ID A0A068R0I4_9GAMM Unreviewed; 443 AA.
AC A0A068R0I4;
DT 01-OCT-2014, integrated into UniProtKB/TrEMBL.
DT 01-OCT-2014, sequence version 1.
DT 24-JAN-2024, entry version 37.
DE RecName: Full=peptidoglycan lytic exotransglycosylase {ECO:0000256|ARBA:ARBA00012587};
DE EC=4.2.2.n1 {ECO:0000256|ARBA:ARBA00012587};
GN Name=mltD {ECO:0000313|EMBL:CDG20431.1};
GN ORFNames=XPG1_0776 {ECO:0000313|EMBL:CDG20431.1};
OS Xenorhabdus poinarii G6.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC Morganellaceae; Xenorhabdus.
OX NCBI_TaxID=1354304 {ECO:0000313|EMBL:CDG20431.1, ECO:0000313|Proteomes:UP000032735};
RN [1] {ECO:0000313|EMBL:CDG20431.1, ECO:0000313|Proteomes:UP000032735}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=G6 {ECO:0000313|EMBL:CDG20431.1,
RC ECO:0000313|Proteomes:UP000032735};
RA Genoscope - CEA;
RL Submitted (JUL-2013) to the EMBL/GenBank/DDBJ databases.
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 -!- SIMILARITY: Belongs to the transglycosylase Slt family.
CC {ECO:0000256|ARBA:ARBA00007734}.
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DR EMBL; FO704551; CDG20431.1; -; Genomic_DNA.
DR RefSeq; WP_045957851.1; NZ_FO704551.1.
DR AlphaFoldDB; A0A068R0I4; -.
DR STRING; 1354304.XPG1_0776; -.
DR KEGG; xpo:XPG1_0776; -.
DR HOGENOM; CLU_009520_1_4_6; -.
DR OrthoDB; 9815002at2; -.
DR Proteomes; UP000032735; Chromosome.
DR GO; GO:0016020; C:membrane; IEA:InterPro.
DR GO; GO:0008933; F:lytic transglycosylase activity; IEA:InterPro.
DR GO; GO:0071555; P:cell wall organization; IEA:UniProtKB-KW.
DR GO; GO:0000270; P:peptidoglycan metabolic process; IEA:InterPro.
DR CDD; cd00118; LysM; 2.
DR CDD; cd16894; MltD-like; 1.
DR Gene3D; 1.10.530.10; -; 1.
DR Gene3D; 3.10.350.10; LysM domain; 2.
DR InterPro; IPR018392; LysM_dom.
DR InterPro; IPR036779; LysM_dom_sf.
DR InterPro; IPR023346; Lysozyme-like_dom_sf.
DR InterPro; IPR000189; Transglyc_AS.
DR InterPro; IPR008258; Transglycosylase_SLT_dom_1.
DR PANTHER; PTHR33734; LYSM DOMAIN-CONTAINING GPI-ANCHORED PROTEIN 2; 1.
DR PANTHER; PTHR33734:SF22; MEMBRANE-BOUND LYTIC MUREIN TRANSGLYCOSYLASE D; 1.
DR Pfam; PF01476; LysM; 2.
DR Pfam; PF01464; SLT; 1.
DR SMART; SM00257; LysM; 2.
DR SUPFAM; SSF54106; LysM domain; 2.
DR SUPFAM; SSF53955; Lysozyme-like; 1.
DR PROSITE; PS51782; LYSM; 2.
DR PROSITE; PS51257; PROKAR_LIPOPROTEIN; 1.
DR PROSITE; PS00922; TRANSGLYCOSYLASE; 1.
PE 3: Inferred from homology;
KW Cell wall biogenesis/degradation {ECO:0000256|ARBA:ARBA00023316};
KW Lyase {ECO:0000256|ARBA:ARBA00023239}.
FT DOMAIN 346..390
FT /note="LysM"
FT /evidence="ECO:0000259|PROSITE:PS51782"
FT DOMAIN 396..440
FT /note="LysM"
FT /evidence="ECO:0000259|PROSITE:PS51782"
FT REGION 23..54
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 23..45
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 443 AA; 50128 MW; DE2F26819783ECEF CRC64;
MKTKAILFAS VLLAGCQSSL QPKVPSQQQA QKMSSTNQRT ESIAGSEDPA NWKASPTARQ
DLWGHIRDEL KMEVPDNNRI SEQQSYYLKH KKYLQNVILR AGPYIYWIVE QIDARHMPME
LVLLPVVESA FNPHATSYAK AAGLWQIIPS TGRHYGLTQD KWFDARRDVA ASTTGALDML
QSLNTQFNGD WLLTIAAYNS GEGRVRRAIR ENQAQGKPTD FWSLSLPRET MHYVPKILAL
SDIIRHNDKF GFALPEPNSQ QALAKVEVGQ QIMLSQAAEL SGLSLTSIKA YNPGYKRGMT
SPHGPHYIML PRKNINQFKM SLANKNVLKD IQREVAQTTR QLQQRNHYIV RAGDTLSTIA
KHFNTTHRNL QRLNGLKTAD RLKIGQVLKI NNDGPITYHV QKGDSFSSIA KYHDVNLNDL
RNWNENVKVK DMKPGMALTL YLN
//
