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Database: UniProt
Entry: A0A1G6RY92_9GAMM
LinkDB: A0A1G6RY92_9GAMM
Original site: A0A1G6RY92_9GAMM 
ID   A0A1G6RY92_9GAMM        Unreviewed;       409 AA.
AC   A0A1G6RY92;
DT   22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT   22-NOV-2017, sequence version 1.
DT   27-MAR-2024, entry version 19.
DE   SubName: Full=Membrane-bound lytic murein transglycosylase D {ECO:0000313|EMBL:SDD08917.1};
GN   ORFNames=SAMN04488509_101145 {ECO:0000313|EMBL:SDD08917.1};
OS   Aquimonas voraii.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Xanthomonadales;
OC   Rhodanobacteraceae; Aquimonas.
OX   NCBI_TaxID=265719 {ECO:0000313|EMBL:SDD08917.1, ECO:0000313|Proteomes:UP000199603};
RN   [1] {ECO:0000313|EMBL:SDD08917.1, ECO:0000313|Proteomes:UP000199603}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 16957 {ECO:0000313|EMBL:SDD08917.1,
RC   ECO:0000313|Proteomes:UP000199603};
RA   de Groot N.N.;
RL   Submitted (OCT-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; FNAG01000001; SDD08917.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1G6RY92; -.
DR   STRING; 265719.SAMN04488509_101145; -.
DR   OrthoDB; 9815002at2; -.
DR   Proteomes; UP000199603; 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; 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; 1.
DR   Pfam; PF01464; SLT; 1.
DR   SMART; SM00257; LysM; 1.
DR   SUPFAM; SSF54106; LysM domain; 1.
DR   SUPFAM; SSF53955; Lysozyme-like; 1.
DR   PROSITE; PS51782; LYSM; 1.
DR   PROSITE; PS00922; TRANSGLYCOSYLASE; 1.
PE   3: Inferred from homology;
KW   Reference proteome {ECO:0000313|Proteomes:UP000199603}.
FT   DOMAIN          353..397
FT                   /note="LysM"
FT                   /evidence="ECO:0000259|PROSITE:PS51782"
FT   REGION          44..81
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        44..80
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   409 AA;  44211 MW;  0F475F202A21D192 CRC64;
     MRHPATLPEL GRAVSAARAL PFGIRPLALL LMLALTGCQA PIRPEPPAPA EPPAAPMPAL
     EAMPAPPPEP PPPTPPPPDV FERLRAQLGS DHCAEDGRQA QWVRLYAPRP ERFGARIAPM
     LPLLDYVLDQ VEAAGLPGEF ALIPIIESSY RPQARSPAGP AGMWQFTANT ARHFGLSVNG
     ERDERLSVVD ATEAALQHLG QLQAEHGDWV LAAAGYNAGA FRVRKLLERL DAPPPPGQLP
     QGLARGTYEY VEKLKAWACM LSEPERFGIA LPDADSFEPL TRVTTPPRMQ RLDLLSEASG
     LNAEALRSLN PLLRLAAPAR GDKDLLLPEN AAAELIAFMD RVKRGEIPLP EPRLHTVVSG
     DTLSVIARRH GLSVTELQRW NGLGAKSVLR IGQVLRLEPA TAGTSARSR
//
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