ID A0A0W0Z974_LEGSP Unreviewed; 523 AA.
AC A0A0W0Z974;
DT 16-MAR-2016, integrated into UniProtKB/TrEMBL.
DT 16-MAR-2016, sequence version 1.
DT 27-MAR-2024, entry version 21.
DE SubName: Full=Membrane bound lytic murein transglycosylase D {ECO:0000313|EMBL:KTD65470.1};
GN Name=mltD {ECO:0000313|EMBL:KTD65470.1};
GN ORFNames=Lspi_0544 {ECO:0000313|EMBL:KTD65470.1};
OS Legionella spiritensis.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Legionellales;
OC Legionellaceae; Legionella.
OX NCBI_TaxID=452 {ECO:0000313|EMBL:KTD65470.1, ECO:0000313|Proteomes:UP000054877};
RN [1] {ECO:0000313|EMBL:KTD65470.1, ECO:0000313|Proteomes:UP000054877}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Mt.St.Helens-9 {ECO:0000313|EMBL:KTD65470.1,
RC ECO:0000313|Proteomes:UP000054877};
RA Burstein D., Amaro F., Zusman T., Lifshitz Z., Cohen O., Gilbert J.A.,
RA Pupko T., Shuman H.A., Segal G.;
RT "Genomic analysis of 38 Legionella species identifies large and diverse
RT effector repertoires.";
RL Submitted (NOV-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:KTD65470.1}.
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; LNYX01000006; KTD65470.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0W0Z974; -.
DR STRING; 452.Lspi_0544; -.
DR PATRIC; fig|452.5.peg.600; -.
DR Proteomes; UP000054877; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:InterPro.
DR GO; GO:0008933; F:lytic transglycosylase activity; IEA:InterPro.
DR GO; GO:0000270; P:peptidoglycan metabolic process; IEA:InterPro.
DR CDD; cd00118; LysM; 3.
DR CDD; cd16894; MltD-like; 1.
DR Gene3D; 1.10.530.10; -; 1.
DR Gene3D; 3.10.350.10; LysM domain; 3.
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; 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; PS51782; LYSM; 3.
DR PROSITE; PS00922; TRANSGLYCOSYLASE; 1.
PE 3: Inferred from homology;
KW Reference proteome {ECO:0000313|Proteomes:UP000054877}.
FT DOMAIN 352..395
FT /note="LysM"
FT /evidence="ECO:0000259|PROSITE:PS51782"
FT DOMAIN 426..470
FT /note="LysM"
FT /evidence="ECO:0000259|PROSITE:PS51782"
FT DOMAIN 478..522
FT /note="LysM"
FT /evidence="ECO:0000259|PROSITE:PS51782"
SQ SEQUENCE 523 AA; 59573 MW; E1B06F330A2C9899 CRC64;
MLRFISNGCE NKHELFETCS YNLKTKKGLS PDNYLVHWQP IHSVQAVTLK VTLSLLARLF
ICFLISYGGI NPAYSRSVPS VWDVLRNQFQ LNHETTQPEV QAQIRWIVAH PSYLQYLAKA
EPYIYHITTE IKKRKLPGEL ALIPMIESTF DPFAYSGAGA AGLWQLMPGT GTTLGLKQDW
WFDARRSIQP STDAALNYLA YLNKFFHGDW ILAIAAYDSG EGTISRAVKS SGRFRNVRFW
NLRVPNETRA YVPRLLALAE VIKYPQRYHV KLPDIPHTPY FEEVNIGSQI DLNHAAKMAG
MTYKELIQLN PGYNRWATAP YKPYKLLIPT DKVAKFNRNL AHVPEEKRVS WMRHQVQKGE
SLSAIASRYF TTVKLIRELN RLRSEKLKTG QFLLIPSSKN TTLSSSKQPV IINAPAQETS
GQPYKVVHIV QSGETYKNLE KKYNVSVAEI SNWNVLDAKM PLRKGQQLII WKKTPKAGVY
IVKAGDSLSR IAKQFNSKVS TLKRLNPHIN ITLIHPGQRL IIG
//
