SLEL_BACAN
ID SLEL_BACAN Reviewed; 430 AA.
AC P0DPJ9;
DT 18-JUL-2018, integrated into UniProtKB/Swiss-Prot.
DT 18-JUL-2018, sequence version 1.
DT 25-MAY-2022, entry version 17.
DE RecName: Full=Cortical fragment-lytic enzyme {ECO:0000303|PubMed:18835992};
DE Short=CFLE {ECO:0000303|PubMed:18835992};
DE EC=3.2.1.- {ECO:0000269|PubMed:18835992, ECO:0000269|PubMed:22343356};
DE AltName: Full=Spore peptidoglycan N-acetylglucosaminidase {ECO:0000250|UniProtKB:P37531};
GN Name=sleL {ECO:0000303|PubMed:18835992};
GN OrderedLocusNames=BAS3402 {ECO:0000312|EMBL:AAT55709.1};
OS Bacillus anthracis.
OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus;
OC Bacillus cereus group.
OX NCBI_TaxID=1392;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Sterne;
RA Brettin T.S., Bruce D., Challacombe J.F., Gilna P., Han C., Hill K.,
RA Hitchcock P., Jackson P., Keim P., Longmire J., Lucas S., Okinaka R.,
RA Richardson P., Rubin E., Tice H.;
RT "Complete genome sequence of Bacillus anthracis Sterne.";
RL Submitted (JAN-2004) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP FUNCTION, INDUCTION, AND DISRUPTION PHENOTYPE.
RC STRAIN=Sterne;
RX PubMed=18835992; DOI=10.1128/jb.01054-08;
RA Lambert E.A., Popham D.L.;
RT "The Bacillus anthracis SleL (YaaH) protein is an N-acetylglucosaminidase
RT involved in spore cortex depolymerization.";
RL J. Bacteriol. 190:7601-7607(2008).
RN [3]
RP FUNCTION, SUBCELLULAR LOCATION, AND DOMAIN.
RC STRAIN=Sterne;
RX PubMed=22343356; DOI=10.1099/mic.0.056630-0;
RA Lambert E.A., Sherry N., Popham D.L.;
RT "In vitro and in vivo analyses of the Bacillus anthracis spore cortex lytic
RT protein SleL.";
RL Microbiology 158:1359-1368(2012).
CC -!- FUNCTION: N-acetylglucosaminidase involved in cortex peptidoglycan
CC degradation during germination (PubMed:18835992, PubMed:22343356).
CC Cleaves only partially degraded spore peptidoglycans. Recognizes
CC muramic acid delta-lactam residues specific to spore peptidoglycans
CC (PubMed:22343356). {ECO:0000269|PubMed:18835992,
CC ECO:0000269|PubMed:22343356}.
CC -!- SUBCELLULAR LOCATION: Forespore {ECO:0000269|PubMed:22343356}.
CC Note=Localizes to the coat or cortex of the endospore.
CC {ECO:0000269|PubMed:22343356}.
CC -!- INDUCTION: Expressed during sporulation. {ECO:0000269|PubMed:18835992}.
CC -!- DOMAIN: The LysM domains are involved in substrate recognition and
CC binding to cortical peptidoglycans. They are also involved in directing
CC protein localization. {ECO:0000269|PubMed:22343356}.
CC -!- DISRUPTION PHENOTYPE: The inactivation of the gene does not affect
CC vegetative growth, spore viability, or the initial stages of
CC germination, including dipicolinic acid release. However, germination
CC of mutant spores is slightly delayed and mutants retain more
CC diaminopimelic acid and N-acetylmuramic acid during germination than
CC wild-type spores. {ECO:0000269|PubMed:18835992}.
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 18 family. Chitinase
CC class II subfamily. {ECO:0000305}.
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DR EMBL; AE017225; AAT55709.1; -; Genomic_DNA.
DR RefSeq; WP_000614841.1; NZ_WXXJ01000029.1.
DR RefSeq; YP_029658.1; NC_005945.1.
DR AlphaFoldDB; P0DPJ9; -.
DR SMR; P0DPJ9; -.
DR STRING; 260799.BAS3402; -.
DR GeneID; 45023390; -.
DR KEGG; bat:BAS3402; -.
DR OMA; WYEAHDY; -.
DR GO; GO:0042763; C:intracellular immature spore; 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 2: Evidence at transcript level;
KW Germination; Glycosidase; Hydrolase; Repeat.
FT CHAIN 1..430
FT /note="Cortical fragment-lytic enzyme"
FT /id="PRO_0000444791"
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; 48169 MW; A20ABFD349A504FD CRC64;
MIQIVTVRSG DSVYSLASKY GSTPDEIVKD NGLNPAETLV VGQALIVNTK GNNYYVQPGD
SLYRISQTYN VPLASLAKVN NLSLKSILHV GQQLYIPKGT KRAVESIAYL QPSTIPIKES
LVNATRAINP FLTYLAYFSF EAKRDGTLKE PTETAKIANI ATQGNTIPML VITNIENGNF
SADLTSVILR DATIQNKFIT NILQTAEKYG MRDIHFDFES VAPEDREAYN RFLRNVKTRL
PSGYTLSTTL VPKTSSNQKG KFFETHDYKA QGQIVDFVVI MTYDWGWQGG PPMAISPIGP
VKEVLQYAKS QMPPQKIMMG QNLYGFDWKL PFKEGNPPAK AISSVAAVAL ARKYNVPIRY
DFTAQAPHFN YFDENGVQHE VWFEDSRSVQ SKFNLMKEQG IGGISYWKIG LPFPQNWRLL
VENFTITKKG
