ID W4B104_9BACL Unreviewed; 275 AA.
AC W4B104;
DT 19-MAR-2014, integrated into UniProtKB/TrEMBL.
DT 19-MAR-2014, sequence version 1.
DT 24-JAN-2024, entry version 27.
DE RecName: Full=Spore cortex-lytic enzyme {ECO:0000256|ARBA:ARBA00018364};
GN ORFNames=C161_11648 {ECO:0000313|EMBL:ETT37159.1};
OS Paenibacillus sp. FSL R5-192.
OC Bacteria; Bacillota; Bacilli; Bacillales; Paenibacillaceae; Paenibacillus.
OX NCBI_TaxID=1226754 {ECO:0000313|EMBL:ETT37159.1, ECO:0000313|Proteomes:UP000019041};
RN [1] {ECO:0000313|EMBL:ETT37159.1, ECO:0000313|Proteomes:UP000019041}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=FSL R5-192 {ECO:0000313|EMBL:ETT37159.1,
RC ECO:0000313|Proteomes:UP000019041};
RX PubMed=24422886; DOI=10.1186/1471-2164-15-26;
RA Moreno Switt A.I., Andrus A.D., Ranieri M.L., Orsi R.H., Ivy R.,
RA den Bakker H.C., Martin N.H., Wiedmann M., Boor K.J.;
RT "Genomic comparison of sporeforming bacilli isolated from milk.";
RL BMC Genomics 15:26-26(2014).
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:ETT37159.1}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; ASPR01000014; ETT37159.1; -; Genomic_DNA.
DR RefSeq; WP_036670407.1; NZ_ASPR01000014.1.
DR AlphaFoldDB; W4B104; -.
DR GeneID; 83562169; -.
DR PATRIC; fig|1226754.4.peg.2385; -.
DR Proteomes; UP000019041; Unassembled WGS sequence.
DR GO; GO:0016787; F:hydrolase activity; IEA:InterPro.
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; 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 Sporulation {ECO:0000256|ARBA:ARBA00022969}.
FT DOMAIN 59..111
FT /note="Peptidoglycan binding-like"
FT /evidence="ECO:0000259|Pfam:PF01471"
FT DOMAIN 176..274
FT /note="Cell wall hydrolase SleB"
FT /evidence="ECO:0000259|Pfam:PF07486"
FT REGION 119..154
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 134..154
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 275 AA; 29911 MW; 921E9EB2F8DB9D36 CRC64;
MRKMNIWLFT AILLMSALGI RYLLPENAAT ESSNQSTSQV EEKALPTFSS NAVKYGSYGQ
DVYELQGRLK YLGFYNGKID SNFGNSTLKS VKWFQSEFGM KADGVVGAET KLKLYNASTK
WSPTEPPLHK ESSGGGGGSN NTADKEQDNM GSANALGLSE NELKIMANAV YGEARGEPFE
GQVAVAAVIM NRVKSPSFPN TPSGVIFQPG AFTAVADGQI YLEPNAQAKK AVEQALNGWD
PSGGCLYYFN PKTATSKWIW TRPQVKTIGQ HIFCM
//