ID A0A0C3DG85_9VIBR Unreviewed; 527 AA.
AC A0A0C3DG85;
DT 01-APR-2015, integrated into UniProtKB/TrEMBL.
DT 01-APR-2015, sequence version 1.
DT 28-JAN-2026, entry version 42.
DE SubName: Full=Murein transglycosylase {ECO:0000313|EMBL:KIN10389.1};
GN ORFNames=SU60_13900 {ECO:0000313|EMBL:KIN10389.1};
OS Vibrio mytili.
OC Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria; Vibrionales;
OC Vibrionaceae; Vibrio.
OX NCBI_TaxID=50718 {ECO:0000313|EMBL:KIN10389.1, ECO:0000313|Proteomes:UP000031977};
RN [1] {ECO:0000313|EMBL:KIN10389.1, ECO:0000313|Proteomes:UP000031977}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CAIM 528 {ECO:0000313|EMBL:KIN10389.1,
RC ECO:0000313|Proteomes:UP000031977};
RA Gonzalez-Castillo A., Gomez-Gil B., Enciso-Ibarra J.;
RT "Draft genome of Vibrio mytili type strain CAIM 528.";
RL Submitted (JAN-2015) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the transglycosylase Slt family.
CC {ECO:0000256|ARBA:ARBA00007734}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:KIN10389.1}.
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DR EMBL; JXOK01000050; KIN10389.1; -; Genomic_DNA.
DR RefSeq; WP_041156039.1; NZ_CBCRVP010000001.1.
DR AlphaFoldDB; A0A0C3DG85; -.
DR STRING; 50718.SU60_13900; -.
DR OrthoDB; 9815002at2; -.
DR Proteomes; UP000031977; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:InterPro.
DR GO; GO:0008932; F:lytic endotransglycosylase activity; IEA:TreeGrafter.
DR GO; GO:0000270; P:peptidoglycan metabolic process; IEA:InterPro.
DR CDD; cd00118; LysM; 3.
DR CDD; cd16894; MltD-like; 1.
DR FunFam; 1.10.530.10:FF:000004; Membrane-bound lytic murein transglycosylase D; 1.
DR Gene3D; 1.10.530.10; -; 1.
DR Gene3D; 3.10.350.10; LysM domain; 3.
DR InterPro; IPR018392; LysM.
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; 3.
DR Pfam; PF01464; SLT; 1.
DR SMART; SM00257; LysM; 3.
DR SUPFAM; SSF54106; LysM domain; 3.
DR SUPFAM; SSF53955; Lysozyme-like; 1.
DR PROSITE; PS00922; TRANSGLYCOSYLASE; 1.
PE 3: Inferred from homology;
KW Reference proteome {ECO:0000313|Proteomes:UP000031977};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..20
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 21..527
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5002163475"
FT DOMAIN 344..387
FT /note="LysM"
FT /evidence="ECO:0000259|SMART:SM00257"
FT DOMAIN 418..462
FT /note="LysM"
FT /evidence="ECO:0000259|SMART:SM00257"
FT DOMAIN 475..519
FT /note="LysM"
FT /evidence="ECO:0000259|SMART:SM00257"
SQ SEQUENCE 527 AA; 58804 MW; FE963B6CC315C579 CRC64;
MRLKYSLALV LLLSGCQVTS PESTTATPET NKAELAAKQA AKAEAKTKQT VTKKKIVKLT
PKVLSPQDQE DVWQRIAMQL EMDIPDNKTV NYYRTWYLKH PNHLKVVSER AKPFLYMITE
RIEERGLPME LALLPVVESS FDAFAYSHGS AAGLWQFVPG TGKMMGLEQN YWYDGRRDVA
ASTDAALDYL EQLNKRFDGS WEHAIAAYNS GGGRVSRAIR KNRKLGKPID FFSLDLPKET
SSYVPKLLAL ADVIANQDKY GLHIPTIDNQ PVLAKVDPQE QLDLAIAAKY AGISVKELQS
YNPAYNQWST SPNGPHELLI PIEKKQAFLA QVEENRGKGM KVARYKVKSG DSLGVLARKY
GTTVNVIRRA NGLSGDNIRI GQYLMIPTST KDDSQYALSA DNRLSKIQST VRGQFKLTHV
VQSGESLWSI AHDNHVSYKS LAKWNGMGPK DTLKKGQKIV IWKQASSKST VRTVFYSVRS
GDTISAIASK FKVKTNDIVK WNSLPKGKYL QPGQKLKLYV DVTKVSA
//
