ID A0A0A0F9W8_ECOLX Unreviewed; 241 AA. AC A0A0A0F9W8; DT 07-JAN-2015, integrated into UniProtKB/TrEMBL. DT 07-JAN-2015, sequence version 1. DT 22-FEB-2023, entry version 20. DE RecName: Full=Endo-type membrane-bound lytic murein transglycosylase A {ECO:0000256|HAMAP-Rule:MF_01381}; DE EC=4.2.2.n2 {ECO:0000256|HAMAP-Rule:MF_01381}; DE AltName: Full=Peptidoglycan lytic endotransglycosylase {ECO:0000256|HAMAP-Rule:MF_01381}; GN Name=emtA {ECO:0000256|HAMAP-Rule:MF_01381}; GN ORFNames=EL76_2828 {ECO:0000313|EMBL:KGM59240.1}; OS Escherichia coli G3/10. OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales; OC Enterobacteriaceae; Escherichia. OX NCBI_TaxID=1455601 {ECO:0000313|EMBL:KGM59240.1, ECO:0000313|Proteomes:UP000030015}; RN [1] {ECO:0000313|EMBL:KGM59240.1, ECO:0000313|Proteomes:UP000030015} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=G3/10 {ECO:0000313|EMBL:KGM59240.1, RC ECO:0000313|Proteomes:UP000030015}; RA Zschuettig A., Auerbach C., Meltke S., Eichhorn C., Brandt M., Blom J., RA Goesmann A., Jarek M., Scharfe M., Zimmermann K., Wassenaar T.M., RA Gunzer F.; RT "Complete sequence of probiotic Symbioflor2 E. coli strain G3/10 and draft RT sequences of Symbioflor2 strains G1/2, G4/9, G5, G6/7 and G8."; RL Submitted (JUL-2014) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Murein-degrading enzyme. May play a role in recycling of CC muropeptides during cell elongation and/or cell division. CC Preferentially cleaves at a distance of more than two disaccharide CC units from the ends of the glycan chain. {ECO:0000256|HAMAP- CC Rule:MF_01381}. CC -!- CATALYTIC ACTIVITY: CC Reaction=Endolytic cleavage of the (1->4)-beta-glycosidic linkage CC between N-acetylmuramic acid (MurNAc) and N-acetylglucosamine CC (GlcNAc) residues in peptidoglycan with concomitant formation of a CC 1,6-anhydrobond in the MurNAc residue.; EC=4.2.2.n2; CC Evidence={ECO:0000256|HAMAP-Rule:MF_01381}; CC -!- CATALYTIC ACTIVITY: CC Reaction=Exolytic cleavage of the (1->4)-beta-glycosidic linkage CC between N-acetylmuramic acid (MurNAc) and N-acetylglucosamine CC (GlcNAc) residues in peptidoglycan, from either the reducing or the CC non-reducing ends of the peptidoglycan chains, with concomitant CC formation of a 1,6-anhydrobond in the MurNAc residue.; EC=4.2.2.n1; CC Evidence={ECO:0000256|ARBA:ARBA00001420}; CC -!- SUBCELLULAR LOCATION: Cell outer membrane {ECO:0000256|HAMAP- CC Rule:MF_01381}; Lipid-anchor {ECO:0000256|HAMAP-Rule:MF_01381}. CC -!- SIMILARITY: Belongs to the transglycosylase Slt family. CC {ECO:0000256|ARBA:ARBA00007734, ECO:0000256|HAMAP-Rule:MF_01381}. 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:KGM59240.1}. 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; JPKI01000003; KGM59240.1; -; Genomic_DNA. DR AlphaFoldDB; A0A0A0F9W8; -. DR EnsemblBacteria; KGM59240; KGM59240; EL76_2828. DR PATRIC; fig|1455601.3.peg.2852; -. DR Proteomes; UP000030015; Unassembled WGS sequence. DR GO; GO:0009279; C:cell outer membrane; IEA:UniProtKB-SubCell. DR GO; GO:0016757; F:glycosyltransferase activity; IEA:UniProtKB-KW. DR GO; GO:0008932; F:lytic endotransglycosylase activity; IEA:InterPro. DR GO; GO:0016998; P:cell wall macromolecule catabolic process; IEA:UniProtKB-UniRule. DR GO; GO:0071555; P:cell wall organization; IEA:UniProtKB-KW. DR GO; GO:0000270; P:peptidoglycan metabolic process; IEA:InterPro. DR CDD; cd16893; LT_MltC_MltE; 1. DR Gene3D; 1.10.530.10; -; 1. DR HAMAP; MF_01381; EmtA; 1. DR InterPro; IPR023946; EmtA. DR InterPro; IPR023346; Lysozyme-like_dom_sf. DR InterPro; IPR000189; Transglyc_AS. DR InterPro; IPR008258; Transglycosylase_SLT_dom_1. DR PANTHER; PTHR37423:SF4; ENDO-TYPE MEMBRANE-BOUND LYTIC MUREIN TRANSGLYCOSYLASE A; 1. DR PANTHER; PTHR37423; SOLUBLE LYTIC MUREIN TRANSGLYCOSYLASE-RELATED; 1. DR Pfam; PF01464; SLT; 1. DR SUPFAM; SSF53955; Lysozyme-like; 1. DR PROSITE; PS00922; TRANSGLYCOSYLASE; 1. PE 3: Inferred from homology; KW Cell outer membrane {ECO:0000256|HAMAP-Rule:MF_01381}; KW Cell wall biogenesis/degradation {ECO:0000256|ARBA:ARBA00023316, KW ECO:0000256|HAMAP-Rule:MF_01381}; KW Glycosyltransferase {ECO:0000313|EMBL:KGM59240.1}; KW Lyase {ECO:0000256|ARBA:ARBA00023239, ECO:0000256|HAMAP-Rule:MF_01381}; KW Membrane {ECO:0000256|HAMAP-Rule:MF_01381}; KW Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|HAMAP-Rule:MF_01381}; KW Transferase {ECO:0000313|EMBL:KGM59240.1}. FT DOMAIN 81..206 FT /note="Transglycosylase SLT" FT /evidence="ECO:0000259|Pfam:PF01464" SQ SEQUENCE 241 AA; 26575 MW; C3CED8A63E1EEC98 CRC64; MKQRHGNSLL TTETKCISCR LGVPLSPQRR FQAIRIEEVK LRWFAFLIVL LAGCSSKHDY TNPPWNAKVP VQRAMQWMPI SQKAGAAWGV DPQLITAIIA IESGGNPNAV SKSNAIGLMQ LKASTSGRDV YRRMGWSGEP TTSELKNPER NISMGAAYLN ILETGPLAGI EDPKVLQYAL VVSYANGAGA LLRTFSSDRK KAISKINDLD ADEFLEHVAR NHPAPQAPRY IYKLEQALDA M //