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Database: UniProt
Entry: A0A1T4RKR1_9GAMM
LinkDB: A0A1T4RKR1_9GAMM
Original site: A0A1T4RKR1_9GAMM 
ID   A0A1T4RKR1_9GAMM        Unreviewed;       666 AA.
AC   A0A1T4RKR1;
DT   10-MAY-2017, integrated into UniProtKB/TrEMBL.
DT   10-MAY-2017, sequence version 1.
DT   27-MAR-2024, entry version 22.
DE   SubName: Full=Soluble lytic murein transglycosylase {ECO:0000313|EMBL:SKA16487.1};
GN   ORFNames=SAMN02745674_02237 {ECO:0000313|EMBL:SKA16487.1};
OS   Lysobacter spongiicola DSM 21749.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Xanthomonadales;
OC   Xanthomonadaceae; Lysobacter.
OX   NCBI_TaxID=1122188 {ECO:0000313|EMBL:SKA16487.1, ECO:0000313|Proteomes:UP000190061};
RN   [1] {ECO:0000313|EMBL:SKA16487.1, ECO:0000313|Proteomes:UP000190061}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 21749 {ECO:0000313|EMBL:SKA16487.1,
RC   ECO:0000313|Proteomes:UP000190061};
RA   Peterson S.W.;
RL   Submitted (FEB-2017) 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; FUXP01000009; SKA16487.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1T4RKR1; -.
DR   STRING; 1122188.SAMN02745674_02237; -.
DR   OrthoDB; 92254at2; -.
DR   Proteomes; UP000190061; Unassembled WGS sequence.
DR   GO; GO:0042597; C:periplasmic space; IEA:InterPro.
DR   GO; GO:0004553; F:hydrolase activity, hydrolyzing O-glycosyl compounds; IEA:InterPro.
DR   CDD; cd13401; Slt70-like; 1.
DR   Gene3D; 1.10.530.10; -; 1.
DR   Gene3D; 1.25.20.10; Bacterial muramidases; 1.
DR   Gene3D; 1.10.1240.20; Lytic transglycosylase, superhelical linker domain; 1.
DR   InterPro; IPR023346; Lysozyme-like_dom_sf.
DR   InterPro; IPR037061; Lytic_TGlycoase_superhlx_L_sf.
DR   InterPro; IPR012289; Lytic_TGlycosylase_superhlx_L.
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   Pfam; PF14718; SLT_L; 1.
DR   SUPFAM; SSF48435; Bacterial muramidases; 1.
DR   SUPFAM; SSF53955; Lysozyme-like; 1.
PE   3: Inferred from homology;
KW   Reference proteome {ECO:0000313|Proteomes:UP000190061};
KW   Signal {ECO:0000256|ARBA:ARBA00022729}.
FT   DOMAIN          413..474
FT                   /note="Lytic transglycosylase superhelical linker"
FT                   /evidence="ECO:0000259|Pfam:PF14718"
FT   DOMAIN          493..603
FT                   /note="Transglycosylase SLT"
FT                   /evidence="ECO:0000259|Pfam:PF01464"
FT   REGION          1..38
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          647..666
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1..18
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   666 AA;  73943 MW;  A2EC82805E95984A CRC64;
     MTCASAACAQ STPGQPAAAQ TAPAAAVPRP ADNRFEPMVD PALPRIDEAI RQAELGRHDA
     SGHGDIAAHP LYRWVEYAAL KRDIDTLPPA RAQAFLQRYQ GDAVAAEFRQ AWLTATARRE
     DAAAFLAAWD DGIDDIRLRC GKLDAQRRLG RTGAEWTREA QDIWRGSGES RPDQCDPVFA
     ALADAGHLPP ALSWERIEKA AAEWQPGVMR VAARNLPPAE RALAEDYAAF IDSPHPRALE
     WPKTDRSRLV ASHGLAKLGK DDPDRAESLL PQYARALGFS EADRGRAMYR IALWSVASYL
     PDSERRLNLV PESSYDERLH EWRVREALSR SDWPAALAAI RKMGPDQRND SRYAYFEARL
     AELTGDAATA QAKYRAAALV PEFHGFLAAD RIDQPYALCP REPSADAALR ASVSANPALR
     RAMGLHQLGR AGWAVKEWHD AMDDFDDSRR HLAVEMAQAN GWYDRAVFSL GRGKPEELRF
     YSLRFPLSHD AVIRREAARN NIDPAWVAAE IRAESIFNPK ARSGANALGL MQVLPATGAS
     VARRIGEPWG GAASLYQPET NIVLGTAYLR QMMDEYGGKP YFAIAGYNAG PTPLQRWQSQ
     RPGMDADFWI ETISYKETRE YVARVFAFSV IYDWRLDGDA LRLSDRMEGR TQGPRKQFRC
     PASPAA
//
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