ID   A0A158GGS9_9BURK        Unreviewed;       552 AA.
AC   A0A158GGS9;
DT   06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT   06-JUL-2016, sequence version 1.
DT   27-MAR-2024, entry version 23.
DE   SubName: Full=Lytic transglycosylase catalytic subunit {ECO:0000313|EMBL:SAL31325.1};
GN   ORFNames=AWB64_02810 {ECO:0000313|EMBL:SAL31325.1};
OS   Caballeronia sordidicola.
OC   Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC   Burkholderiaceae; Caballeronia.
OX   NCBI_TaxID=196367 {ECO:0000313|EMBL:SAL31325.1, ECO:0000313|Proteomes:UP000054893};
RN   [1] {ECO:0000313|EMBL:SAL31325.1, ECO:0000313|Proteomes:UP000054893}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=LMG 22029 {ECO:0000313|EMBL:SAL31325.1};
RA   Oliw E.H.;
RL   Submitted (JAN-2016) 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; FCOC02000007; SAL31325.1; -; Genomic_DNA.
DR   RefSeq; WP_060819767.1; NZ_FCOC02000007.1.
DR   AlphaFoldDB; A0A158GGS9; -.
DR   OrthoDB; 9815002at2; -.
DR   Proteomes; UP000054893; 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; 2.
DR   CDD; cd16894; MltD-like; 1.
DR   Gene3D; 1.10.530.10; -; 1.
DR   Gene3D; 3.10.350.10; LysM domain; 1.
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; 1.
DR   PROSITE; PS51257; PROKAR_LIPOPROTEIN; 1.
DR   PROSITE; PS00922; TRANSGLYCOSYLASE; 1.
PE   3: Inferred from homology;
KW   Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..17
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           18..552
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5007810369"
FT   DOMAIN          340..384
FT                   /note="LysM"
FT                   /evidence="ECO:0000259|PROSITE:PS51782"
FT   REGION          488..552
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   552 AA;  60127 MW;  AD1171EF250A75C1 CRC64;
     MRLIFSALLV LTLAACASQG PTATNSLSSL PSAQKQQAVA DTIRKTAAAR ETINVDKTSV
     DSLSGPDGDL WGRIRRGFQI PDLQSDLVDM QVSWYAQRPD YVERMTGRSQ KYLYHIVEEL
     EQRHMPTELA LLPFIESAYN PQALSVAKAA GMWQFVPGTG RDYNLKQNMF QDERRDVLAS
     TSAALDYLSR LHDMFGDWHL ALAAYNWGEG SVQRAIAKNE ALGLPTDYQS LRMPNETRNY
     VPKLQAVKNI IANPQMYGLT LPDIPNHPYF VTVTTARDID VTMAARLAGM TVEEFRSLNP
     SFAKPVILGA TNPQILLPFD NANAFQKNLK SYSGALSSWT TYTVSERATP AVIAQKIGVD
     PDTLMSVNRI PAGMRLKAGS TIVVPRGDDD DEDISADVAE SAMLAVEPDV PDTRKMLIRV
     RRAQSMSTFA DRYNVSVGQL KGWNRTHRDS VLPGQVMVLH VPVGRAVPAE PGPVRVETVS
     VTSRTKGGVT KIGTHAPQSK GVSSRNAKGS AAPAKVTRVA EKTSAPAKAK PIAVKPVAAA
     SKSTKTGKDK KK
//