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Database: UniProt
Entry: A0A1I6PK33_9FLAO
LinkDB: A0A1I6PK33_9FLAO
Original site: A0A1I6PK33_9FLAO 
ID   A0A1I6PK33_9FLAO        Unreviewed;       512 AA.
AC   A0A1I6PK33;
DT   22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT   22-NOV-2017, sequence version 1.
DT   24-JAN-2024, entry version 18.
DE   SubName: Full=Membrane-bound lytic murein transglycosylase D {ECO:0000313|EMBL:SFS40577.1};
GN   ORFNames=SAMN04488006_1121 {ECO:0000313|EMBL:SFS40577.1};
OS   Lutibacter maritimus.
OC   Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales;
OC   Flavobacteriaceae; Lutibacter.
OX   NCBI_TaxID=593133 {ECO:0000313|EMBL:SFS40577.1, ECO:0000313|Proteomes:UP000199312};
RN   [1] {ECO:0000313|Proteomes:UP000199312}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 24450 {ECO:0000313|Proteomes:UP000199312};
RA   Varghese N., Submissions S.;
RL   Submitted (OCT-2016) 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; FOZP01000002; SFS40577.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1I6PK33; -.
DR   STRING; 593133.SAMN04488006_1121; -.
DR   OrthoDB; 9815002at2; -.
DR   Proteomes; UP000199312; 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; 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; PS00922; TRANSGLYCOSYLASE; 1.
PE   3: Inferred from homology;
KW   Reference proteome {ECO:0000313|Proteomes:UP000199312}.
FT   DOMAIN          394..437
FT                   /note="LysM"
FT                   /evidence="ECO:0000259|PROSITE:PS51782"
FT   DOMAIN          464..509
FT                   /note="LysM"
FT                   /evidence="ECO:0000259|PROSITE:PS51782"
SQ   SEQUENCE   512 AA;  59745 MW;  88D76857BEF8EDA8 CRC64;
     MKKIVILILI LVINIGYTQD KKDTKVLEKL KDTENLFSHE DSTFYKKLDS VKFQFHHEVS
     TIDSLWINEL INSPLNDTLR YSLEDDEFFI SELKELPTEL LKQRLEELDS KTPFNISYNP
     QLEQIIKSYL SKRKPVFSVI MERARFYFPM FEEHLDKYNI PLELKYLAIV ESALKPTAKS
     RVGATGLWQF MYQTGVLYNL NISSYVDERS DPIRATEAAC KYLSTLYKIY NDWDLALAAY
     NSGPGNVNKA IRRAGGSRNF WNIRNYLPRE TAGYVPAFYA TMYIFKYANE HNIKARENTI
     TRFETDTIQI KRQITFEQIN ETLNVDIEIL KFLNPQYKLD IIPYVKNKNY VLTLPTKHVG
     NFVSNEKLIY AYVDYQESKR EKALPQYLEV KDQITYKVRK GDYLGRIANK YNVSVSYLKR
     WNNLKSNNLR IGQRLKIYSN NVNVAATSKS TSTKAKEVPK GDYNTYIVKS GDSLWTIAQK
     YANVSVTNIK EWNNIWSAKS LKPGTKLKIF SK
//
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