ID A0A1Q2GYC7_9GAMM Unreviewed; 486 AA.
AC A0A1Q2GYC7;
DT 12-APR-2017, integrated into UniProtKB/TrEMBL.
DT 12-APR-2017, sequence version 1.
DT 27-MAR-2024, entry version 24.
DE SubName: Full=Lytic transglycosylase {ECO:0000313|EMBL:AQQ00095.1};
GN ORFNames=B0W48_10015 {ECO:0000313|EMBL:AQQ00095.1};
OS Pseudoalteromonas aliena.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Alteromonadales;
OC Pseudoalteromonadaceae; Pseudoalteromonas.
OX NCBI_TaxID=247523 {ECO:0000313|EMBL:AQQ00095.1, ECO:0000313|Proteomes:UP000188243};
RN [1] {ECO:0000313|EMBL:AQQ00095.1, ECO:0000313|Proteomes:UP000188243}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=EH1 {ECO:0000313|EMBL:AQQ00095.1,
RC ECO:0000313|Proteomes:UP000188243};
RA Kim E., Heo E., Kim H., Kim D.;
RT "Complete genome sequence of the cold-active Pseudoalteromonas aliena
RT strain EH1 isolated from Arctic seawater.";
RL Submitted (FEB-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; CP019628; AQQ00095.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1Q2GYC7; -.
DR STRING; 247523.B0W48_10015; -.
DR KEGG; paln:B0W48_10015; -.
DR Proteomes; UP000188243; 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; 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; PS51257; PROKAR_LIPOPROTEIN; 1.
DR PROSITE; PS00922; TRANSGLYCOSYLASE; 1.
PE 3: Inferred from homology;
FT DOMAIN 338..381
FT /note="LysM"
FT /evidence="ECO:0000259|PROSITE:PS51782"
FT DOMAIN 413..457
FT /note="LysM"
FT /evidence="ECO:0000259|PROSITE:PS51782"
SQ SEQUENCE 486 AA; 55379 MW; 3A5C1352D8A47F1D CRC64;
MRSLVLFCLS LFLFGCGSTE PELQDAPKIL THHEADYQSE NELQKKQISS KLAPSPLKQT
DIKKRQTQVT DLWVHVANNL HFKIHKNVAL NKRINWYLKQ PNYLRTVNKR AAPYFYHIVK
KVEKKGLPME LALLPFVESG FRPTIVSSQQ AVGIWQLVAA TAHHFGVKSD QWYDGRQDVL
ASTDAALDYL SYLHKRFDGN WLHALAAYNT GEGRVKRAIE KNKKRGKSTD YWSLSLPKET
ADYVPKLLAL SYLVKHPQKP LKRPKLAYKP LTTQMDVGQQ FDFSVIAKLS GVGSKKLHAL
NQGYLKNQSS PNGPHTLLLP IRQEALLKSQ FFRANFAGEY IVIKNDTLYS IARRFDMSVI
ALKQLNNKQT NLISVGEKLL VGQPKTLQKS LTVDYKISPY LEHKELVIPT IEINYEVKQG
DNLWEISQLY HVAHSDLAKW NKLSASSVLK PGTQLVMFIP QAKKPKAIPI KKNLLLDLQK
TLNQPR
//
