ID A0A396MDH1_9BACT Unreviewed; 430 AA.
AC A0A396MDH1;
DT 05-DEC-2018, integrated into UniProtKB/TrEMBL.
DT 05-DEC-2018, sequence version 1.
DT 27-MAR-2024, entry version 15.
DE SubName: Full=LysM peptidoglycan-binding domain-containing protein {ECO:0000313|EMBL:RHR64443.1};
GN ORFNames=DWW79_04900 {ECO:0000313|EMBL:RHR64443.1};
OS Alistipes sp. AF17-16.
OC Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Rikenellaceae;
OC Alistipes.
OX NCBI_TaxID=2292190 {ECO:0000313|EMBL:RHR64443.1, ECO:0000313|Proteomes:UP000265869};
RN [1] {ECO:0000313|EMBL:RHR64443.1, ECO:0000313|Proteomes:UP000265869}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AF17-16 {ECO:0000313|EMBL:RHR64443.1,
RC ECO:0000313|Proteomes:UP000265869};
RA Zou Y., Xue W., Luo G.;
RT "A genome reference for cultivated species of the human gut microbiota.";
RL Submitted (AUG-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:RHR64443.1}.
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DR EMBL; QUGX01000002; RHR64443.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A396MDH1; -.
DR Proteomes; UP000265869; 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; PTHR37423:SF2; SOLUBLE LYTIC MUREIN TRANSGLYCOSYLASE; 1.
DR PANTHER; PTHR37423; SOLUBLE LYTIC MUREIN TRANSGLYCOSYLASE-RELATED; 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:UP000265869};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..18
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 19..430
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5017265684"
FT DOMAIN 385..428
FT /note="LysM"
FT /evidence="ECO:0000259|PROSITE:PS51782"
FT REGION 363..385
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 363..377
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 430 AA; 48087 MW; 219885520564C347 CRC64;
MPKSLTALLI LTLLPLFAKT QADPREQLNI VGSPTVYDSV VASWRTDNIN ETFGDYLRDY
IELDTTRYLP AVSTVTDNVC RTRLKNMVSP IYLPYNDIVK KHIVAYATTH KSVTRRMLSY
GKYYFPMIEH ELAKNGLPLE LKFVAVIESA LNPTATSPSG AVGLWQFMLQ TGRQYGLEIS
SMVDARRDPV QATAAACRYM KDLYDIYHDW TLVMASYNYG PGNVNKALQR AGANASTYWD
IYPFLPKATR DYVPAFVALA YLYYYHSDYG VVPFASPLPL ATDTVMVSRR IDLNRVSEKL
NLPSELVKLL NPQYKQDVIP ATVKSYPLVL PQQEVCRFIE CEQARLAQAD TLPADTVSDG
RLTASAASSQ QGGSNGDGYS GPDPLTYKVK KGDTLGAIAH KYKVTVSQLM KWNQLKNSNL
KIGQTLKIIR
//
