ID A0A1J4T5M9_9DELT Unreviewed; 137 AA. AC A0A1J4T5M9; DT 15-FEB-2017, integrated into UniProtKB/TrEMBL. DT 15-FEB-2017, sequence version 1. DT 14-DEC-2022, entry version 14. DE RecName: Full=Lysozyme {ECO:0000256|RuleBase:RU003788}; DE EC=3.2.1.17 {ECO:0000256|RuleBase:RU003788}; GN ORFNames=AUJ49_00205 {ECO:0000313|EMBL:OIO06157.1}; OS Desulfovibrionaceae bacterium CG1_02_65_16. OC Bacteria; Proteobacteria; Deltaproteobacteria; Desulfovibrionales; OC Desulfovibrionaceae. OX NCBI_TaxID=1805130 {ECO:0000313|EMBL:OIO06157.1, ECO:0000313|Proteomes:UP000183907}; RN [1] {ECO:0000313|EMBL:OIO06157.1, ECO:0000313|Proteomes:UP000183907} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=CG1_02_65_16 {ECO:0000313|EMBL:OIO06157.1}; RX PubMed=27112493; RA Probst A.J., Castelle C.J., Singh A., Brown C.T., Anantharaman K., RA Sharon I., Hug L.A., Burstein D., Emerson J.B., Thomas B.C., Banfield J.F.; RT "Genomic resolution of a cold subsurface aquifer community provides RT metabolic insights for novel microbes adapted to high CO concentrations."; RL Environ. Microbiol. 0:0-0(2016). CC -!- CATALYTIC ACTIVITY: CC Reaction=Hydrolysis of (1->4)-beta-linkages between N-acetylmuramic CC acid and N-acetyl-D-glucosamine residues in a peptidoglycan and CC between N-acetyl-D-glucosamine residues in chitodextrins.; CC EC=3.2.1.17; Evidence={ECO:0000256|ARBA:ARBA00000632, CC ECO:0000256|RuleBase:RU003788}; CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 24 family. CC {ECO:0000256|RuleBase:RU003788}. 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:OIO06157.1}. 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; MNUQ01000003; OIO06157.1; -; Genomic_DNA. DR AlphaFoldDB; A0A1J4T5M9; -. DR Proteomes; UP000183907; Unassembled WGS sequence. DR GO; GO:0003796; F:lysozyme activity; IEA:UniProtKB-EC. DR GO; GO:0016998; P:cell wall macromolecule catabolic process; IEA:InterPro. DR GO; GO:0019835; P:cytolysis; IEA:UniProtKB-KW. DR GO; GO:0042742; P:defense response to bacterium; IEA:UniProtKB-KW. DR GO; GO:0009253; P:peptidoglycan catabolic process; IEA:InterPro. DR Gene3D; 1.10.530.40; -; 1. DR InterPro; IPR002196; Glyco_hydro_24. DR InterPro; IPR023346; Lysozyme-like_dom_sf. DR InterPro; IPR023347; Lysozyme_dom_sf. DR Pfam; PF00959; Phage_lysozyme; 1. DR SUPFAM; SSF53955; Lysozyme-like; 1. PE 3: Inferred from homology; KW Antimicrobial {ECO:0000256|ARBA:ARBA00022529, KW ECO:0000256|RuleBase:RU003788}; KW Bacteriolytic enzyme {ECO:0000256|ARBA:ARBA00022638, KW ECO:0000256|RuleBase:RU003788}; KW Glycosidase {ECO:0000256|RuleBase:RU003788}; KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|RuleBase:RU003788}. SQ SEQUENCE 137 AA; 14932 MW; 5C6CF74EB5A7CD1B CRC64; MNRQRLADQL IVDEGLKLKP YRCTAGRLTI GVGRNLDDRG ITRGEALFLL GNDIDDCWAR LLNTLAWLEN APEPVQEALT NMAFNLGVAG LLEFRQTLAA LAARDYAGAA RLMLASKWAR QVGPRAARLA QAVKSAG //