(data stored in ACNUC7421 zone)

SWISSPROT: 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   11-DEC-2019, entry version 134.
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;
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 wall, spore coat
CC       {ECO:0000269|PubMed:19933362}. Note=Probably present in the inner coat.
CC       {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};
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   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; BSU00160.
DR   GeneID; 937029; -.
DR   KEGG; bsu:BSU00160; -.
DR   PATRIC; fig|224308.179.peg.16; -.
DR   eggNOG; ENOG4105VRS; Bacteria.
DR   eggNOG; COG3858; LUCA.
DR   HOGENOM; HOG000056153; -.
DR   InParanoid; P37531; -.
DR   KO; K06306; -.
DR   PhylomeDB; P37531; -.
DR   BioCyc; BSUB:BSU00160-MONOMER; -.
DR   Proteomes; UP000001570; Chromosome.
DR   GO; GO:0031160; C:spore wall; 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   PROSITE; PS51782; LYSM; 2.
PE   1: Evidence at protein level;
DR   PRODOM; P37531.
DR   SWISS-2DPAGE; P37531.
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"
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
//

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