AC MF_02016; DC Protein; auto TR HAMAP; MF_02016; -; 1; level=0 XX Names: MltF XX ID MLTF DE RecName: Full=Membrane-bound lytic murein transglycosylase F; DE EC=4.2.2.n1; DE AltName: Full=Murein lyase F; DE Flags: Precursor; GN Name=mltF; XX CC -!- FUNCTION: Murein-degrading enzyme that degrades murein glycan strands CC and insoluble, high-molecular weight murein sacculi, with the CC concomitant formation of a 1,6-anhydromuramoyl product. Lytic CC transglycosylases (LTs) play an integral role in the metabolism of the CC peptidoglycan (PG) sacculus. Their lytic action creates space within CC the PG sacculus to allow for its expansion as well as for the insertion CC of various structures such as secretion systems and flagella. 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 -!- SUBCELLULAR LOCATION: Cell outer membrane; Peripheral membrane protein. CC Note=Attached to the inner leaflet of the outer membrane. CC -!- DOMAIN: The N-terminal domain does not have lytic activity and probably CC modulates enzymatic activity. The C-terminal domain is the catalytic CC active domain. CC -!- SIMILARITY: In the N-terminal section; belongs to the bacterial solute- CC binding protein 3 family. CC -!- SIMILARITY: In the C-terminal section; belongs to the transglycosylase CC Slt family. XX DR PROSITE; PS00922; TRANSGLYCOSYLASE; 1; trigger=no DR Pfam; PF00497; SBP_bac_3; 1; trigger=no DR Pfam; PF01464; SLT; 1; trigger=no DR General; Signal; -; 1; trigger=yes XX KW Cell outer membrane KW Cell wall biogenesis/degradation KW Lyase KW Membrane KW Signal XX GO GO:0016998; P:cell wall macromolecule catabolic process GO GO:0008933; F:lytic transglycosylase activity GO GO:0009279; C:cell outer membrane XX FT From: MLTF_ECOLI (P0AGC5) FT REGION 22..269 FT /note="Non-LT domain" FT REGION 270..Cter FT /note="LT domain" FT ACT_SITE 314 FT Condition: E XX Size: 450-537; Related: None; Template: P0AGC5; Scope: Bacteria; Pseudomonadota Fusion: Nter: None Cter: None Duplicate: in ALKEH Plasmid: None Comments: None XX # Revision 1.14 2023/01/26 //