ID A0A0D5YSU3_9FLAO Unreviewed; 540 AA.
AC A0A0D5YSU3;
DT 27-MAY-2015, integrated into UniProtKB/TrEMBL.
DT 27-MAY-2015, sequence version 1.
DT 27-MAR-2024, entry version 26.
DE SubName: Full=Lytic transglycosylase catalytic {ECO:0000313|EMBL:AKA34974.1};
GN ORFNames=VC82_1346 {ECO:0000313|EMBL:AKA34974.1};
OS Allomuricauda lutaonensis.
OC Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales;
OC Flavobacteriaceae; Allomuricauda.
OX NCBI_TaxID=516051 {ECO:0000313|EMBL:AKA34974.1, ECO:0000313|Proteomes:UP000032726};
RN [1] {ECO:0000313|EMBL:AKA34974.1, ECO:0000313|Proteomes:UP000032726}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CC-HSB-11 {ECO:0000313|EMBL:AKA34974.1,
RC ECO:0000313|Proteomes:UP000032726};
RA Kim K.M.;
RT "Complete genome sequence of Muricauda lutaonensis CC-HSB-11T, isolated
RT from a coastal hot spring.";
RL Submitted (MAR-2015) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the transglycosylase Slt family.
CC {ECO:0000256|ARBA:ARBA00007734}.
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DR EMBL; CP011071; AKA34974.1; -; Genomic_DNA.
DR RefSeq; WP_045801683.1; NZ_CP011071.1.
DR AlphaFoldDB; A0A0D5YSU3; -.
DR STRING; 516051.VC82_1346; -.
DR KEGG; mlt:VC82_1346; -.
DR PATRIC; fig|516051.4.peg.1392; -.
DR HOGENOM; CLU_009520_1_0_10; -.
DR Proteomes; UP000032726; Chromosome.
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:UP000032726}.
FT DOMAIN 417..460
FT /note="LysM"
FT /evidence="ECO:0000259|PROSITE:PS51782"
FT DOMAIN 491..535
FT /note="LysM"
FT /evidence="ECO:0000259|PROSITE:PS51782"
FT REGION 26..46
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 540 AA; 61177 MW; 005D36B5A6A198DC CRC64;
MNQLTNIFLF VFCLAVANFY GQEQERSPVE ASEEKMSVTD TGPSTEKVPA LDVRKLDGQL
VEIKETKAGT IELADLEEAY RYDSLWLHEL HKNAALFTEM YDEVVNLPTE DTEKSALDLP
TDTLKARLQR LNEKTPFNIA YNPSLESVIK SFLTRKRGLM ERMLTASQFY FPLFEQELDN
HGVPLEIKYL SIVESALNPR AKSRVGATGL WQFMYGTGKM YGLDVSSYVD ERSDPIASTT
AACKYLAKLY DIFEDWDLAL AAYNSGPGNV NKAIRRSGGY RNYWNIRPFL PRETAGYVPA
FLATMYIFEY AEEHGLKRVN VERPYFETDT VHVKNLITFE QISKVVDIDM EELEMLNPAY
KLKIIPKIEG KTYALRLPKS KIGKFVNNEA AIYAYAKKQL DSLEKPLPQL VQANSKIRYR
VRSGDYLGKI AQRYGVGISQ IKRWNGLRSN NLRVGQRLTI YPRKPVVAQS PKVQKRTSKT
GASAAVASNA KVHTVQEGDS LWTISRKYPG VSIENLREWN GISGNNLKPG TKLKLCDCSS
//
