ID A4J6B6_DESRM Unreviewed; 239 AA.
AC A4J6B6;
DT 01-MAY-2007, integrated into UniProtKB/TrEMBL.
DT 01-MAY-2007, sequence version 1.
DT 27-MAR-2024, entry version 78.
DE SubName: Full=Cell wall hydrolase, SleB {ECO:0000313|EMBL:ABO50619.1};
GN OrderedLocusNames=Dred_2102 {ECO:0000313|EMBL:ABO50619.1};
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:ABO50619.1, ECO:0000313|Proteomes:UP000001556};
RN [1] {ECO:0000313|EMBL:ABO50619.1, ECO:0000313|Proteomes:UP000001556}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MI-1 {ECO:0000313|EMBL:ABO50619.1,
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.
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DR EMBL; CP000612; ABO50619.1; -; Genomic_DNA.
DR RefSeq; WP_011878425.1; NC_009253.1.
DR AlphaFoldDB; A4J6B6; -.
DR STRING; 349161.Dred_2102; -.
DR CAZy; CBM50; Carbohydrate-Binding Module Family 50.
DR KEGG; drm:Dred_2102; -.
DR eggNOG; COG3773; Bacteria.
DR HOGENOM; CLU_053345_1_2_9; -.
DR OrthoDB; 9785345at2; -.
DR Proteomes; UP000001556; Chromosome.
DR GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
DR CDD; cd00118; LysM; 1.
DR Gene3D; 6.20.240.60; -; 1.
DR Gene3D; 1.10.10.2520; Cell wall hydrolase SleB, domain 1; 1.
DR Gene3D; 3.10.350.10; LysM domain; 1.
DR InterPro; IPR011105; Cell_wall_hydrolase_SleB.
DR InterPro; IPR018392; LysM_dom.
DR InterPro; IPR036779; LysM_dom_sf.
DR InterPro; IPR042047; SleB_dom1.
DR PANTHER; PTHR33734:SF35; LYSM DOMAIN-CONTAINING GPI-ANCHORED PROTEIN 1; 1.
DR PANTHER; PTHR33734; LYSM DOMAIN-CONTAINING GPI-ANCHORED PROTEIN 2; 1.
DR Pfam; PF07486; Hydrolase_2; 1.
DR Pfam; PF01476; LysM; 1.
DR SMART; SM00257; LysM; 1.
DR SUPFAM; SSF54106; LysM domain; 1.
DR PROSITE; PS51782; LYSM; 1.
PE 4: Predicted;
KW Hydrolase {ECO:0000313|EMBL:ABO50619.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000001556};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..25
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 26..239
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5038522536"
FT DOMAIN 53..96
FT /note="LysM"
FT /evidence="ECO:0000259|PROSITE:PS51782"
SQ SEQUENCE 239 AA; 25933 MW; B48DDB032E47D3B4 CRC64;
MNKKYRKIAT LMAVLVAVTS SFMVATVATG AAGDGAGGLE CEGSDPDRSS SEVYYTVQPG
DTLYQVCRDY HVSLGSLMRA NNLKNTTIYP DQRLVIPTVS ISSYGMVLSR GDVSREDIKL
LARLIHAEAR GETFEGKVAV GAVILNRLVS PGFPKSIREI ILENNNLVYQ FSPVQDGSIN
LEPDEDSMKA ALEALMGRDP TGGALFFYNP IVATDKWIKT LPVVTRIGNH VFATKATKI
//
