ID A0A0K6H1K2_9GAMM Unreviewed; 539 AA.
AC A0A0K6H1K2;
DT 11-NOV-2015, integrated into UniProtKB/TrEMBL.
DT 11-NOV-2015, sequence version 1.
DT 24-JAN-2024, entry version 29.
DE SubName: Full=Transglycosylase SLT domain/LysM domain {ECO:0000313|EMBL:CUA84701.1};
GN ORFNames=Ga0061064_0980 {ECO:0000313|EMBL:CUA84701.1};
OS Pseudidiomarina woesei.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Alteromonadales;
OC Idiomarinaceae; Pseudidiomarina.
OX NCBI_TaxID=1381080 {ECO:0000313|EMBL:CUA84701.1, ECO:0000313|Proteomes:UP000182598};
RN [1] {ECO:0000313|Proteomes:UP000182598}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 27808 {ECO:0000313|Proteomes:UP000182598};
RA Varghese N.;
RL Submitted (AUG-2015) 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; CYHB01000002; CUA84701.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0K6H1K2; -.
DR Proteomes; UP000182598; 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; 3.
DR CDD; cd16894; MltD-like; 1.
DR Gene3D; 1.10.530.10; -; 1.
DR Gene3D; 3.10.350.10; LysM domain; 3.
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; 3.
DR Pfam; PF01464; SLT; 1.
DR SMART; SM00257; LysM; 3.
DR SUPFAM; SSF54106; LysM domain; 3.
DR SUPFAM; SSF53955; Lysozyme-like; 1.
DR PROSITE; PS51782; LYSM; 3.
DR PROSITE; PS51257; PROKAR_LIPOPROTEIN; 1.
DR PROSITE; PS00922; TRANSGLYCOSYLASE; 1.
PE 3: Inferred from homology;
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..19
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 20..539
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5005503538"
FT DOMAIN 351..394
FT /note="LysM"
FT /evidence="ECO:0000259|PROSITE:PS51782"
FT DOMAIN 425..469
FT /note="LysM"
FT /evidence="ECO:0000259|PROSITE:PS51782"
FT DOMAIN 484..528
FT /note="LysM"
FT /evidence="ECO:0000259|PROSITE:PS51782"
SQ SEQUENCE 539 AA; 61193 MW; FE8E16BEA67D7922 CRC64;
MMYMKKWIAL AISSTLATGC SLTPWQSDSA ANETIQTVPA EPVAEPVETN TLLEAEAIAE
HSEVEPAVIE LTPQQEADLW QRIRRQLTME APELPRLVSQ RNWYLNNPYY MERVAKRAQP
FMYMIVDEIE RRGMPLELAL LPIVESAFDP FAYSHGRAAG VWQFIPGTAR HYGLEINWWY
DGRRDVYAAT HAALDYLDAL QKRFDGDWLH ALAAYNSGEG RVAGSIRRNK RAGKPTDFWS
LDLPRETRAY VPKLLALADI LKNYDDYAKH WLPIDNKPYL AVVEAHSQID LAKAAEIAEL
DLDTLHHYNS AYNRWATDPV GPHRLLLPIE NASKLQTWLA TADSKELVQW TRHQVKSGES
LLVIAKQYHT TAKAIQQANN ISGHIIRAGD HLLVPVATRD LDEYSLSAEQ RLVSKQSQSR
GAYKVEHEVV SGDTLWDISR EYNVNLRSLA SWNGMAPTDP LRPGKKLVVW LPHSEKPAGV
VRSLNYKVRS GDSLARIASR FNVSITDIEK WNQINRNNYL QPGQQLKLYV DVTRLNTQS
//