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Database: UniProt
Entry: F0G1K3_9BURK
LinkDB: F0G1K3_9BURK
Original site: F0G1K3_9BURK 
ID   F0G1K3_9BURK            Unreviewed;       473 AA.
AC   F0G1K3;
DT   03-MAY-2011, integrated into UniProtKB/TrEMBL.
DT   03-MAY-2011, sequence version 1.
DT   27-MAR-2024, entry version 33.
DE   SubName: Full=Membrane-bound lytic murein transglycosylase D {ECO:0000313|EMBL:EGD04626.1};
DE   Flags: Fragment;
GN   ORFNames=B1M_10508 {ECO:0000313|EMBL:EGD04626.1};
OS   Burkholderia sp. TJI49.
OC   Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC   Burkholderiaceae; Burkholderia.
OX   NCBI_TaxID=987057 {ECO:0000313|EMBL:EGD04626.1, ECO:0000313|Proteomes:UP000003049};
RN   [1] {ECO:0000313|EMBL:EGD04626.1, ECO:0000313|Proteomes:UP000003049}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=TJI49 {ECO:0000313|EMBL:EGD04626.1,
RC   ECO:0000313|Proteomes:UP000003049};
RX   PubMed=23653265; DOI=10.1007/s11274-013-1366-5;
RA   Khan A., Asif H., Studholme D.J., Khan I.A., Azim M.K.;
RT   "Genome characterization of a novel Burkholderia cepacia complex genomovar
RT   isolated from dieback affected mango orchards.";
RL   World J. Microbiol. Biotechnol. 29:2033-2044(2013).
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:EGD04626.1}.
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DR   EMBL; AEXE01000542; EGD04626.1; -; Genomic_DNA.
DR   AlphaFoldDB; F0G1K3; -.
DR   Proteomes; UP000003049; 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; 1.
DR   SUPFAM; SSF53955; Lysozyme-like; 1.
DR   PROSITE; PS51782; LYSM; 2.
DR   PROSITE; PS00922; TRANSGLYCOSYLASE; 1.
PE   3: Inferred from homology;
FT   DOMAIN          325..369
FT                   /note="LysM"
FT                   /evidence="ECO:0000259|PROSITE:PS51782"
FT   DOMAIN          401..444
FT                   /note="LysM"
FT                   /evidence="ECO:0000259|PROSITE:PS51782"
FT   REGION          454..473
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   NON_TER         473
FT                   /evidence="ECO:0000313|EMBL:EGD04626.1"
SQ   SEQUENCE   473 AA;  52209 MW;  9FB9190501B9D6DD CRC64;
     MVLLLAACAS QGPVANNAAD SQATSTYLRK SATAKETVDV DKQSVGDLTS ADSDLWARIR
     RGFQMPDLQS DLVDMQTTWY TQRPDYVQRM TERSQKYLYH IVEELEARHM PTELALLPFI
     ESAYNPQALS VAKAAGMWQF MPGTGRTYNL KRNMWQDERR DVLASTSAAL DYLSRLHDMF
     GDWYLALAAY NWGEGNVQRA IARNQAAGLP TDYQNLRMPN ETRNYVPKLQ AVKNIIANPQ
     QYGLTLPDIP NHPYFVTVTT SRDIDVSVAA KLANLSLDEF KSLNPSFSKP VILGATDPQI
     LLPFDNAAAF EKNLKSYGGQ LSSWTTYTVS ERARPAAIAE KIGVDADTLM SVNKIPAGMR
     LKPGSTIVVP RGDDDDEDIS ADVAENGVLA MEPDVPDTRK MLIRVRRKQS MATIASRYGV
     SVGQLKAWNR THRDLAMPGQ ALVLHVPVGR AVPAEPGPER IATSVGGGHI ERA
//
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