ID A0A083ZWX7_9GAMM Unreviewed; 642 AA.
AC A0A083ZWX7;
DT 29-OCT-2014, integrated into UniProtKB/TrEMBL.
DT 29-OCT-2014, sequence version 1.
DT 27-MAR-2024, entry version 27.
DE RecName: Full=peptidoglycan lytic exotransglycosylase {ECO:0000256|ARBA:ARBA00012587};
DE EC=4.2.2.n1 {ECO:0000256|ARBA:ARBA00012587};
GN Name=slt {ECO:0000313|EMBL:KEY57556.1};
GN ORFNames=SRDD_35370 {ECO:0000313|EMBL:KEY57556.1};
OS Serratia sp. DD3.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC Yersiniaceae; Serratia.
OX NCBI_TaxID=1410619 {ECO:0000313|EMBL:KEY57556.1, ECO:0000313|Proteomes:UP000017810};
RN [1] {ECO:0000313|EMBL:KEY57556.1, ECO:0000313|Proteomes:UP000017810}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DD3 {ECO:0000313|EMBL:KEY57556.1,
RC ECO:0000313|Proteomes:UP000017810};
RX PubMed=25212623;
RA Poehlein A., Freese H.M., Daniel R., Simeonova D.D.;
RT "Draft Genome Sequence of Serratia sp. Strain DD3, Isolated from the Guts
RT of Daphnia magna.";
RL Genome Announc. 2:e00903-14(2014).
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Exolytic cleavage of the (1->4)-beta-glycosidic linkage
CC between N-acetylmuramic acid (MurNAc) and N-acetylglucosamine
CC (GlcNAc) residues in peptidoglycan, from either the reducing or the
CC non-reducing ends of the peptidoglycan chains, with concomitant
CC formation of a 1,6-anhydrobond in the MurNAc residue.; EC=4.2.2.n1;
CC Evidence={ECO:0000256|ARBA:ARBA00001420};
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:KEY57556.1}.
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DR EMBL; AYKS02000089; KEY57556.1; -; Genomic_DNA.
DR RefSeq; WP_023489661.1; NZ_AYKS02000089.1.
DR AlphaFoldDB; A0A083ZWX7; -.
DR STRING; 1410619.SRDD_35370; -.
DR eggNOG; COG0741; Bacteria.
DR OrthoDB; 92254at2; -.
DR Proteomes; UP000017810; Unassembled WGS sequence.
DR GO; GO:0009279; C:cell outer membrane; IEA:UniProtKB-KW.
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:0071555; P:cell wall organization; IEA:UniProtKB-KW.
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 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; 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 Pfam; PF14718; SLT_L; 1.
DR SUPFAM; SSF48435; Bacterial muramidases; 1.
DR SUPFAM; SSF53955; Lysozyme-like; 1.
DR PROSITE; PS00922; TRANSGLYCOSYLASE; 1.
PE 3: Inferred from homology;
KW Cell outer membrane {ECO:0000256|ARBA:ARBA00023237};
KW Cell wall biogenesis/degradation {ECO:0000256|ARBA:ARBA00023316};
KW Lyase {ECO:0000256|ARBA:ARBA00023239, ECO:0000313|EMBL:KEY57556.1};
KW Membrane {ECO:0000256|ARBA:ARBA00023136};
KW Reference proteome {ECO:0000313|Proteomes:UP000017810};
KW Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..25
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 26..642
FT /note="peptidoglycan lytic exotransglycosylase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5001770475"
FT DOMAIN 405..469
FT /note="Lytic transglycosylase superhelical linker"
FT /evidence="ECO:0000259|Pfam:PF14718"
FT DOMAIN 482..593
FT /note="Transglycosylase SLT"
FT /evidence="ECO:0000259|Pfam:PF01464"
SQ SEQUENCE 642 AA; 73045 MW; 783DCBC1471412C5 CRC64;
MSKVDKWRIW AVGLSLTVFS SAVVADSLDA QRQRYLQIKQ AWDSNQMATV QQLMPTLQDY
PLYPYLEYRQ LAQDLSIVNV AQVSQFLQRN PTLPPAQSLS SRFVNELARR EDWRTLLAFS
PQEPKAAAAR CNYYYAKWVT GEQQVAWRGA GDIWLSGESL PSSCDKLFSV WQSAGKQTPA
DIQARMKLAL KAGNSGLVNA LYRQLPANEQ TMGEALVRLQ NDPGTVESFA RSAGPTDLTR
AATMIVFARL ARQDAENARL MIPTLARLQK MSDGEKLELE EAVAWRLMDN NATLAQTQWR
DQVILRSQSS ALLERRARMA LGMGDRQGLK TWLARLPQES RDKDEWRYWR AVQMIDEGQR
SEGEATLRSL MRERGFYPMV AAQKLNVPYP VMVEVATKPR ADLVSRPEID RVRELMYWNM
DNQARSEWSS LVASHNRADQ EALARYAFEQ KWAELSVQAT IVGKLWDHLE ERFPIAWEAE
FHRATEDKGI TPSYAMAIAR QESAWNPKAQ SPVGAAGLMQ VMPRTAEHTV QLYGIPGYSS
PSQLFDPKTN ITIGTHYLES VYQQFGRNRI LSSAAYNAGP SRVNTWLGNT EGRVDAVAFV
ESIPFNETRS YVKNVLAYDA FYRHFMNRPA KVLTDAEWSR RY
//
