ID   A0A1I4E761_9RHOB        Unreviewed;       650 AA.
AC   A0A1I4E761;
DT   22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT   22-NOV-2017, sequence version 1.
DT   27-MAR-2024, entry version 15.
DE   SubName: Full=Soluble lytic murein transglycosylase {ECO:0000313|EMBL:SFL01648.1};
GN   ORFNames=SAMN04488036_10479 {ECO:0000313|EMBL:SFL01648.1};
OS   Shimia haliotis.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC   Roseobacteraceae.
OX   NCBI_TaxID=1280847 {ECO:0000313|EMBL:SFL01648.1, ECO:0000313|Proteomes:UP000198851};
RN   [1] {ECO:0000313|EMBL:SFL01648.1, ECO:0000313|Proteomes:UP000198851}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 28453 {ECO:0000313|EMBL:SFL01648.1,
RC   ECO:0000313|Proteomes:UP000198851};
RA   de Groot N.N.;
RL   Submitted (OCT-2016) to the EMBL/GenBank/DDBJ databases.
CC   -!- SIMILARITY: Belongs to the transglycosylase Slt family.
CC       {ECO:0000256|ARBA:ARBA00007734}.
CC   -!- SIMILARITY: Belongs to the virb1 family.
CC       {ECO:0000256|ARBA:ARBA00009387}.
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DR   EMBL; FOSZ01000004; SFL01648.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1I4E761; -.
DR   STRING; 1280847.SAMN04488036_10479; -.
DR   OrthoDB; 9815002at2; -.
DR   Proteomes; UP000198851; Unassembled WGS sequence.
DR   GO; GO:0016020; C:membrane; IEA:InterPro.
DR   GO; GO:0042597; C:periplasmic space; IEA:InterPro.
DR   GO; GO:0004553; F:hydrolase activity, hydrolyzing O-glycosyl compounds; IEA:InterPro.
DR   GO; GO:0008933; F:lytic transglycosylase activity; IEA:InterPro.
DR   GO; GO:0000270; P:peptidoglycan metabolic process; IEA:InterPro.
DR   CDD; cd13401; Slt70-like; 1.
DR   Gene3D; 1.10.530.10; -; 1.
DR   Gene3D; 1.25.20.10; Bacterial muramidases; 1.
DR   InterPro; IPR023346; Lysozyme-like_dom_sf.
DR   InterPro; IPR008939; Lytic_TGlycosylase_superhlx_U.
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; PF01464; SLT; 1.
DR   SUPFAM; SSF48435; Bacterial muramidases; 1.
DR   SUPFAM; SSF53955; Lysozyme-like; 1.
DR   PROSITE; PS00922; TRANSGLYCOSYLASE; 1.
PE   3: Inferred from homology;
KW   Signal {ECO:0000256|ARBA:ARBA00022729}.
FT   DOMAIN          489..588
FT                   /note="Transglycosylase SLT"
FT                   /evidence="ECO:0000259|Pfam:PF01464"
SQ   SEQUENCE   650 AA;  71165 MW;  D99EF12CFBF7A353 CRC64;
     MLRSFPALCL AVGVTLSGVG GARADLGAAM DAVRARDWAA ATAEVRGESQ IAKDIVEWHR
     LRAGQGQPDE VLAFLNRRGD WPGLPYLRKQ SEEAFFGVSH EMAMSFYVHG SPQTAQGALT
     QAEVLAHAGE EGTAQAGIVL AWRTMPMDSQ TQGVYLDRYG KLLADHHTAR LDSMLWKGWK
     ENARRMYRFV PESWVALAQA RIALRDRAAG VDGLIEAVPA ALQDNPGLAY ERFVWRHRKG
     LDDRAIELLL ARSKAGTLGE PEQWAQRRRS LIRSQMRAGN YQTAYDLASV HGMAPDAGYG
     FSDCEWLAGY MALRFLNQPD IAAAHFVRFA QSVETPISLG RAGYWLGRAY EAMGDTATAK
     QAFVAGAAHQ TSFYGLLAAE KGGVAPDQAL RGDEAFPDWR EAAWTTSSVH QAAKMLLDAG
     ELSLAERFWI HLSERLDRPG LGQMGEMAQD LGQPHIAVML GKAIVKRGIT LPGPYYPLHP
     LVSQDLPVAD ELSLAIARRE SEFDPVVVSH AGARGLMQLM PGTARDVSRE IGEAYVLGNL
     TADPKYNARL GSAYLAGLAE QFDGNIIMIS AGYNAGPHRP TRWMVKNGDP RGGSVEAMVD
     WIEMIPFNET RNYVMRVSES LPVYRARLGK SALPVPFGQE ITGGTIRVIR
//