ID S6GD20_9GAMM Unreviewed; 443 AA.
AC S6GD20;
DT 16-OCT-2013, integrated into UniProtKB/TrEMBL.
DT 16-OCT-2013, sequence version 1.
DT 27-MAR-2024, entry version 29.
DE RecName: Full=LysM domain-containing protein {ECO:0000259|PROSITE:PS51782};
GN ORFNames=OFPII_35470 {ECO:0000313|EMBL:EPJ44360.1};
OS Osedax symbiont Rs1.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Oceanospirillales;
OC Oceanospirillaceae.
OX NCBI_TaxID=1330036 {ECO:0000313|EMBL:EPJ44360.1, ECO:0000313|Proteomes:UP000014822};
RN [1] {ECO:0000313|EMBL:EPJ44360.1, ECO:0000313|Proteomes:UP000014822}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Rs1 {ECO:0000313|Proteomes:UP000014822};
RA Yi H., Goffredi S.;
RT "Comparative genomics of two novel heterotrophic symbionts of deep-sea
RT Osedax worms: functional variation and environmental selection.";
RL Submitted (MAY-2013) 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:EPJ44360.1}.
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DR EMBL; ASZJ01000165; EPJ44360.1; -; Genomic_DNA.
DR AlphaFoldDB; S6GD20; -.
DR PATRIC; fig|1330036.3.peg.3395; -.
DR Proteomes; UP000014822; 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; PS51257; PROKAR_LIPOPROTEIN; 1.
DR PROSITE; PS00922; TRANSGLYCOSYLASE; 1.
PE 3: Inferred from homology;
KW Reference proteome {ECO:0000313|Proteomes:UP000014822};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..23
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 24..443
FT /note="LysM domain-containing protein"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5004538534"
FT DOMAIN 330..373
FT /note="LysM"
FT /evidence="ECO:0000259|PROSITE:PS51782"
FT DOMAIN 396..440
FT /note="LysM"
FT /evidence="ECO:0000259|PROSITE:PS51782"
SQ SEQUENCE 443 AA; 49507 MW; 6DF6F3400DD0FAEB CRC64;
MQLAKILIIF FSSLLIISCQ SIAVNTSYVS NYNGYDKNGV PIKLAKGAVN AISTTDLWHK
TRSNFKLADD FQHARVVEEI KFFNRFPRHM KKVSEQANPF YYYVLQEVMK RGLPSEVALL
PVIESLYNPN AYSSGKASGI WQFIPSTAKY LGIEMNEWYD GRRDLITSTQ TALDYLERYN
KRFNGDWLLT FAAYNSGGGT VSKAIRKNKE KGLPTDYWSL KLPAETAKYV PRILAIAAIV
NTPQAYNMSL PSIPDTPYFS IVDLGGQIDL NKVAKMAKLK KAHLLWLNSG FSHSVTPPRG
PHRVLVPVKS AAGLELALAS INKPERMNWA RYIVKAGDNL GSIANKYSTS VSIIKQVNSL
TSSKLRINKK LFIPTALALK GNRSKAKTKN RSSRHKIHKI NNGDTVWDIA KKHKITVRQI
LAYNGLSKNS TLRVGAALKI PQG
//
