SLEL_BACSU
ID SLEL_BACSU Reviewed; 431 AA.
AC P37531;
DT 01-OCT-1994, integrated into UniProtKB/Swiss-Prot.
DT 18-JUL-2018, sequence version 2.
DT 03-AUG-2022, entry version 144.
DE RecName: Full=Cortical fragment-lytic enzyme {ECO:0000250|UniProtKB:Q9K3E4};
DE Short=CFLE {ECO:0000250|UniProtKB:Q9K3E4};
DE EC=3.2.1.- {ECO:0000250|UniProtKB:Q9K3E4};
DE AltName: Full=Spore germination protein {ECO:0000305};
DE AltName: Full=Spore peptidoglycan N-acetylglucosaminidase {ECO:0000312|EMBL:CAB11792.1};
GN Name=sleL {ECO:0000250|UniProtKB:Q9K3E4}; Synonyms=yaaH;
GN OrderedLocusNames=BSU00160;
OS Bacillus subtilis (strain 168).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX NCBI_TaxID=224308;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=168;
RX PubMed=7584024; DOI=10.1093/dnares/1.1.1;
RA Ogasawara N., Nakai S., Yoshikawa H.;
RT "Systematic sequencing of the 180 kilobase region of the Bacillus subtilis
RT chromosome containing the replication origin.";
RL DNA Res. 1:1-14(1994).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=168;
RX PubMed=9384377; DOI=10.1038/36786;
RA Kunst F., Ogasawara N., Moszer I., Albertini A.M., Alloni G., Azevedo V.,
RA Bertero M.G., Bessieres P., Bolotin A., Borchert S., Borriss R.,
RA Boursier L., Brans A., Braun M., Brignell S.C., Bron S., Brouillet S.,
RA Bruschi C.V., Caldwell B., Capuano V., Carter N.M., Choi S.-K.,
RA Codani J.-J., Connerton I.F., Cummings N.J., Daniel R.A., Denizot F.,
RA Devine K.M., Duesterhoeft A., Ehrlich S.D., Emmerson P.T., Entian K.-D.,
RA Errington J., Fabret C., Ferrari E., Foulger D., Fritz C., Fujita M.,
RA Fujita Y., Fuma S., Galizzi A., Galleron N., Ghim S.-Y., Glaser P.,
RA Goffeau A., Golightly E.J., Grandi G., Guiseppi G., Guy B.J., Haga K.,
RA Haiech J., Harwood C.R., Henaut A., Hilbert H., Holsappel S., Hosono S.,
RA Hullo M.-F., Itaya M., Jones L.-M., Joris B., Karamata D., Kasahara Y.,
RA Klaerr-Blanchard M., Klein C., Kobayashi Y., Koetter P., Koningstein G.,
RA Krogh S., Kumano M., Kurita K., Lapidus A., Lardinois S., Lauber J.,
RA Lazarevic V., Lee S.-M., Levine A., Liu H., Masuda S., Mauel C.,
RA Medigue C., Medina N., Mellado R.P., Mizuno M., Moestl D., Nakai S.,
RA Noback M., Noone D., O'Reilly M., Ogawa K., Ogiwara A., Oudega B.,
RA Park S.-H., Parro V., Pohl T.M., Portetelle D., Porwollik S.,
RA Prescott A.M., Presecan E., Pujic P., Purnelle B., Rapoport G., Rey M.,
RA Reynolds S., Rieger M., Rivolta C., Rocha E., Roche B., Rose M., Sadaie Y.,
RA Sato T., Scanlan E., Schleich S., Schroeter R., Scoffone F., Sekiguchi J.,
RA Sekowska A., Seror S.J., Serror P., Shin B.-S., Soldo B., Sorokin A.,
RA Tacconi E., Takagi T., Takahashi H., Takemaru K., Takeuchi M.,
RA Tamakoshi A., Tanaka T., Terpstra P., Tognoni A., Tosato V., Uchiyama S.,
RA Vandenbol M., Vannier F., Vassarotti A., Viari A., Wambutt R., Wedler E.,
RA Wedler H., Weitzenegger T., Winters P., Wipat A., Yamamoto H., Yamane K.,
RA Yasumoto K., Yata K., Yoshida K., Yoshikawa H.-F., Zumstein E.,
RA Yoshikawa H., Danchin A.;
RT "The complete genome sequence of the Gram-positive bacterium Bacillus
RT subtilis.";
RL Nature 390:249-256(1997).
RN [3]
RP PROTEIN SEQUENCE OF 1-25, AND DISRUPTION PHENOTYPE.
RX PubMed=12177332; DOI=10.1099/00221287-148-8-2383;
RA Chirakkal H., O'Rourke M., Atrih A., Foster S.J., Moir A.;
RT "Analysis of spore cortex lytic enzymes and related proteins in Bacillus
RT subtilis endospore germination.";
RL Microbiology 148:2383-2392(2002).
RN [4]
RP DEVELOPMENTAL STAGE, INDUCTION, AND DISRUPTION PHENOTYPE.
RC STRAIN=168;
RX PubMed=10419957; DOI=10.1128/jb.181.15.4584-4591.1999;
RA Kodama T., Takamatsu H., Asai K., Kobayashi K., Ogasawara N., Watabe K.;
RT "The Bacillus subtilis yaaH gene is transcribed by SigE RNA polymerase
RT during sporulation, and its product is involved in germination of spores.";
RL J. Bacteriol. 181:4584-4591(1999).
RN [5]
RP SUBCELLULAR LOCATION.
RX PubMed=19933362; DOI=10.1128/jb.01103-09;
RA Imamura D., Kuwana R., Takamatsu H., Watabe K.;
RT "Localization of proteins to different layers and regions of Bacillus
RT subtilis spore coats.";
RL J. Bacteriol. 192:518-524(2010).
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:0000250|UniProtKB:Q9K3E4}.
CC -!- SUBCELLULAR LOCATION: Spore coat {ECO:0000269|PubMed:19933362}.
CC Note=Probably present in the inner coat. {ECO:0000269|PubMed:19933362}.
CC -!- DEVELOPMENTAL STAGE: Expressed in the mother cell compartment from T2
CC of sporulation. {ECO:0000269|PubMed:10419957}.
CC -!- INDUCTION: Expression is regulated by the sporulation transcription
CC factor sigma E. {ECO:0000269|PubMed:10419957}.
CC -!- DISRUPTION PHENOTYPE: Inactivation of the gene does not impair
CC vegetative growth nor prevent the development of resistance to heat,
CC chloroform and lysozyme (PubMed:10419957). According to Kodama et al,
CC the germination of the mutant spores induced by L-alanine is defective.
CC However Chirakkal et al reported that the mutant shows wild-type
CC germination kinetics in L-alanine (PubMed:12177332, PubMed:10419957).
CC {ECO:0000269|PubMed:10419957, ECO:0000269|PubMed:12177332}.
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 18 family. Chitinase
CC class II subfamily. {ECO:0000305}.
CC -!- CAUTION: Was originally thought to have epimerase activity.
CC {ECO:0000305|PubMed:12177332}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAA05252.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC Sequence=CAB11792.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR EMBL; D26185; BAA05252.1; ALT_INIT; Genomic_DNA.
DR EMBL; AL009126; CAB11792.1; ALT_INIT; Genomic_DNA.
DR PIR; S66046; S66046.
DR RefSeq; NP_387897.1; NC_000964.3.
DR AlphaFoldDB; P37531; -.
DR SMR; P37531; -.
DR STRING; 224308.BSU00160; -.
DR CAZy; CBM50; Carbohydrate-Binding Module Family 50.
DR CAZy; GH18; Glycoside Hydrolase Family 18.
DR PaxDb; P37531; -.
DR PRIDE; P37531; -.
DR EnsemblBacteria; CAB11792; CAB11792; BSU_00160.
DR GeneID; 937029; -.
DR KEGG; bsu:BSU00160; -.
DR PATRIC; fig|224308.179.peg.16; -.
DR eggNOG; COG1388; Bacteria.
DR eggNOG; COG3858; Bacteria.
DR InParanoid; P37531; -.
DR PhylomeDB; P37531; -.
DR BioCyc; BSUB:BSU00160-MON; -.
DR Proteomes; UP000001570; Chromosome.
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;
KW Reference proteome; Repeat.
FT CHAIN 1..431
FT /note="Cortical fragment-lytic enzyme"
FT /id="PRO_0000049432"
FT DOMAIN 2..46
FT /note="LysM 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01118"
FT DOMAIN 51..95
FT /note="LysM 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01118"
FT DOMAIN 103..431
FT /note="GH18"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01258"
FT ACT_SITE 217
FT /note="Proton donor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01258"
FT BINDING 148..149
FT /ligand="chitin"
FT /ligand_id="ChEBI:CHEBI:17029"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01258"
FT BINDING 174..177
FT /ligand="chitin"
FT /ligand_id="ChEBI:CHEBI:17029"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01258"
FT BINDING 218
FT /ligand="chitin"
FT /ligand_id="ChEBI:CHEBI:17029"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01258"
FT BINDING 280..283
FT /ligand="chitin"
FT /ligand_id="ChEBI:CHEBI:17029"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01258"
FT BINDING 406
FT /ligand="chitin"
FT /ligand_id="ChEBI:CHEBI:17029"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01258"
SQ SEQUENCE 431 AA; 49140 MW; AE77CBD0EC46F5F2 CRC64;
MQIYVVKQGD TLSAIASQYR TTTNDITETN EIPNPDSLVV GQTIVIPIAG QFYDVKRGDT
LTSIARQFNT TAAELARVNR IQLNTVLQIG FRLYIPPAPK RDIESNAYLE PRGNQVSENL
QQAAREASPY LTYLGAFSFQ AQRNGTLVAP PLTNLRSITE SQNTTLMMII TNLENQAFSD
ELGRILLNDE TVKRRLLNEI VENARRYGFR DIHFDFEYLR PQDREAYNQF LREARDLFHR
EGLEISTALA PKTSATQQGR WYEAHDYRAH GEIVDFVVLM TYEWGYSGGP PQAVSPIGPV
RDVIEYALTE MPANKIVMGQ NLYGYDWTLP YTAGGTPARA VSPQQAIVIA DQNNASIQYD
QTAQAPFFRY TDAENRRHEV WFEDARSIQA KFNLIKELNL RGISYWKLGL SFPQNWLLLS
DQFNVVKKTF R
