ID A0A1I6G335_9FLAO Unreviewed; 536 AA.
AC A0A1I6G335;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 24-JAN-2024, entry version 17.
DE SubName: Full=Membrane-bound lytic murein transglycosylase D {ECO:0000313|EMBL:SFR36530.1};
GN ORFNames=SAMN04490243_1148 {ECO:0000313|EMBL:SFR36530.1};
OS Robiginitalea myxolifaciens.
OC Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales;
OC Flavobacteriaceae; Robiginitalea.
OX NCBI_TaxID=400055 {ECO:0000313|EMBL:SFR36530.1, ECO:0000313|Proteomes:UP000199534};
RN [1] {ECO:0000313|EMBL:SFR36530.1, ECO:0000313|Proteomes:UP000199534}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 21019 {ECO:0000313|EMBL:SFR36530.1,
RC ECO:0000313|Proteomes:UP000199534};
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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; FOYQ01000001; SFR36530.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1I6G335; -.
DR STRING; 400055.SAMN04490243_1148; -.
DR OrthoDB; 9815002at2; -.
DR Proteomes; UP000199534; 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; 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; PS00922; TRANSGLYCOSYLASE; 1.
PE 3: Inferred from homology;
KW Reference proteome {ECO:0000313|Proteomes:UP000199534};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..18
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 19..536
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5011774034"
FT DOMAIN 411..454
FT /note="LysM"
FT /evidence="ECO:0000259|PROSITE:PS51782"
FT DOMAIN 486..530
FT /note="LysM"
FT /evidence="ECO:0000259|PROSITE:PS51782"
FT REGION 457..484
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 460..483
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 536 AA; 60018 MW; 7EFD9F35D4AD7F9F CRC64;
MKQIVAIWLL VGCSLVSAQE NEAQESQQSL TDSVVVEASK PELADDTRVA LEGQASLDSA
QSEASELKDL PLAATYDSLW LKELTEAASR YGDMYAVVQE AVSDSTLDAL EGWDTEVFKE
RLAEMDALTP FEVEYNPSLE RVVKSFLLQR RDLMERMLSA SQFYFPLFEE SLAKNDLPLE
LKYLAIVESA LNPRARSRVG ATGLWQFMYG TGRMYGLSVS SYVDERNDPL LATAAASAYL
SKLYEIFGDW DLALAAYNSG PGNVNKAIRR SGGQTNYWNI RRNLPRETAG YVPAFLATYY
IFHYAEEHGL RPTEAPRPYL ETDTIHIKQT LTFDQISKVT AISVPELRIL NPAYKLDIIP
KVKGKEYALR LPVYAIGRFV NNEAKIYEEA KEALAKREKP LPELVQAEDR IRYRVRSGDY
LGKIAERYGV GVSQIKRWNG LRSNNLRIGQ RLTIYPRKPV TTAKPSTSNS SKETTTTASS
SAGGAKIHVV RKGDSLWTIS QQYPGVSIEN LKEWNGLRGN TLMPGTRLKL CNCNSL
//
