ID A4J9E4_DESRM Unreviewed; 234 AA.
AC A4J9E4;
DT 01-MAY-2007, integrated into UniProtKB/TrEMBL.
DT 01-MAY-2007, sequence version 1.
DT 27-MAR-2024, entry version 75.
DE RecName: Full=Spore cortex-lytic enzyme {ECO:0000256|ARBA:ARBA00018364};
GN OrderedLocusNames=Dred_3195 {ECO:0000313|EMBL:ABO51697.1};
OS Desulforamulus reducens (strain ATCC BAA-1160 / DSM 100696 / MI-1)
OS (Desulfotomaculum reducens).
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Peptococcaceae;
OC Desulforamulus.
OX NCBI_TaxID=349161 {ECO:0000313|EMBL:ABO51697.1, ECO:0000313|Proteomes:UP000001556};
RN [1] {ECO:0000313|EMBL:ABO51697.1, ECO:0000313|Proteomes:UP000001556}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MI-1 {ECO:0000313|EMBL:ABO51697.1,
RC ECO:0000313|Proteomes:UP000001556};
RG US DOE Joint Genome Institute;
RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S.,
RA Sims D., Brettin T., Bruce D., Han C., Tapia R., Schmutz J., Larimer F.,
RA Land M., Hauser L., Kyrpides N., Kim E., Tebo B.M., Richardson P.;
RT "Complete sequence of Desulfotomaculum reducens MI-1.";
RL Submitted (MAR-2007) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the SleB family.
CC {ECO:0000256|ARBA:ARBA00007010}.
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DR EMBL; CP000612; ABO51697.1; -; Genomic_DNA.
DR RefSeq; WP_011879485.1; NC_009253.1.
DR AlphaFoldDB; A4J9E4; -.
DR STRING; 349161.Dred_3195; -.
DR KEGG; drm:Dred_3195; -.
DR eggNOG; COG3409; Bacteria.
DR eggNOG; COG3773; Bacteria.
DR HOGENOM; CLU_053345_0_0_9; -.
DR OrthoDB; 9785345at2; -.
DR Proteomes; UP000001556; 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; 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:0000313|EMBL:ABO51697.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000001556};
KW Signal {ECO:0000256|SAM:SignalP};
KW Sporulation {ECO:0000256|ARBA:ARBA00022969}.
FT SIGNAL 1..28
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 29..234
FT /note="Spore cortex-lytic enzyme"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5002670756"
FT DOMAIN 38..94
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 234 AA; 25641 MW; AE4C5F963562B6F0 CRC64;
MQLGNKKKYL IWFITAIFLC SVAGYAFAQN DTLYWGSSGT KVRAVQQRLK DWGYYDGPVD
GYFSGKTASA VRKFQAYHGL ATDGIVGPKT FSAMGLYTPP RKTTYTAKTT TTGVYVGNDH
NINLLARVIM GEAADEPYVG KVAVGAVLLN RTRSSSFPQT LSGVVYQPMA FESVSNGQYN
RALSPEAVKA ARDALAGYDP TGGAIFFWNP YKPVSKWIWS RSIVTQIGNH VFAK
//
