ID A0A370N726_9BURK Unreviewed; 564 AA.
AC A0A370N726;
DT 07-NOV-2018, integrated into UniProtKB/TrEMBL.
DT 07-NOV-2018, sequence version 1.
DT 24-JAN-2024, entry version 20.
DE SubName: Full=Lytic transglycosylase {ECO:0000313|EMBL:RDK01409.1};
GN ORFNames=DLM46_18390 {ECO:0000313|EMBL:RDK01409.1};
OS Paraburkholderia lacunae.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Burkholderiaceae; Paraburkholderia.
OX NCBI_TaxID=2211104 {ECO:0000313|EMBL:RDK01409.1, ECO:0000313|Proteomes:UP000254875};
RN [1] {ECO:0000313|Proteomes:UP000254875}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=S27 {ECO:0000313|Proteomes:UP000254875};
RA Feng T.;
RL Submitted (MAY-2018) 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:RDK01409.1}.
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DR EMBL; QHKS01000011; RDK01409.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A370N726; -.
DR OrthoDB; 9815002at2; -.
DR Proteomes; UP000254875; 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; 1.
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;
KW Reference proteome {ECO:0000313|Proteomes:UP000254875};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..22
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 23..564
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5016943119"
FT DOMAIN 339..383
FT /note="LysM"
FT /evidence="ECO:0000259|PROSITE:PS51782"
FT DOMAIN 415..458
FT /note="LysM"
FT /evidence="ECO:0000259|PROSITE:PS51782"
FT REGION 492..564
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 492..510
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 520..547
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 564 AA; 61545 MW; 979A5B379158D533 CRC64;
MRFIFSALLV LMLAACASQG PATNSPTTAT NSASQQAVAD ALRKTATAKE TIDVDQGSVA
QLTSADADLW GRIRRGFQMP DLQTDLVDMQ VNWYAQRPDY VQRMTERSQK YLYHIVEELE
ARHMPTELAL LPFIESAYSP QALSVAKAAG MWQFMPGTGR TYNLKQNMWQ DERRDVLAST
SAALDYLSRL HDMFGDWQLA LAAYNWGEGN VQRAIARNEA AGLPTDYLSL RMPNETRNYV
PKLQAVKNIV MNPQMYGLAL PSIPNHPYFV TVTTSHDIDV EMAAKLANLS LDEFRSLNPS
FRKPVILGAT QPQILLPFDN ASAFERNLKT YSGSLSSWTT YTVTERSAPA AIAQKIGVDA
DTLMEVNKIP AGMRLKPGST IVVPRASDDD EDISADVAES AVLAMEPDVP DTRKMLIRVR
RNQTMAAIAV RYGVSVGQLK AWNRTHRDQV SRGQVIVLHV PVGKAMPSEP GPERIATDVQ
GGGVEKIGTR VADTRNDSRY DRKKGRGRSA VVKVSEPVGK ASKSTASGAS KGKVTKVSAS
TSGKASKAAA DSRPKTAANA KKGQ
//
