ID   SLEB_BACCR              Reviewed;         259 AA.
AC   P0A3V0; P70874;
DT   15-MAR-2005, integrated into UniProtKB/Swiss-Prot.
DT   15-MAR-2005, sequence version 1.
DT   25-MAY-2022, entry version 89.
DE   RecName: Full=Spore cortex-lytic enzyme;
DE            Short=SCLE;
DE   AltName: Full=Germination-specific amidase;
DE   Flags: Precursor;
GN   Name=sleB; OrderedLocusNames=BC_2753;
OS   Bacillus cereus (strain ATCC 14579 / DSM 31 / CCUG 7414 / JCM 2152 / NBRC
OS   15305 / NCIMB 9373 / NCTC 2599 / NRRL B-3711).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus;
OC   Bacillus cereus group.
OX   NCBI_TaxID=226900;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 14579 / DSM 31 / CCUG 7414 / JCM 2152 / NBRC 15305 / NCIMB 9373
RC   / NCTC 2599 / NRRL B-3711;
RX   PubMed=12721630; DOI=10.1038/nature01582;
RA   Ivanova N., Sorokin A., Anderson I., Galleron N., Candelon B., Kapatral V.,
RA   Bhattacharyya A., Reznik G., Mikhailova N., Lapidus A., Chu L., Mazur M.,
RA   Goltsman E., Larsen N., D'Souza M., Walunas T., Grechkin Y., Pusch G.,
RA   Haselkorn R., Fonstein M., Ehrlich S.D., Overbeek R., Kyrpides N.C.;
RT   "Genome sequence of Bacillus cereus and comparative analysis with Bacillus
RT   anthracis.";
RL   Nature 423:87-91(2003).
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 (By similarity). {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Forespore {ECO:0000250}. Note=Expressed in the
CC       forespore and then transported across the inner forespore membrane and
CC       deposited on the outside of the cortex. {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the SleB family. {ECO:0000305}.
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DR   EMBL; AE016877; AAP09706.1; -; Genomic_DNA.
DR   RefSeq; NP_832505.1; NC_004722.1.
DR   RefSeq; WP_001249053.1; NZ_CP034551.1.
DR   PDB; 4F55; X-ray; 1.85 A; A=136-259.
DR   PDB; 6TCI; X-ray; 1.47 A; A=32-105.
DR   PDBsum; 4F55; -.
DR   PDBsum; 6TCI; -.
DR   AlphaFoldDB; P0A3V0; -.
DR   SMR; P0A3V0; -.
DR   STRING; 226900.BC_2753; -.
DR   EnsemblBacteria; AAP09706; AAP09706; BC_2753.
DR   GeneID; 67467074; -.
DR   KEGG; bce:BC2753; -.
DR   PATRIC; fig|226900.8.peg.2808; -.
DR   HOGENOM; CLU_053345_0_0_9; -.
DR   OMA; KTYMAVR; -.
DR   Proteomes; UP000001417; Chromosome.
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   3D-structure; Cell wall biogenesis/degradation; Germination; Hydrolase;
KW   Reference proteome; Signal; Sporulation.
FT   SIGNAL          1..32
FT                   /evidence="ECO:0000250"
FT   CHAIN           33..259
FT                   /note="Spore cortex-lytic enzyme"
FT                   /id="PRO_0000022356"
FT   REGION          109..142
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   HELIX           45..56
FT                   /evidence="ECO:0007829|PDB:6TCI"
FT   HELIX           70..82
FT                   /evidence="ECO:0007829|PDB:6TCI"
FT   HELIX           93..102
FT                   /evidence="ECO:0007829|PDB:6TCI"
FT   HELIX           144..158
FT                   /evidence="ECO:0007829|PDB:4F55"
FT   HELIX           163..178
FT                   /evidence="ECO:0007829|PDB:4F55"
FT   HELIX           186..191
FT                   /evidence="ECO:0007829|PDB:4F55"
FT   HELIX           197..201
FT                   /evidence="ECO:0007829|PDB:4F55"
FT   STRAND          204..206
FT                   /evidence="ECO:0007829|PDB:4F55"
FT   HELIX           210..220
FT                   /evidence="ECO:0007829|PDB:4F55"
FT   STRAND          231..233
FT                   /evidence="ECO:0007829|PDB:4F55"
FT   TURN            235..237
FT                   /evidence="ECO:0007829|PDB:4F55"
FT   HELIX           241..245
FT                   /evidence="ECO:0007829|PDB:4F55"
FT   STRAND          248..252
FT                   /evidence="ECO:0007829|PDB:4F55"
FT   STRAND          255..258
FT                   /evidence="ECO:0007829|PDB:4F55"
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