ID A0A2P8HW62_9BACI Unreviewed; 313 AA.
AC A0A2P8HW62;
DT 23-MAY-2018, integrated into UniProtKB/TrEMBL.
DT 23-MAY-2018, sequence version 1.
DT 28-JAN-2026, entry version 26.
DE RecName: Full=Spore cortex-lytic enzyme {ECO:0000256|ARBA:ARBA00018364, ECO:0000256|NCBIfam:TIGR02869};
GN ORFNames=B0H94_10385 {ECO:0000313|EMBL:PSL50473.1};
OS Salsuginibacillus halophilus.
OC Bacteria; Bacillati; Bacillota; Bacilli; Bacillales; Bacillaceae;
OC Salsuginibacillus.
OX NCBI_TaxID=517424 {ECO:0000313|EMBL:PSL50473.1, ECO:0000313|Proteomes:UP000242310};
RN [1] {ECO:0000313|EMBL:PSL50473.1, ECO:0000313|Proteomes:UP000242310}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CGMCC 1.07653 {ECO:0000313|EMBL:PSL50473.1,
RC ECO:0000313|Proteomes:UP000242310};
RA Whitman W.;
RT "Genomic Encyclopedia of Type Strains, Phase III (KMG-III): the genomes of
RT soil and plant-associated and newly described type strains.";
RL Submitted (MAR-2018) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the SleB family.
CC {ECO:0000256|ARBA:ARBA00007010}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:PSL50473.1}.
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DR EMBL; PYAV01000003; PSL50473.1; -; Genomic_DNA.
DR RefSeq; WP_427909925.1; NZ_PYAV01000003.1.
DR AlphaFoldDB; A0A2P8HW62; -.
DR Proteomes; UP000242310; Unassembled WGS sequence.
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:UniProtKB-UniRule.
DR GO; GO:0030435; P:sporulation resulting in formation of a cellular spore; IEA:UniProtKB-KW.
DR FunFam; 1.10.10.2520:FF:000001; Spore cortex-lytic enzyme; 1.
DR FunFam; 6.20.240.60:FF:000001; Spore cortex-lytic enzyme; 1.
DR Gene3D; 6.20.240.60; -; 1.
DR Gene3D; 1.10.10.2520; Cell wall hydrolase SleB, domain 1; 1.
DR Gene3D; 1.10.101.10; PGBD-like superfamily/PGBD; 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 NCBIfam; TIGR02869; spore_SleB; 1.
DR Pfam; PF07486; Hydrolase_2; 1.
DR Pfam; PF01471; PG_binding_1; 1.
DR SUPFAM; SSF47090; PGBD-like; 1.
PE 3: Inferred from homology;
KW Cell wall biogenesis/degradation {ECO:0000256|ARBA:ARBA00023316};
KW Germination {ECO:0000256|ARBA:ARBA00022544};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Reference proteome {ECO:0000313|Proteomes:UP000242310};
KW Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP};
KW Sporulation {ECO:0000256|ARBA:ARBA00022969}.
FT SIGNAL 1..30
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 31..313
FT /note="Spore cortex-lytic enzyme"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5015175583"
FT DOMAIN 41..97
FT /note="Peptidoglycan binding-like"
FT /evidence="ECO:0000259|Pfam:PF01471"
FT DOMAIN 214..312
FT /note="Cell wall hydrolase SleB"
FT /evidence="ECO:0000259|Pfam:PF07486"
FT REGION 118..182
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 172..182
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 313 AA; 33938 MW; F3A307E923793FB2 CRC64;
MQQMLQTTVR LIIICSGVIC LSFPAATVDA FSEQTIQRGA TGDDVVELQA RLQYNGYYEG
TIDGVYGWGT YWAVRNFQEA FGLEVDGLVG NEMKDRLVEA TSYDEAFVQR MLQEGRSFTH
YGGTPLENQK GPAPDTGSGG TGESAPPAEG DQSPPEGEGD EGEPPDTGGN EAADEEVTEE
DGEADIHQAM NVPDGFSDND IQMLANAVHG EARGEPYTGQ VAVAAVIINR MNSDEFPDTV
NGVVFEPLAF EAVMDGQIWL EPNEESRQAV LDAINGQDPT GGALYFFNPE TAESDWIWSR
PQIKQIGKHI FAE
//
