000005337; Unassembled WGS sequence.
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:0009253; P:peptidoglycan catabolic process; IEA:InterPro.
DR CDD; cd06525; GH25_Lyc-like; 1.
DR Gene3D; 3.20.20.80; Glycosidases; 1.
DR Gene3D; 2.30.30.40; SH3 Domains; 2.
DR InterPro; IPR002053; Glyco_hydro_25.
DR InterPro; IPR008270; Glyco_hydro_25_AS.
DR InterPro; IPR018077; Glyco_hydro_fam25_subgr.
DR InterPro; IPR017853; Glycoside_hydrolase_SF.
DR InterPro; IPR003646; SH3-like_bac-type.
DR PANTHER; PTHR34135; LYSOZYME; 1.
DR PANTHER; PTHR34135:SF2; LYSOZYME; 1.
DR Pfam; PF01183; Glyco_hydro_25; 1.
DR Pfam; PF08239; SH3_3; 2.
DR SMART; SM00641; Glyco_25; 1.
DR SMART; SM00287; SH3b; 2.
DR SUPFAM; SSF51445; (Trans)glycosidases; 1.
DR PROSITE; PS00953; GLYCOSYL_HYDROL_F25_1; 1.
DR PROSITE; PS51904; GLYCOSYL_HYDROL_F25_2; 1.
DR PROSITE; PS51781; SH3B; 2.
PE 3: Inferred from homology;
KW Glycosidase {ECO:0000256|ARBA:ARBA00023295, ECO:0000256|RuleBase:RU361176};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|RuleBase:RU361176}.
FT DOMAIN 212..276
FT /note="SH3b"
FT /evidence="ECO:0000259|PROSITE:PS51781"
FT DOMAIN 278..342
FT /note="SH3b"
FT /evidence="ECO:0000259|PROSITE:PS51781"
SQ SEQUENCE 342 AA; 39605 MW; 1B8F0B56D82BED50 CRC64;
MEGRNDNNLK GIDVSNWQGN INFKSVKNEG IEVVYIKATE GDYFKDSYAK QNYERAKAEG
LKVGFYHFFK PNKNAKRQAK YFIDYLNEIG ATDYDCKLAL DVETTEGRSA YELTTICIEF
LEEVRKITNR EVVVYTYTSF ANNNLDNRLG VYPLWIAEYG VKAPKDNRVW SSWIGFQYSD
KGNVAGVSGN CDMNEFKEEI LDVKNNFKLY NATTKNILTY LNIREKGEID SKIIGKIPAG
EKFMIKWVDS NYLGWYLIEY KNITGYVSSK YVEKFQMATT YNVRTFLNVR ERGTTDSKVV
AIIDAGEIFR IDWVDSDYIG WYRITTKYGK NGFVKADFVK KI
//
