ID A0A0W7U5L3_9GAMM Unreviewed; 509 AA.
AC A0A0W7U5L3;
DT 16-MAR-2016, integrated into UniProtKB/TrEMBL.
DT 16-MAR-2016, sequence version 1.
DT 27-MAR-2024, entry version 36.
DE SubName: Full=Lytic transglycosylase {ECO:0000313|EMBL:KUE81287.1};
GN ORFNames=ATO46_12370 {ECO:0000313|EMBL:KUE81287.1};
OS Aeromonas schubertii.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Aeromonadales;
OC Aeromonadaceae; Aeromonas.
OX NCBI_TaxID=652 {ECO:0000313|EMBL:KUE81287.1, ECO:0000313|Proteomes:UP000054876};
RN [1] {ECO:0000313|EMBL:KUE81287.1, ECO:0000313|Proteomes:UP000054876}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 43700 {ECO:0000313|EMBL:KUE81287.1,
RC ECO:0000313|Proteomes:UP000054876};
RA Liu L., Li Q., Zhang F., Shi B.;
RT "Complete genome sequence of Aeromonas schubertii strain ATCC43700.";
RL Submitted (DEC-2015) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the transglycosylase Slt family.
CC {ECO:0000256|ARBA:ARBA00007734}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:KUE81287.1}.
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DR EMBL; LPUO01000002; KUE81287.1; -; Genomic_DNA.
DR RefSeq; WP_050666134.1; NZ_LPUO01000002.1.
DR AlphaFoldDB; A0A0W7U5L3; -.
DR STRING; 652.WL1483_672; -.
DR OrthoDB; 9815002at2; -.
DR Proteomes; UP000054876; 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; 3.
DR CDD; cd16894; MltD-like; 1.
DR Gene3D; 1.10.530.10; -; 1.
DR Gene3D; 3.10.350.10; LysM domain; 3.
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; 3.
DR Pfam; PF01464; SLT; 1.
DR SMART; SM00257; LysM; 3.
DR SUPFAM; SSF54106; LysM domain; 3.
DR SUPFAM; SSF53955; Lysozyme-like; 1.
DR PROSITE; PS51782; LYSM; 3.
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 406..450
FT /note="LysM"
FT /evidence="ECO:0000259|PROSITE:PS51782"
FT DOMAIN 459..503
FT /note="LysM"
FT /evidence="ECO:0000259|PROSITE:PS51782"
SQ SEQUENCE 509 AA; 56681 MW; 984DE397CE3E5769 CRC64;
MKVRTALLAA LFLSGCQNLS NQDDRALTAI EPIKSPQVSK KTHKRYASGV WLNDDQLESV
AGSDDLWVRI SEDMQLEVPD NDRVRRQRTS ILRNERHMAT IASRAEPYLY LMVEEIERRG
LPMELVVIPM IESTFDPTAR SRSNAVGLWQ FVPQTGRNFG LAHDRWYDGR KDVVASTRAA
LDYLEYLNRF FDGDWLNTMA AYNAGEGRVR NAIVRNQKRG QSTDYWSLDL PRETEQYVPK
ILAMADVISN SERYGLSLPN LANEPKLRAI DVGGQIDIAT AANLVGMRQS QLKELNPALV
RGVTSPRGPH RIMVPVEYAD SLELALADLP RNERVKGRSY QVERGDTLSL IASRHGVSVS
ELKMTNNLRG NSLRAGQTLH LPAGAVDSGR TLASREPVSK RASAVTRYTV KAGDTLWEIS
RKHGVPQKSL MQWNGLSARA TLKPGAKLVI KGKSGNGSVS YQVRRGDSLS SIAAKFQVAV
VDVMRWNQLN KRSYLQPGQT LTLFVGDNG
//
