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Database: UniProt
Entry: A0A0Q8FCI9_9GAMM
LinkDB: A0A0Q8FCI9_9GAMM
Original site: A0A0Q8FCI9_9GAMM 
ID   A0A0Q8FCI9_9GAMM        Unreviewed;       298 AA.
AC   A0A0Q8FCI9;
DT   20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT   20-JAN-2016, sequence version 1.
DT   27-MAR-2024, entry version 21.
DE   SubName: Full=Transglycosylase {ECO:0000313|EMBL:KRA53331.1};
GN   ORFNames=ASD77_01175 {ECO:0000313|EMBL:KRA53331.1};
OS   Pseudoxanthomonas sp. Root65.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Xanthomonadales;
OC   Xanthomonadaceae; Pseudoxanthomonas.
OX   NCBI_TaxID=1736576 {ECO:0000313|EMBL:KRA53331.1, ECO:0000313|Proteomes:UP000051430};
RN   [1] {ECO:0000313|EMBL:KRA53331.1, ECO:0000313|Proteomes:UP000051430}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Root65 {ECO:0000313|EMBL:KRA53331.1,
RC   ECO:0000313|Proteomes:UP000051430};
RA   Gilbert D.G.;
RL   Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:KRA53331.1, ECO:0000313|Proteomes:UP000051430}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Root65 {ECO:0000313|EMBL:KRA53331.1,
RC   ECO:0000313|Proteomes:UP000051430};
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   -!- 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:KRA53331.1}.
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DR   EMBL; LMHA01000001; KRA53331.1; -; Genomic_DNA.
DR   RefSeq; WP_055936142.1; NZ_LMHA01000001.1.
DR   AlphaFoldDB; A0A0Q8FCI9; -.
DR   STRING; 1736576.ASD77_01175; -.
DR   OrthoDB; 9815002at2; -.
DR   Proteomes; UP000051430; Unassembled WGS sequence.
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; cd00254; LT-like; 1.
DR   Gene3D; 1.10.530.10; -; 1.
DR   InterPro; IPR023346; Lysozyme-like_dom_sf.
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; SSF53955; Lysozyme-like; 1.
DR   PROSITE; PS00922; TRANSGLYCOSYLASE; 1.
PE   3: Inferred from homology;
KW   Reference proteome {ECO:0000313|Proteomes:UP000051430};
KW   Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..21
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           22..298
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5006339819"
FT   DOMAIN          173..271
FT                   /note="Transglycosylase SLT"
FT                   /evidence="ECO:0000259|Pfam:PF01464"
SQ   SEQUENCE   298 AA;  31464 MW;  50B3CA5A861661C8 CRC64;
     MRGTLTLLAM LAALTALPAS AGTLYKCTGA DGVPAYVSKR VSGSRCEVVS RYTPDRSRPT
     QVASVSRPVE TTPAIGAANA PALSDSASAI VPAAVTAPVP AATGPRRVVS GQVYSYIKDG
     VRHYTSARPQ GGTQVASLRT IKYSYIETCF ACGNPGVDFG RLRLNTSAYQ AEIAAASREF
     GVEEAVLRAI MHAESSYNPM ALSHAGAQGL MQLMPATARR FGVTDSYNAG QNIRGGAQYL
     SWLLKRFNGN LTLAAAGYNA GEGAVDRHGG VPPYKETQRY VQRVAVLADR YRQAVAAR
//
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