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Database: UniProt
Entry: A0A1D7QE64_9SPHI
LinkDB: A0A1D7QE64_9SPHI
Original site: A0A1D7QE64_9SPHI 
ID   A0A1D7QE64_9SPHI        Unreviewed;       405 AA.
AC   A0A1D7QE64;
DT   18-JAN-2017, integrated into UniProtKB/TrEMBL.
DT   18-JAN-2017, sequence version 1.
DT   27-MAR-2024, entry version 20.
DE   SubName: Full=Lytic transglycosylase {ECO:0000313|EMBL:AOM76957.1};
GN   ORFNames=BFS30_07100 {ECO:0000313|EMBL:AOM76957.1};
OS   Pedobacter steynii.
OC   Bacteria; Bacteroidota; Sphingobacteriia; Sphingobacteriales;
OC   Sphingobacteriaceae; Pedobacter.
OX   NCBI_TaxID=430522 {ECO:0000313|EMBL:AOM76957.1, ECO:0000313|Proteomes:UP000094313};
RN   [1] {ECO:0000313|EMBL:AOM76957.1, ECO:0000313|Proteomes:UP000094313}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DX4 {ECO:0000313|EMBL:AOM76957.1,
RC   ECO:0000313|Proteomes:UP000094313};
RA   Seilhamer J.J.;
RL   Submitted (AUG-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; CP017141; AOM76957.1; -; Genomic_DNA.
DR   RefSeq; WP_069378650.1; NZ_CP017141.1.
DR   AlphaFoldDB; A0A1D7QE64; -.
DR   KEGG; psty:BFS30_07100; -.
DR   OrthoDB; 9815002at2; -.
DR   Proteomes; UP000094313; Chromosome.
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; 1.
DR   CDD; cd16894; MltD-like; 1.
DR   Gene3D; 1.10.530.10; -; 1.
DR   Gene3D; 3.10.350.10; LysM domain; 1.
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; PTHR37423:SF2; SOLUBLE LYTIC MUREIN TRANSGLYCOSYLASE; 1.
DR   PANTHER; PTHR37423; SOLUBLE LYTIC MUREIN TRANSGLYCOSYLASE-RELATED; 1.
DR   Pfam; PF01476; LysM; 1.
DR   Pfam; PF01464; SLT; 1.
DR   SMART; SM00257; LysM; 1.
DR   SUPFAM; SSF54106; LysM domain; 1.
DR   SUPFAM; SSF53955; Lysozyme-like; 1.
DR   PROSITE; PS51782; LYSM; 1.
DR   PROSITE; PS00922; TRANSGLYCOSYLASE; 1.
PE   3: Inferred from homology;
KW   Reference proteome {ECO:0000313|Proteomes:UP000094313};
KW   Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..21
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           22..405
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5009098507"
FT   DOMAIN          347..390
FT                   /note="LysM"
FT                   /evidence="ECO:0000259|PROSITE:PS51782"
SQ   SEQUENCE   405 AA;  45905 MW;  C1EFEAC7870AD9FE CRC64;
     MKINVLFASC ILALTSFSAI AQQPKDLIIN DTVPVPVLPE TPSFYNHNYG YKSRLDSIQK
     MVPLSYNEHV QKYIDIYSGR KDMMGKMIGL SEYYFPVFEK ALKYYNIPEE IKYLPVIESS
     MNAHAVSRVG ATGLWQFMFA TAKDYGLNMD NFVDERKDPI QASYAAAAYF RDAYEELGDW
     LLAIAAYNCG MGNVKRAMVK ADSQDFWEIR RYLPTETRNY VPAFIAAIYV MNYPGQHQIK
     AQKSPFVKST DTIHVNRFVS LPKLAEALSM DEGALCSLNP SYKKKIVNGT EIEPKRIIIP
     KVNMAQFAQI YDVLNNTELD VNPNVVLASN DDRRRKKIVE RPLVAVSYHK VSPGQTLSAI
     ADKYHVEVQD LKVWNGLKSS SIVPGQKLKI HNPQSSKKRK MAIKG
//
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