ID A0A140L6M3_9FIRM Unreviewed; 235 AA.
AC A0A140L6M3;
DT 08-JUN-2016, integrated into UniProtKB/TrEMBL.
DT 08-JUN-2016, sequence version 1.
DT 28-JAN-2026, entry version 25.
DE RecName: Full=Spore cortex-lytic enzyme {ECO:0000256|ARBA:ARBA00018364, ECO:0000256|NCBIfam:TIGR02869};
GN Name=sleB_2 {ECO:0000313|EMBL:KXG76198.1};
GN ORFNames=AN619_11550 {ECO:0000313|EMBL:KXG76198.1};
OS Thermotalea metallivorans.
OC Bacteria; Bacillati; Bacillota; Clostridia; Peptostreptococcales;
OC Thermotaleaceae; Thermotalea.
OX NCBI_TaxID=520762 {ECO:0000313|EMBL:KXG76198.1, ECO:0000313|Proteomes:UP000070456};
RN [1] {ECO:0000313|EMBL:KXG76198.1, ECO:0000313|Proteomes:UP000070456}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=B2-1 {ECO:0000313|EMBL:KXG76198.1,
RC ECO:0000313|Proteomes:UP000070456};
RA Patel B.K.;
RT "Draft genome sequence of the thermoanaerobe Thermotalea metallivorans, an
RT isolate from the runoff channel of the Great Artesian Basin, Australia.";
RL Submitted (DEC-2015) 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:KXG76198.1}.
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; LOEE01000028; KXG76198.1; -; Genomic_DNA.
DR RefSeq; WP_068555648.1; NZ_LOEE01000028.1.
DR AlphaFoldDB; A0A140L6M3; -.
DR STRING; 520762.AN619_11550; -.
DR PATRIC; fig|520762.4.peg.1292; -.
DR OrthoDB; 9785345at2; -.
DR Proteomes; UP000070456; 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 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:UP000070456};
KW Signal {ECO:0000256|ARBA:ARBA00022729};
KW Sporulation {ECO:0000256|ARBA:ARBA00022969}.
FT DOMAIN 41..97
FT /note="Peptidoglycan binding-like"
FT /evidence="ECO:0000259|Pfam:PF01471"
FT DOMAIN 136..233
FT /note="Cell wall hydrolase SleB"
FT /evidence="ECO:0000259|Pfam:PF07486"
SQ SEQUENCE 235 AA; 25723 MW; 869BE3163DA8797F CRC64;
MRTIALFTCM ILIFVFTVGT LYIDSWFSRG EAQETLYWGS SGELVRKLQS TLKDWGYYDG
PVDGVFGGGT FEAVKKFQRK HGLTPDGVVG PATAEKLGFP VKKTEAQTAY RASGSYASRD
DEVTLLAKAI TGEARGEPYI GQVAVGAVIL NRTRHPSFPN TIPGVIYQPG AFTAVSDGQI
NLPPDESCLK AARDALNGWD PTGGCLYYWN PATATSKWIW SRKVVKKIGK HWFGN
//
