ID A0A418X279_9BURK Unreviewed; 498 AA.
AC A0A418X279;
DT 08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT 08-MAY-2019, sequence version 1.
DT 27-MAR-2024, entry version 13.
DE SubName: Full=LysM peptidoglycan-binding domain-containing protein {ECO:0000313|EMBL:RJG06531.1};
GN ORFNames=D3870_11370 {ECO:0000313|EMBL:RJG06531.1};
OS Noviherbaspirillum cavernae.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Oxalobacteraceae; Noviherbaspirillum.
OX NCBI_TaxID=2320862 {ECO:0000313|EMBL:RJG06531.1, ECO:0000313|Proteomes:UP000285190};
RN [1] {ECO:0000313|EMBL:RJG06531.1, ECO:0000313|Proteomes:UP000285190}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K2R10-39 {ECO:0000313|EMBL:RJG06531.1,
RC ECO:0000313|Proteomes:UP000285190};
RA Zhu H.;
RL Submitted (SEP-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:RJG06531.1}.
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DR EMBL; QYUN01000002; RJG06531.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A418X279; -.
DR OrthoDB; 9815002at2; -.
DR Proteomes; UP000285190; 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; 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:UP000285190};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..24
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 25..498
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5019280806"
FT DOMAIN 411..454
FT /note="LysM"
FT /evidence="ECO:0000259|PROSITE:PS51782"
FT REGION 454..498
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 498 AA; 55479 MW; A9E96D67A78D68C7 CRC64;
MPLPKTRIIP FAALLLCTSL TSHAADLSLP LYNWSQISAM EGPYDPNDPL AQVLGMEEID
VWGRIRKGFG IPDLDNPLVA NQTQWYSSRP DYIQRTTTRA SRYLFHVVQE LEKRNMPTEL
ALLPFIESAF NPQAYSSAHA AGMWQFIPST GRDYNLKQNM FKDERRDVLA STDAALTYLQ
KLYGMFGDWQ LALAAYNWGE GSVQRAINKN RAAGLPTDFN GLSPNMPLET RNYVPKLQAV
KNIIAAPAQY SIVLPKVDNQ PYFVTIGKTR DIDLKVAAQL AELSIDEFKA LNPQYNRPVI
VGSADTRILL PQSNAEKFKT NLSKWGRALS SWSAHTVTNA RERIETIASK FGTTPEVIRE
VNNIPPRMRL KAGSTVLVPK TEAAIEKDIS SDLAENAIMA IEPDVPDTRR ITVKVGKRDS
LASIAQRHKV SVAQIKSWND LRQDKVANGQ SLHIQVPYKP AARPASKQAT RTPVRKVAAP
RNATQRKAAP TTGKPRRS
//
