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Database: UniProt
Entry: A0A0Q5VCJ1_9CAUL
LinkDB: A0A0Q5VCJ1_9CAUL
Original site: A0A0Q5VCJ1_9CAUL 
ID   A0A0Q5VCJ1_9CAUL        Unreviewed;       557 AA.
AC   A0A0Q5VCJ1;
DT   20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT   20-JAN-2016, sequence version 1.
DT   27-MAR-2024, entry version 23.
DE   SubName: Full=Transglycosylase {ECO:0000313|EMBL:KQS55547.1};
GN   ORFNames=ASG17_05580 {ECO:0000313|EMBL:KQS55547.1};
OS   Brevundimonas sp. Leaf363.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Caulobacterales;
OC   Caulobacteraceae; Brevundimonas.
OX   NCBI_TaxID=1736353 {ECO:0000313|EMBL:KQS55547.1, ECO:0000313|Proteomes:UP000051182};
RN   [1] {ECO:0000313|EMBL:KQS55547.1, ECO:0000313|Proteomes:UP000051182}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Leaf363 {ECO:0000313|EMBL:KQS55547.1,
RC   ECO:0000313|Proteomes:UP000051182};
RA   Gilbert D.G.;
RL   Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:KQS55547.1, ECO:0000313|Proteomes:UP000051182}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Leaf363 {ECO:0000313|EMBL:KQS55547.1,
RC   ECO:0000313|Proteomes:UP000051182};
RA   Schulze-Lefert P.;
RT   "Functional overlap of the Arabidopsis leaf and root microbiotas.";
RL   Submitted (NOV-2015) 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   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:KQS55547.1}.
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DR   EMBL; LMPZ01000002; KQS55547.1; -; Genomic_DNA.
DR   RefSeq; WP_056100313.1; NZ_LMPZ01000002.1.
DR   AlphaFoldDB; A0A0Q5VCJ1; -.
DR   STRING; 1736353.ASG17_05580; -.
DR   OrthoDB; 9815002at2; -.
DR   Proteomes; UP000051182; 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; 2.
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   Reference proteome {ECO:0000313|Proteomes:UP000051182};
KW   Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..29
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           30..557
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5006265698"
FT   DOMAIN          370..470
FT                   /note="Transglycosylase SLT"
FT                   /evidence="ECO:0000259|Pfam:PF01464"
SQ   SEQUENCE   557 AA;  60022 MW;  7E2528F9BD837A36 CRC64;
     MVLFRRANLA LTLGLVSALM LGAPAGARAM EAPTALSSAD RINYTTAFDA LRRGDLETAR
     AAARAAHDRV LLGQVEFERM FHADYSVTYD ELVAWLNDYA DMPCAGRVYN LALRRQPDGA
     APPPRPVTLI SRTWNIVSPG GGADPEDPAK QARIAYNNDD LTDAVDKGRD SGDWWTVGLA
     TWRLNQFQAS LEAFDRVADD PTQDAWVRAG AGVWAARAAL RVGHQDRVTP YLQQAAQWPA
     TFYGQIALRQ LGIEPTIQNQ GPTPYQPGGL QRASFTADSN TEAGVDARQL EAFVQSDARA
     KRSVAFFEVG RRQDAEAELR TGIRTATEGN ARRLWTALAR ALGPRTPGGA EAATIDATRY
     PTPVLEPEGG FTIERALVYA IARKETGFNA SARSGVGAYG MMQVMPGTAA QMTGDRDFIA
     HPERLFQPAT NLRLGQVYVN RVLQMPALQG DLLRAVASYN AGPGPMVAAV RKLGPDADPL
     LLIETIDVPQ ARDYVEKVVA AYWIYQRMFG GPLNTLDAVA SGATAIPISL DYVAPPPAPV
     QPASMEVAAV APPVGTR
//
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