ID A0A0A0F9W8_ECOLX Unreviewed; 241 AA. AC A0A0A0F9W8; DT 07-JAN-2015, integrated into UniProtKB/TrEMBL. DT 07-JAN-2015, sequence version 1. DT 09-DEC-2015, entry version 7. 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; Enterobacteriales; OC Enterobacteriaceae; Escherichia. OX NCBI_TaxID=1455601 {ECO:0000313|EMBL:KGM59240.1}; RN [1] {ECO:0000313|EMBL:KGM59240.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=G3/10 {ECO:0000313|EMBL:KGM59240.1}; RA Zschuettig A., Auerbach C., Meltke S., Eichhorn C., Brandt M., RA Blom J., Goesmann A., Jarek M., Scharfe M., Zimmermann K., RA Wassenaar T.M., Gunzer F.; RT "Complete sequence of probiotic Symbioflor2 E. coli strain G3/10 and RT draft 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: Endolytic cleavage of the (1->4)-beta- CC glycosidic linkage between N-acetylmuramic acid (MurNAc) and N- CC acetylglucosamine (GlcNAc) residues in peptidoglycan with CC concomitant formation of a 1,6-anhydrobond in the MurNAc residue. CC {ECO:0000256|HAMAP-Rule:MF_01381}. 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|HAMAP-Rule:MF_01381}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {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 ProteinModelPortal; A0A0A0F9W8; -. DR EnsemblBacteria; KGM59240; KGM59240; EL76_2828. DR GO; GO:0009279; C:cell outer membrane; IEA:UniProtKB-SubCell. DR GO; GO:0016837; F:carbon-oxygen lyase activity, acting on polysaccharides; IEA:UniProtKB-HAMAP. DR GO; GO:0008932; F:lytic endotransglycosylase activity; IEA:InterPro. DR GO; GO:0016998; P:cell wall macromolecule catabolic process; IEA:UniProtKB-HAMAP. DR GO; GO:0071555; P:cell wall organization; IEA:UniProtKB-KW. DR GO; GO:0000270; P:peptidoglycan metabolic process; IEA:InterPro. DR HAMAP; MF_01381; EmtA; 1. DR InterPro; IPR023946; EmtA. DR InterPro; IPR023346; Lysozyme-like_dom. DR InterPro; IPR000189; Transglyc_AS. DR InterPro; IPR008258; Transglycosylase_SLT_dom_1. DR Pfam; PF01464; SLT; 1. DR SUPFAM; SSF53955; SSF53955; 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|HAMAP-Rule:MF_01381}; KW Glycosyltransferase {ECO:0000313|EMBL:KGM59240.1}; KW Lyase {ECO:0000256|HAMAP-Rule:MF_01381}; KW Membrane {ECO:0000256|HAMAP-Rule:MF_01381}; KW Signal {ECO:0000256|HAMAP-Rule:MF_01381}; KW Transferase {ECO:0000313|EMBL:KGM59240.1}. FT DOMAIN 81 206 SLT. {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 //