ID MLTF_CROS8 Reviewed; 519 AA. AC A7MGZ5; DT 25-NOV-2008, integrated into UniProtKB/Swiss-Prot. DT 02-OCT-2007, sequence version 1. DT 27-MAR-2024, entry version 83. DE RecName: Full=Membrane-bound lytic murein transglycosylase F {ECO:0000255|HAMAP-Rule:MF_02016}; DE EC=4.2.2.n1 {ECO:0000255|HAMAP-Rule:MF_02016}; DE AltName: Full=Murein lyase F {ECO:0000255|HAMAP-Rule:MF_02016}; DE Flags: Precursor; GN Name=mltF {ECO:0000255|HAMAP-Rule:MF_02016}; GN OrderedLocusNames=ESA_00703; OS Cronobacter sakazakii (strain ATCC BAA-894) (Enterobacter sakazakii). OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales; OC Enterobacteriaceae; Cronobacter. OX NCBI_TaxID=290339; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC BAA-894; RX PubMed=20221447; DOI=10.1371/journal.pone.0009556; RA Kucerova E., Clifton S.W., Xia X.Q., Long F., Porwollik S., Fulton L., RA Fronick C., Minx P., Kyung K., Warren W., Fulton R., Feng D., Wollam A., RA Shah N., Bhonagiri V., Nash W.E., Hallsworth-Pepin K., Wilson R.K., RA McClelland M., Forsythe S.J.; RT "Genome sequence of Cronobacter sakazakii BAA-894 and comparative genomic RT hybridization analysis with other Cronobacter species."; RL PLoS ONE 5:E9556-E9556(2010). 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 {ECO:0000255|HAMAP-Rule:MF_02016}. 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:0000255|HAMAP-Rule:MF_02016}; CC -!- SUBCELLULAR LOCATION: Cell outer membrane; Peripheral membrane protein. CC Note=Attached to the inner leaflet of the outer membrane. CC {ECO:0000255|HAMAP-Rule:MF_02016}. 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. {ECO:0000255|HAMAP-Rule:MF_02016}. CC -!- SIMILARITY: In the N-terminal section; belongs to the bacterial solute- CC binding protein 3 family. {ECO:0000255|HAMAP-Rule:MF_02016}. CC -!- SIMILARITY: In the C-terminal section; belongs to the transglycosylase CC Slt family. {ECO:0000255|HAMAP-Rule:MF_02016}. 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; CP000783; ABU75981.1; -; Genomic_DNA. DR RefSeq; WP_012124025.1; NC_009778.1. DR AlphaFoldDB; A7MGZ5; -. DR SMR; A7MGZ5; -. DR CAZy; GH23; Glycoside Hydrolase Family 23. DR KEGG; esa:ESA_00703; -. DR PATRIC; fig|290339.8.peg.621; -. DR HOGENOM; CLU_027494_0_1_6; -. DR Proteomes; UP000000260; Chromosome. DR GO; GO:0009279; C:cell outer membrane; IEA:UniProtKB-SubCell. DR GO; GO:0008933; F:lytic transglycosylase activity; IEA:UniProtKB-UniRule. 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 CDD; cd13403; MLTF-like; 1. DR CDD; cd01009; PBP2_YfhD_N; 1. DR Gene3D; 1.10.530.10; -; 1. DR Gene3D; 3.40.190.10; Periplasmic binding protein-like II; 2. DR HAMAP; MF_02016; MltF; 1. DR InterPro; IPR023346; Lysozyme-like_dom_sf. DR InterPro; IPR023703; MltF. DR InterPro; IPR001638; Solute-binding_3/MltF_N. DR InterPro; IPR008258; Transglycosylase_SLT_dom_1. DR PANTHER; PTHR35936; MEMBRANE-BOUND LYTIC MUREIN TRANSGLYCOSYLASE F; 1. DR PANTHER; PTHR35936:SF32; MEMBRANE-BOUND LYTIC MUREIN TRANSGLYCOSYLASE F; 1. DR Pfam; PF00497; SBP_bac_3; 1. DR Pfam; PF01464; SLT; 1. DR SMART; SM00062; PBPb; 1. DR SUPFAM; SSF53955; Lysozyme-like; 1. DR SUPFAM; SSF53850; Periplasmic binding protein-like II; 1. PE 3: Inferred from homology; KW Cell outer membrane; Cell wall biogenesis/degradation; Lyase; Membrane; KW Reference proteome; Signal. FT SIGNAL 1..32 FT /evidence="ECO:0000255|HAMAP-Rule:MF_02016" FT CHAIN 33..519 FT /note="Membrane-bound lytic murein transglycosylase F" FT /id="PRO_0000353936" FT REGION 33..269 FT /note="Non-LT domain" FT /evidence="ECO:0000255|HAMAP-Rule:MF_02016" FT REGION 270..519 FT /note="LT domain" FT /evidence="ECO:0000255|HAMAP-Rule:MF_02016" FT REGION 495..519 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 504..519 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT ACT_SITE 314 FT /evidence="ECO:0000255|HAMAP-Rule:MF_02016" SQ SEQUENCE 519 AA; 57617 MW; 818FB065D8B03B13 CRC64; MKKLKLNYLL IGVVTLLLAV ALWPAIPWSG KADNRIAAIQ ARGVLRVSTI ATPLTMYRAG DTMSGLDYEL SQAFADYLGV KLKITVRQNI SQLFDDLDNN DADLLAAGLV YNEARSQHYQ AGPIYYSVSQ QMVYRVGSLR PRSLASIKEG QLTIAPGHVA QSELEQLKAS KYPDLTWRVD PKLSSNELML QVAQGTLDYT IADSVAISLF QRVHPQLAVA LDLSDEQPVT WFSRRSSDNS LSAALLDFFN QINEDGTLAR LEEKYLGHGN DFDYVDTRSF LRAVDSVLPE LQPLFEKYAT DIDWRLLAAI SYQESHWDSQ ATSPTGVRGL MMLTRNTAQS LGLTDRLDAE QSISGGARYL KDMMSKVPES VPEEERIWFA LAAYNMGYAH MLDARALTAK QKGNPDSWSD VKQRLPLLSQ RPYYSKLTYG YARGHEAYAY VENIRKYQIS LVGYLLEKEK QAAAAAQPKL VQSYPTNITP QGLFPSPFSS LPLGPFSQAG AGGKTHSALP NTLSPVSPR //