ID   SLEL_BACCE              Reviewed;         430 AA.
AC   Q9K3E4;
DT   18-JUL-2018, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2000, sequence version 1.
DT   25-MAY-2022, entry version 81.
DE   RecName: Full=Cortical fragment-lytic enzyme {ECO:0000303|PubMed:10692353};
DE            Short=CFLE {ECO:0000303|PubMed:10692353};
DE            EC=3.2.1.- {ECO:0000269|PubMed:10692353};
DE   AltName: Full=Germination-specific spore peptidoglycan hydrolase {ECO:0000303|PubMed:10692353};
DE   AltName: Full=Spore peptidoglycan N-acetylglucosaminidase {ECO:0000250|UniProtKB:P37531};
GN   Name=sleL {ECO:0000303|PubMed:10692353};
OS   Bacillus cereus.
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus;
OC   Bacillus cereus group.
OX   NCBI_TaxID=1396;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 1-20; 51-63;
RP   198-208; 360-371; 398-408 AND 409-418, FUNCTION, ACTIVITY REGULATION,
RP   BIOPHYSICOCHEMICAL PROPERTIES, AND SUBCELLULAR LOCATION.
RC   STRAIN=NBRC 13597;
RX   PubMed=10692353; DOI=10.1128/jb.182.6.1499-1506.2000;
RA   Chen Y., Fukuoka S., Makino S.;
RT   "A novel spore peptidoglycan hydrolase of Bacillus cereus: biochemical
RT   characterization and nucleotide sequence of the corresponding gene, sleL.";
RL   J. Bacteriol. 182:1499-1506(2000).
CC   -!- FUNCTION: N-acetylglucosaminidase involved in cortex peptidoglycan
CC       degradation during germination. Cleaves only partially degraded spore
CC       peptidoglycans. Recognizes muramic acid delta-lactam residues specific
CC       to spore peptidoglycans. {ECO:0000269|PubMed:10692353}.
CC   -!- ACTIVITY REGULATION: Inhibited by diethylpyrocarbonate.
CC       {ECO:0000269|PubMed:10692353}.
CC   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       pH dependence:
CC         Optimum pH is 6.0. {ECO:0000269|PubMed:10692353};
CC   -!- SUBCELLULAR LOCATION: Spore cortex {ECO:0000269|PubMed:10692353}.
CC       Note=Probably localizes to the exterior of the cortex layer.
CC       {ECO:0000269|PubMed:10692353}.
CC   -!- SIMILARITY: Belongs to the glycosyl hydrolase 18 family. Chitinase
CC       class II subfamily. {ECO:0000305}.
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DR   EMBL; AB029921; BAA92376.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q9K3E4; -.
DR   SMR; Q9K3E4; -.
DR   STRING; 1396.DJ87_1344; -.
DR   CAZy; CBM50; Carbohydrate-Binding Module Family 50.
DR   CAZy; GH18; Glycoside Hydrolase Family 18.
DR   GO; GO:0043595; C:endospore cortex; IEA:UniProtKB-SubCell.
DR   GO; GO:0008061; F:chitin binding; IEA:InterPro.
DR   GO; GO:0016798; F:hydrolase activity, acting on glycosyl bonds; IEA:UniProtKB-KW.
DR   GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro.
DR   CDD; cd02874; GH18_CFLE_spore_hydrolase; 1.
DR   CDD; cd00118; LysM; 2.
DR   Gene3D; 3.10.350.10; -; 2.
DR   Gene3D; 3.10.50.10; -; 1.
DR   InterPro; IPR041704; CFLE_GH18.
DR   InterPro; IPR011583; Chitinase_II.
DR   InterPro; IPR029070; Chitinase_insertion_sf.
DR   InterPro; IPR001223; Glyco_hydro18_cat.
DR   InterPro; IPR017853; Glycoside_hydrolase_SF.
DR   InterPro; IPR018392; LysM_dom.
DR   InterPro; IPR036779; LysM_dom_sf.
DR   Pfam; PF00704; Glyco_hydro_18; 1.
DR   Pfam; PF01476; LysM; 2.
DR   SMART; SM00636; Glyco_18; 1.
DR   SMART; SM00257; LysM; 2.
DR   SUPFAM; SSF51445; SSF51445; 1.
DR   SUPFAM; SSF54106; SSF54106; 2.
DR   PROSITE; PS51910; GH18_2; 1.
DR   PROSITE; PS51782; LYSM; 2.
PE   1: Evidence at protein level;
KW   Direct protein sequencing; Germination; Glycosidase; Hydrolase; Repeat.
FT   CHAIN           1..430
FT                   /note="Cortical fragment-lytic enzyme"
FT                   /id="PRO_0000444792"
FT   DOMAIN          3..47
FT                   /note="LysM 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01118"
FT   DOMAIN          52..96
FT                   /note="LysM 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01118"
FT   DOMAIN          104..430
FT                   /note="GH18"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01258"
FT   ACT_SITE        219
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01258"
SQ   SEQUENCE   430 AA;  48138 MW;  2EA51439873DBA19 CRC64;
     MIQIVTVRSG DSVYSLASKY GSTPDEIVKD NGLNPAETLV VGQALIVNTK GNNYYVQPGD
     SLYRISQTYN VPLASLAKVN NLSLKSILHV GQQLYVPKGT KRAVESIAYL QPSTIPIKES
     LVNATRAINP FLTYLAYFSF EAKRDGTLKE PTETAKIANI ATQGKTIPML VITNIENGNF
     SADLTSVILR DATIQNKFIT NILQTAQKYG MRDIHFDFES VAPEDREAYN RFLRNVKTRL
     PSGYTLSTTL VPKTSSNQKG KFFEAHDYKA QGQIVDFVVN MTYDWGWQGG PPMAISPIGP
     VKEVLQYAKS QMPPQKIMMG QNLYGFDWKL PFKQGNPPAK AISSVAAVAL ARKYNVPIRY
     DFTAQAPHFN YFDENGVQHE VWFEDSRSVQ SKFNLMKEQG IGGISYWKIG LPFPQNWRLL
     VENFTITKKG