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Database: UniProt
Entry: A0A124FTA6_9FIRM
LinkDB: A0A124FTA6_9FIRM
Original site: A0A124FTA6_9FIRM 
ID   A0A124FTA6_9FIRM        Unreviewed;       236 AA.
AC   A0A124FTA6;
DT   13-APR-2016, integrated into UniProtKB/TrEMBL.
DT   13-APR-2016, sequence version 1.
DT   13-SEP-2023, entry version 21.
DE   RecName: Full=Spore cortex-lytic enzyme {ECO:0000256|ARBA:ARBA00018364};
GN   ORFNames=XD84_1119 {ECO:0000313|EMBL:KUK64822.1};
OS   Desulfotomaculum sp. 46_80.
OC   Bacteria; Bacillota; Clostridia; Eubacteriales; Desulfotomaculaceae;
OC   Desulfotomaculum.
OX   NCBI_TaxID=1641375 {ECO:0000313|EMBL:KUK64822.1, ECO:0000313|Proteomes:UP000053828};
RN   [1] {ECO:0000313|Proteomes:UP000053828}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=26787827; DOI=10.1128/mbio.01669-15;
RA   Hu P., Tom L., Singh A., Thomas B.C., Baker B.J., Piceno Y.M.,
RA   Andersen G.L., Banfield J.F.;
RT   "Genome-Resolved Metagenomic Analysis Reveals Roles for Candidate Phyla and
RT   Other Microbial Community Members in Biogeochemical Transformations in Oil
RT   Reservoirs.";
RL   MBio 7:e01669-15(2015).
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:KUK64822.1}.
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DR   EMBL; LGGF01000018; KUK64822.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A124FTA6; -.
DR   PATRIC; fig|1641375.3.peg.795; -.
DR   Proteomes; UP000053828; 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          41..97
FT                   /note="Peptidoglycan binding-like"
FT                   /evidence="ECO:0000259|Pfam:PF01471"
FT   DOMAIN          137..235
FT                   /note="Cell wall hydrolase SleB"
FT                   /evidence="ECO:0000259|Pfam:PF07486"
SQ   SEQUENCE   236 AA;  25335 MW;  DC820A3CB1F2DE56 CRC64;
     MNKYKSAVVL FIAFLVLGGF VIFSNAEKAP AQNRPVYWGL TGNDVSRLQQ TLYDWGYYPG
     PVDGVFGNTT YRSLISFQAN NGLASDGVAG PATWAALGFS SGSDPDSQPA PAEVSRGVSN
     RDETHLLARV IEGEAANESF AGKVAVGAVI LNRLESAAFP HSLAGIVYQP GAFESVSNGQ
     YDRPLTDDSL RAATMAMSGW DPTGGALYFW NPAKPVSPWV WTRNVVTQIG RHIFAR
//
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