SLEB_ALKHC
ID SLEB_ALKHC Reviewed; 330 AA.
AC Q9KCE0; Q9RC83;
DT 25-NOV-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 108.
DE RecName: Full=Spore cortex-lytic enzyme;
DE Short=SCLE;
DE Flags: Precursor;
GN Name=sleB; OrderedLocusNames=BH1631;
OS Alkalihalobacillus halodurans (strain ATCC BAA-125 / DSM 18197 / FERM 7344
OS / JCM 9153 / C-125) (Bacillus halodurans).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Alkalihalobacillus.
OX NCBI_TaxID=272558;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-125 / DSM 18197 / FERM 7344 / JCM 9153 / C-125;
RX PubMed=11058132; DOI=10.1093/nar/28.21.4317;
RA Takami H., Nakasone K., Takaki Y., Maeno G., Sasaki R., Masui N., Fuji F.,
RA Hirama C., Nakamura Y., Ogasawara N., Kuhara S., Horikoshi K.;
RT "Complete genome sequence of the alkaliphilic bacterium Bacillus halodurans
RT and genomic sequence comparison with Bacillus subtilis.";
RL Nucleic Acids Res. 28:4317-4331(2000).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 95-330.
RC STRAIN=ATCC BAA-125 / DSM 18197 / FERM 7344 / JCM 9153 / C-125;
RX PubMed=10484179; DOI=10.1007/s007920050120;
RA Takami H., Takaki Y., Nakasone K., Sakiyama T., Maeno G., Sasaki R.,
RA Hirama C., Fuji F., Masui N.;
RT "Genetic analysis of the chromosome of alkaliphilic Bacillus halodurans C-
RT 125.";
RL Extremophiles 3:227-233(1999).
CC -!- FUNCTION: Required for spore cortex hydrolysis during germination.
CC {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the SleB family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAA83916.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; BA000004; BAB05350.1; -; Genomic_DNA.
DR EMBL; AB024552; BAA83916.1; ALT_INIT; Genomic_DNA.
DR PIR; G83853; G83853.
DR RefSeq; WP_010897794.1; NC_002570.2.
DR AlphaFoldDB; Q9KCE0; -.
DR SMR; Q9KCE0; -.
DR STRING; 272558.10174248; -.
DR EnsemblBacteria; BAB05350; BAB05350; BAB05350.
DR KEGG; bha:BH1631; -.
DR eggNOG; COG3409; Bacteria.
DR eggNOG; COG3773; Bacteria.
DR HOGENOM; CLU_053345_0_0_9; -.
DR OMA; WAVRNYQ; -.
DR OrthoDB; 682655at2; -.
DR Proteomes; UP000001258; Chromosome.
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 3: Inferred from homology;
KW Cell wall biogenesis/degradation; Germination; Hydrolase;
KW Reference proteome; Signal; Sporulation.
FT SIGNAL 1..29
FT /evidence="ECO:0000255"
FT CHAIN 30..330
FT /note="Spore cortex-lytic enzyme"
FT /id="PRO_0000022357"
FT REGION 117..195
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 131..175
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 176..190
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 330 AA; 36565 MW; 790413286D28C51D CRC64;
MSTRGWLKIP LLSLALFLSL MSMTTTAHAF SDQVIQHGAT GDDVVELQAR LQYIGFYNKK
IDGVFGWSTY WAVRNYQYEF GMEVDGLVGP EMKAKLEKTT NFNRDFVDRA LTQGRKFTHY
GGVPKQIQKG PKGSADERRR GREGVRQPRA DRPGRDAPAA PRDERAPRRE ERPAPTPEPT
PAPPEEPTPY EEAPDAQDDE ANIEKATNVP AGYSDNDIQL MAQAVYGEAR GEPYVGQVAV
AAVILNRLNS PTFPDNVSGV IFEPLAFTAV ADGQIYMTPD ETARRAVLDA LNGQDPSGGA
TYYFNPDTAT SGWIWSRPQI KRIGKHIFCN