ID   SLEB_BACCE              Reviewed;         259 AA.
AC   P0A3V1; P70874;
DT   15-MAR-2005, integrated into UniProtKB/Swiss-Prot.
DT   15-MAR-2005, sequence version 1.
DT   25-MAY-2022, entry version 80.
DE   RecName: Full=Spore cortex-lytic enzyme;
DE            Short=SCLE;
DE   AltName: Full=Germination-specific amidase;
DE   Flags: Precursor;
GN   Name=sleB;
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 33-52; 64-80; 83-94
RP   AND 215-234, AND MUTAGENESIS OF CYS-258.
RC   STRAIN=NBRC 13597;
RX   PubMed=8752358; DOI=10.1128/jb.178.17.5330-5332.1996;
RA   Moriyama R., Kudoh S., Miyata S., Nonobe S., Hattori A., Makino S.;
RT   "A germination-specific spore cortex-lytic enzyme from Bacillus cereus
RT   spores: cloning and sequencing of the gene and molecular characterization
RT   of the enzyme.";
RL   J. Bacteriol. 178:5330-5332(1996).
RN   [2]
RP   PROTEIN SEQUENCE OF 33-51.
RC   STRAIN=NBRC 13597;
RX   PubMed=8081503; DOI=10.1099/00221287-140-6-1403;
RA   Makino S., Ito N., Inoue T., Miyata S., Moriyama R.;
RT   "A spore-lytic enzyme released from Bacillus cereus spores during
RT   germination.";
RL   Microbiology 140:1403-1410(1994).
RN   [3]
RP   CHARACTERIZATION.
RX   PubMed=10197998; DOI=10.1128/jb.181.8.2373-2378.1999;
RA   Moriyama R., Fukuoka H., Miyata S., Kudoh S., Hattori A., Kozuka S.,
RA   Yasuda Y., Tochikubo K., Makino S.;
RT   "Expression of a germination-specific amidase, SleB, of Bacilli in the
RT   forespore compartment of sporulating cells and its localization on the
RT   exterior side of the cortex in dormant spores.";
RL   J. Bacteriol. 181:2373-2378(1999).
CC   -!- FUNCTION: Probable N-acetylmuramyl-L-alanine amidase. Required for
CC       spore cortex hydrolysis during germination. May form a complex with
CC       some hydrophobic spore component, leading to a stabilization of the
CC       enzyme in a spore-bound form.
CC   -!- ACTIVITY REGULATION: Inhibited by HgCl(2). Activity is recovered by the
CC       addition of 2-mercaptoethanol.
CC   -!- SUBCELLULAR LOCATION: Forespore. Note=Expressed in the forespore and
CC       then transported across the inner forespore membrane and deposited on
CC       the outside of the cortex.
CC   -!- DEVELOPMENTAL STAGE: Expressed during sporulation and active during
CC       germination. Exists as mature but inactive form in the dormant spore.
CC   -!- INDUCTION: Expression is sigma G-dependent.
CC   -!- MISCELLANEOUS: B.cereus SleB could not be detected with anti-B.subtilis
CC       SleB antiserum and vice versa.
CC   -!- SIMILARITY: Belongs to the SleB family. {ECO:0000305}.
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DR   EMBL; D63645; BAA09800.1; -; Genomic_DNA.
DR   RefSeq; WP_001249053.1; NZ_WBPP01000045.1.
DR   AlphaFoldDB; P0A3V1; -.
DR   SMR; P0A3V1; -.
DR   STRING; 1396.DJ87_2143; -.
DR   GeneID; 67467074; -.
DR   eggNOG; COG3409; Bacteria.
DR   eggNOG; COG3773; Bacteria.
DR   OMA; KTYMAVR; -.
DR   GO; GO:0042763; C:intracellular immature spore; IEA:UniProtKB-SubCell.
DR   GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
DR   GO; GO:0071555; P:cell wall organization; IEA:UniProtKB-KW.
DR   GO; GO:0009847; P:spore germination; IEA:InterPro.
DR   GO; GO:0030435; P:sporulation resulting in formation of a cellular spore; IEA:UniProtKB-KW.
DR   Gene3D; 1.10.10.2520; -; 1.
DR   Gene3D; 1.10.101.10; -; 1.
DR   InterPro; IPR011105; Cell_wall_hydrolase_SleB.
DR   InterPro; IPR002477; Peptidoglycan-bd-like.
DR   InterPro; IPR036365; PGBD-like_sf.
DR   InterPro; IPR036366; PGBDSf.
DR   InterPro; IPR042047; SleB_dom1.
DR   InterPro; IPR014224; Spore_cortex_SleB.
DR   Pfam; PF07486; Hydrolase_2; 1.
DR   Pfam; PF01471; PG_binding_1; 1.
DR   SUPFAM; SSF47090; SSF47090; 1.
DR   TIGRFAMs; TIGR02869; spore_SleB; 1.
PE   1: Evidence at protein level;
KW   Cell wall biogenesis/degradation; Direct protein sequencing; Germination;
KW   Hydrolase; Signal; Sporulation.
FT   SIGNAL          1..32
FT                   /evidence="ECO:0000269|PubMed:8081503,
FT                   ECO:0000269|PubMed:8752358"
FT   CHAIN           33..259
FT                   /note="Spore cortex-lytic enzyme"
FT                   /id="PRO_0000022355"
FT   REGION          109..142
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MUTAGEN         258
FT                   /note="C->G: Strong decrease in activity."
FT                   /evidence="ECO:0000269|PubMed:8752358"
FT   CONFLICT        46
FT                   /note="D -> K (in Ref. 2; AA sequence)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   259 AA;  28257 MW;  36F266D32EDA544E CRC64;
     MRQKAIFKIA VLLAFIGLSL MVSSIQLKNV EAFSNQVIQR GASGEDVIEL QSRLKYNGFY
     TGKVDGVFGW GTYWALRNFQ EKFGLPVDGL AGAKTKQMLV KATKYDKSTA NKGTTTNKGN
     SGGTAQENKP PQNKGTNVPN GYSQNDIQLM ANAVYGESRG EPYLGQVAVA AVILNRVTSA
     SFPNTVSGVI FEPRAFTAVA DGQIYLTPNE TAKKAVLDAI NGWDPTGNAL YYFNPDTATS
     KWIWTRPQIK KIGKHIFCK