ID A0A220W5I4_9SPHN Unreviewed; 663 AA.
AC A0A220W5I4;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 27-MAR-2024, entry version 16.
DE SubName: Full=Soluble lytic murein transglycosylase {ECO:0000313|EMBL:ASK88080.1};
DE EC=4.2.2.- {ECO:0000313|EMBL:ASK88080.1};
GN Name=slt {ECO:0000313|EMBL:ASK88080.1};
GN ORFNames=SPHFLASMR4Y_01315 {ECO:0000313|EMBL:ASK88080.1};
OS Sphingorhabdus sp. SMR4y.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Sphingomonadales;
OC Sphingomonadaceae; Sphingorhabdus.
OX NCBI_TaxID=2584094 {ECO:0000313|EMBL:ASK88080.1, ECO:0000313|Proteomes:UP000198359};
RN [1] {ECO:0000313|EMBL:ASK88080.1, ECO:0000313|Proteomes:UP000198359}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SMR4y {ECO:0000313|EMBL:ASK88080.1,
RC ECO:0000313|Proteomes:UP000198359};
RA Topel M., Pinder M.I.M., Johansson O.N., Kourtchenko O., Godhe A.,
RA Clarke A.K.;
RT "Genome Sequence of Sphingorhabdus flavimaris Strain SMR4y Isolated from a
RT culture of the Diatom Skeletonema marinoi.";
RL Submitted (JUL-2017) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the transglycosylase Slt family.
CC {ECO:0000256|ARBA:ARBA00007734}.
CC -!- SIMILARITY: Belongs to the virb1 family.
CC {ECO:0000256|ARBA:ARBA00009387}.
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; CP022336; ASK88080.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A220W5I4; -.
DR KEGG; sfla:SPHFLASMR4Y_01315; -.
DR OrthoDB; 9815002at2; -.
DR Proteomes; UP000198359; Chromosome.
DR GO; GO:0042597; C:periplasmic space; IEA:InterPro.
DR GO; GO:0004553; F:hydrolase activity, hydrolyzing O-glycosyl compounds; IEA:InterPro.
DR GO; GO:0016829; F:lyase activity; IEA:UniProtKB-KW.
DR CDD; cd13401; Slt70-like; 1.
DR Gene3D; 1.10.530.10; -; 1.
DR Gene3D; 1.25.20.10; Bacterial muramidases; 1.
DR InterPro; IPR023346; Lysozyme-like_dom_sf.
DR InterPro; IPR008939; Lytic_TGlycosylase_superhlx_U.
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; PF01464; SLT; 1.
DR SUPFAM; SSF48435; Bacterial muramidases; 1.
DR SUPFAM; SSF53955; Lysozyme-like; 1.
PE 3: Inferred from homology;
KW Lyase {ECO:0000313|EMBL:ASK88080.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000198359};
KW Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..22
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 23..663
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5012081284"
FT DOMAIN 503..603
FT /note="Transglycosylase SLT"
FT /evidence="ECO:0000259|Pfam:PF01464"
SQ SEQUENCE 663 AA; 73512 MW; 1C9D660AD77D7F5A CRC64;
MSSMVSRFVI AALLFSPATC MAADNIGEQM GWQKESAGLS DPTGGNAILG LQRWRVLTQS
DNYSFEDYAG FLVTFPGWPE DTRMQRNAEQ AININSFSPA RVLAFFNRFE PITNAGAAKF
AVALQATGQR ELADKWARTA WRGGTLTDED EAMLIARFSS VFSIEDHDAR MDALLWARAT
RDAARQLGFT SPQRRPVFAA RLAQLTESAD ANDQASAVGA IARDDAGYLA DRARYLRNRG
QSAAARQLLA TRPELRVKPA LPETWFEAML LNAKAAENDR QWSTAYNIAS KIEDAYAEPT
RIADQNSRVR DRYSDLAWIA GTAALNGLRQ PARAVRMFDL YAQSYDSPNI TSKGYYWAGR
AAAEAGQTEQ AQAYFEKAAA FPDYFYGQLS LERLGRPLPE FNRKPAIEIT EEDRRAYDSE
PLVIAAKASI RTGPWREQIR FHRALAYNAK TPKDYLLLSD LATRIGARDL GVIKGISALS
AGVGPIDETS FPTMQVPFGH EGSWTLIHAI TRQESQFAEG AISHAGARGL MQLMPGTARE
QSGKANLSYN LSSLTDDPQY NIRLGSGYIQ RMMDYYGGSY PLAVAAYNAG PGNVNKWLRA
NGDPRMGGID WIQWIEDIPI SETRNYVKRV LENAVVYDTK NPRGPTIRSD TPLTRYIGKN
YKG
//
