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Database: UniProt
Entry: A0A1D8UWW6_9PROT
LinkDB: A0A1D8UWW6_9PROT
Original site: A0A1D8UWW6_9PROT 
ID   A0A1D8UWW6_9PROT        Unreviewed;       576 AA.
AC   A0A1D8UWW6;
DT   15-FEB-2017, integrated into UniProtKB/TrEMBL.
DT   15-FEB-2017, sequence version 1.
DT   27-MAR-2024, entry version 20.
DE   RecName: Full=Transglycosylase SLT domain-containing protein {ECO:0000259|Pfam:PF01464};
GN   ORFNames=A0U89_06700 {ECO:0000313|EMBL:AOX18175.1};
OS   Kozakia baliensis.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodospirillales;
OC   Acetobacteraceae; Kozakia.
OX   NCBI_TaxID=153496 {ECO:0000313|EMBL:AOX18175.1, ECO:0000313|Proteomes:UP000179145};
RN   [1] {ECO:0000313|EMBL:AOX18175.1, ECO:0000313|Proteomes:UP000179145}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 14400 {ECO:0000313|EMBL:AOX18175.1,
RC   ECO:0000313|Proteomes:UP000179145};
RX   PubMed=27716345;
RA   Brandt J.U., Jakob F., Behr J., Geissler A.J., Vogel R.F.;
RT   "Dissection of exopolysaccharide biosynthesis in Kozakia baliensis.";
RL   Microb. Cell Fact. 15:170-170(2016).
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}.
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DR   EMBL; CP014674; AOX18175.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1D8UWW6; -.
DR   STRING; 153496.A0U89_06700; -.
DR   KEGG; kba:A0U89_06700; -.
DR   eggNOG; COG0741; Bacteria.
DR   Proteomes; UP000179145; Chromosome.
DR   GO; GO:0016020; C:membrane; IEA:InterPro.
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:0008933; F:lytic transglycosylase activity; IEA:InterPro.
DR   GO; GO:0000270; P:peptidoglycan metabolic process; 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   InterPro; IPR023346; Lysozyme-like_dom_sf.
DR   InterPro; IPR008939; Lytic_TGlycosylase_superhlx_U.
DR   InterPro; IPR000189; Transglyc_AS.
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.
DR   PROSITE; PS00922; TRANSGLYCOSYLASE; 1.
PE   3: Inferred from homology;
KW   Reference proteome {ECO:0000313|Proteomes:UP000179145};
KW   Signal {ECO:0000256|ARBA:ARBA00022729}.
FT   DOMAIN          424..530
FT                   /note="Transglycosylase SLT"
FT                   /evidence="ECO:0000259|Pfam:PF01464"
SQ   SEQUENCE   576 AA;  62782 MW;  69B37AA2D40D3A91 CRC64;
     MPARDYAVFL QEQPAWPGRA VMLARFQHAL VTRTDDGELS SLCPLFPLTQ AQALLKCADR
     IADAPVQARR LWMNGGISLS DETPFLARFG QAFSSADHWT RFEHLEATHQ YTAASHQISR
     LALSKQALAR AFLAYRTTSP EADALFTGLS PTDQRDPALT FARLHHLRRA DQLGDALALW
     NAAGLAAQQS APSSAWSVER AGLARALLSA GSPQDAIILA DDRTLPLTNA NRLEAQFLSG
     WIALRRLHDA QRAEAYFLPL TTQPSLITRS RGYYWIGRAQ EAAGQKEAAQ ASYRQAAAMP
     TTFYGQMALS ALNGDVATLP PQGAPVPHLA EALNALPIVA TGTLARPDLA QAAQELVGMQ
     DQDHAREFLM MLYVQTRDVA GQAALAQFSL QLGVAEPAVF ATRAAGKKGV ALYPQGWPSL
     SDIREESVGL PESLALAVAR QESSFDPHAQ SPAQAIGLMQ LQTGTAQDVA RRAGLIGLDT
     SISGLRDPQT NLTLGRAYLS QLLDRYNQVL PMALSAYNAG PHRTDQWLQA DPPPTIPTQI
     DLVDWIESLP YEETRSYIER IEESLNLYRL KESSHA
//
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