ID A0A974PTR2_9HYPH Unreviewed; 398 AA.
AC A0A974PTR2;
DT 22-FEB-2023, integrated into UniProtKB/TrEMBL.
DT 22-FEB-2023, sequence version 1.
DT 28-JAN-2026, entry version 12.
DE SubName: Full=Lytic murein transglycosylase {ECO:0000313|EMBL:QRG09376.1};
GN ORFNames=EZH22_00020 {ECO:0000313|EMBL:QRG09376.1};
OS Xanthobacter dioxanivorans.
OC Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
OC Hyphomicrobiales; Xanthobacteraceae; Xanthobacter.
OX NCBI_TaxID=2528964 {ECO:0000313|EMBL:QRG09376.1, ECO:0000313|Proteomes:UP000596427};
RN [1] {ECO:0000313|EMBL:QRG09376.1, ECO:0000313|Proteomes:UP000596427}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=YN2 {ECO:0000313|EMBL:QRG09376.1,
RC ECO:0000313|Proteomes:UP000596427};
RA Ma F., Wang Y., Yang J., Guo H., Su D., Yu L.;
RT "Degradation of 1,4-Dioxane by Xanthobacter sp. YN2, via a Novel Group-2
RT Soluble Di-Iron Monooxygenase.";
RL Submitted (OCT-2020) to the EMBL/GenBank/DDBJ databases.
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DR EMBL; CP063362; QRG09376.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A974PTR2; -.
DR KEGG; xdi:EZH22_00020; -.
DR Proteomes; UP000596427; Chromosome.
DR GO; GO:0008933; F:peptidoglycan lytic transglycosylase activity; IEA:TreeGrafter.
DR GO; GO:0009253; P:peptidoglycan catabolic process; IEA:TreeGrafter.
DR Gene3D; 1.10.530.10; -; 1.
DR Gene3D; 1.10.8.350; Bacterial muramidase; 1.
DR Gene3D; 1.10.101.10; PGBD-like superfamily/PGBD; 1.
DR InterPro; IPR023346; Lysozyme-like_dom_sf.
DR InterPro; IPR043426; MltB-like.
DR InterPro; IPR011970; MltB_2.
DR InterPro; IPR002477; Peptidoglycan-bd-like.
DR InterPro; IPR036365; PGBD-like_sf.
DR InterPro; IPR036366; PGBDSf.
DR InterPro; IPR031304; SLT_2.
DR NCBIfam; TIGR02283; MltB_2; 1.
DR PANTHER; PTHR30163:SF8; LYTIC MUREIN TRANSGLYCOSYLASE; 1.
DR PANTHER; PTHR30163; MEMBRANE-BOUND LYTIC MUREIN TRANSGLYCOSYLASE B; 1.
DR Pfam; PF01471; PG_binding_1; 1.
DR Pfam; PF13406; SLT_2; 1.
DR SUPFAM; SSF53955; Lysozyme-like; 1.
DR SUPFAM; SSF47090; PGBD-like; 1.
PE 4: Predicted;
KW Reference proteome {ECO:0000313|Proteomes:UP000596427};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..17
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 18..398
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5037754386"
FT DOMAIN 19..319
FT /note="Transglycosylase SLT"
FT /evidence="ECO:0000259|Pfam:PF13406"
FT DOMAIN 340..392
FT /note="Peptidoglycan binding-like"
FT /evidence="ECO:0000259|Pfam:PF01471"
SQ SEQUENCE 398 AA; 43676 MW; 0C9C314C143E664B CRC64;
MLLAALALQA PARAADAAFT QFIASLWPQA QTAGVSRETF ERETRGLEPD YKLPDLALPG
RPATGASAQA EFVQVPASYV KESTIARLAA EGRRLMQKHR AALDRIEGQF GVPATMVLAL
WGRETDYGRY TSPHDTLRVV ATQAYVGRRK DQYRDEFILA LKILDDGAVA RKDFRSSWAG
ATGLTQFLPS EYYKHGVDLD GDGRVDIWRS VPDALASAAK QLADKGWQPG VRWAYEVRAP
ANADCTLGVP EVKRPIGEWL RSGFAPVERL SAAEQGQPAS LLQPEGTYGP SFLTTKNYFV
IKEYNFSDLY VLFVGHLSDR MVDPQPFVTP WTASTQLRTT SVVAMQKHLT RMGLYGDKID
GKAGMLTRAA LGAYQKSAGL KVDCWPSEAV LQSMGAAR
//