ID   A0A239GNT7_9PSED        Unreviewed;       482 AA.
AC   A0A239GNT7;
DT   25-OCT-2017, integrated into UniProtKB/TrEMBL.
DT   25-OCT-2017, sequence version 1.
DT   24-JAN-2024, entry version 16.
DE   SubName: Full=Membrane-bound lytic murein transglycosylase D {ECO:0000313|EMBL:SNS70472.1};
GN   ORFNames=SAMN05444352_11375 {ECO:0000313|EMBL:SNS70472.1};
OS   Pseudomonas japonica.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Pseudomonadales;
OC   Pseudomonadaceae; Pseudomonas.
OX   NCBI_TaxID=256466 {ECO:0000313|EMBL:SNS70472.1, ECO:0000313|Proteomes:UP000198407};
RN   [1] {ECO:0000313|Proteomes:UP000198407}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 22348 {ECO:0000313|Proteomes:UP000198407};
RA   Varghese N., Submissions S.;
RL   Submitted (JUN-2017) to the EMBL/GenBank/DDBJ databases.
CC   -!- SIMILARITY: Belongs to the transglycosylase Slt family.
CC       {ECO:0000256|ARBA:ARBA00007734}.
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DR   EMBL; FZOL01000013; SNS70472.1; -; Genomic_DNA.
DR   RefSeq; WP_042126268.1; NZ_FZOL01000013.1.
DR   AlphaFoldDB; A0A239GNT7; -.
DR   STRING; 1215104.GCA_000730585_02167; -.
DR   OrthoDB; 9815002at2; -.
DR   Proteomes; UP000198407; 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; 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; IPR010511; MltD_lipid-attach.
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; PF06474; MLTD_N; 1.
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   Reference proteome {ECO:0000313|Proteomes:UP000198407}.
FT   DOMAIN          365..408
FT                   /note="LysM"
FT                   /evidence="ECO:0000259|PROSITE:PS51782"
FT   DOMAIN          434..477
FT                   /note="LysM"
FT                   /evidence="ECO:0000259|PROSITE:PS51782"
SQ   SEQUENCE   482 AA;  53648 MW;  9D1FFBCCFE83218B CRC64;
     MSSNSRRTLT PAALTRLAQA VALGLTATLV GCQSTSHMGD NESVRVHVQP RIKQKPVFVQ
     AKPAEQVPQD VWERIRQGFQ LQDDIGVNPR IEQQRLWFAS NPTFLETAGD RGSLYIHYIV
     ERLEERDMPL ELALLPAIES AYNPMAYSRA HAVGLWQFIP STGRHYNLRQ TRFYDGRRDI
     TASTNAALDY LSRLHDMFNG DWLLALAAYN AGEGTVSRAI ERNERVGLPT DYWNLPLPQE
     TRDYVPKLLA LSQVVLTPEA YGVNLNPIAN EPYFEAVAIK DRLDLSRVAA LAEIDEDELF
     QLNPAFKKRM TVDGPQQLLV PTAKAQLLTS SLSSMKPEEL LALQPKAAVF EAALAEASAP
     AARSVRYRVK RGDSLGSIAK ANRVSVKDLQ RWNKISGNRL KAGQTLVLQS SQPITVASAT
     KSVSAGGNGK QRATQYKVKK GDSLYLVAKR FNVEMQHLKR WNPRSGQALK PGQTLTVYLP
     HQ
//