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Database: UniProt
Entry: A0A1V3Q880_9GAMM
LinkDB: A0A1V3Q880_9GAMM
Original site: A0A1V3Q880_9GAMM 
ID   A0A1V3Q880_9GAMM        Unreviewed;       680 AA.
AC   A0A1V3Q880;
DT   07-JUN-2017, integrated into UniProtKB/TrEMBL.
DT   07-JUN-2017, sequence version 1.
DT   27-MAR-2024, entry version 24.
DE   SubName: Full=Lytic murein transglycosylase {ECO:0000313|EMBL:OOG60664.1};
GN   ORFNames=B0E47_02015 {ECO:0000313|EMBL:OOG60664.1};
OS   Rhodanobacter sp. B05.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Xanthomonadales;
OC   Rhodanobacteraceae; Rhodanobacter.
OX   NCBI_TaxID=1945859 {ECO:0000313|EMBL:OOG60664.1, ECO:0000313|Proteomes:UP000188464};
RN   [1] {ECO:0000313|EMBL:OOG60664.1, ECO:0000313|Proteomes:UP000188464}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=B05 {ECO:0000313|EMBL:OOG60664.1,
RC   ECO:0000313|Proteomes:UP000188464};
RA   Lycus P., Bothun K.L., Bergaust L., Shapleigh J.P., Bakken L.R.,
RA   Frostegard A.;
RT   "Phenotypic and genotypic richness of denitrifiers revealed by a novel
RT   isolation strategy.";
RL   Submitted (FEB-2017) 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:OOG60664.1}.
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DR   EMBL; MUNU01000007; OOG60664.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1V3Q880; -.
DR   STRING; 1945859.B0E47_02015; -.
DR   OrthoDB; 92254at2; -.
DR   Proteomes; UP000188464; 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:UP000188464};
KW   Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..28
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           29..680
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5012302210"
FT   DOMAIN          408..468
FT                   /note="Lytic transglycosylase superhelical linker"
FT                   /evidence="ECO:0000259|Pfam:PF14718"
FT   DOMAIN          488..596
FT                   /note="Transglycosylase SLT"
FT                   /evidence="ECO:0000259|Pfam:PF01464"
SQ   SEQUENCE   680 AA;  74025 MW;  3FF01B8FBFDDDA47 CRC64;
     MPVSKPPCRP AFNWLLICTW LLAASLHAGE PTAAQRAAFK QAYAAAQQGD DNWRKLASGL
     HHYPLYPYLQ AAALEHDIQS IDLDMVQSYL RQYPDWIPAA DLRRSFLREL ARRQDWTDFL
     ALYQPGLGES LSCDALQAKL AQGGSLDFER DLATLWARPS LPNACDPVLS AAQAQGLLTD
     ARLWTRIDQA ADAGQAGTIV SLTDWLPAAE QASARQLALA LRDPAGALAT ASNWPDTPRD
     RQAATLALTR LARRQSSSAD SFWQQLQTHF SFGQQQRDQV LHALALFHAT DFDDGALARL
     IALPPAAQSD STREWRVRVA LARMNWPAVL AAIEAMTADQ QQDGEWQYFR ARALAASGHA
     GQARQQFAAL ADKSTFFGFL AADQLQQPYA ICPLTLADDS QREQQLLTRP GLRRAFELFA
     VDLPALARRE WTQALQGADG DTLRIAADLA NRRGWYDRAV FTLSSGEALR LYDLRFPLAS
     QDGLVPQAEQ AGIEPAWAYG ILRAESAWMS DARSGADARG LMQLLPATAA LVAKRNGLAW
     SGAASLYDPS VNIALGTRYL AQMAQRFNGS PWLASAAYNA GPNRVDQWLA ARGTLAPALF
     VATIPFKETR EYVARVMAFS VIYDWRLHGS AVPLTLRLSA IGQPYGLPDK DTPRRAISCP
     AAAPAAASSA PAAAATAAGN
//
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