ID A0A317MXJ3_9GAMM Unreviewed; 650 AA.
AC A0A317MXJ3;
DT 10-OCT-2018, integrated into UniProtKB/TrEMBL.
DT 10-OCT-2018, sequence version 1.
DT 27-MAR-2024, entry version 12.
DE SubName: Full=Soluble lytic murein transglycosylase {ECO:0000313|EMBL:PWV63248.1};
GN ORFNames=C7443_103173 {ECO:0000313|EMBL:PWV63248.1};
OS Plasticicumulans acidivorans.
OC Bacteria; Pseudomonadota; Gammaproteobacteria;
OC Candidatus Competibacteraceae; Plasticicumulans.
OX NCBI_TaxID=886464 {ECO:0000313|EMBL:PWV63248.1, ECO:0000313|Proteomes:UP000246569};
RN [1] {ECO:0000313|EMBL:PWV63248.1, ECO:0000313|Proteomes:UP000246569}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 23606 {ECO:0000313|EMBL:PWV63248.1,
RC ECO:0000313|Proteomes:UP000246569};
RA Goeker M.;
RT "Genomic Encyclopedia of Type Strains, Phase IV (KMG-IV): sequencing the
RT most valuable type-strain genomes for metagenomic binning, comparative
RT biology and taxonomic classification.";
RL Submitted (MAY-2018) 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:PWV63248.1}.
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DR EMBL; QGTJ01000003; PWV63248.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A317MXJ3; -.
DR Proteomes; UP000246569; Unassembled WGS sequence.
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 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 Reference proteome {ECO:0000313|Proteomes:UP000246569};
KW Signal {ECO:0000256|ARBA:ARBA00022729}.
FT DOMAIN 412..478
FT /note="Lytic transglycosylase superhelical linker"
FT /evidence="ECO:0000259|Pfam:PF14718"
FT DOMAIN 492..604
FT /note="Transglycosylase SLT"
FT /evidence="ECO:0000259|Pfam:PF01464"
SQ SEQUENCE 650 AA; 73253 MW; 7804775D21DF5D93 CRC64;
MALPLGRWAL AGWLIFAPCL ITPTTWAAPL TESALASQRR AFVDAERALL SGDTVRLRAL
SVQLHDYPLY PYLRYRELSR SLATSDARTV RRFLADFADT PLAPRLRGEW LRLLADQSRW
DDIVLDYRPD GDLELSCIQR TALLQQQRTA QALAGFDAAW LGEKTLPGRC DPVVQAWATQ
GGLTPAMAWQ RFTIGMQAGS TSAARQALPW LDPEDQDWAR LWLAVDQNPA LILQDSRLQA
SGDEHVEMIV AHGLMRWMNR DSVAAAPAVD EIRRRRTVTE EQLLPIERTL AIYMAARQHP
DALRRIDAIP TAYENDTLRE WRVRLYLLRG NWRATIDAIE HMPPAQLARP AWRYWRARAL
EGIGERSAAD IAYRELASLR DYYGFLAASH TSQRPAMTDH PVAKPLAAMQ TLASLPAVNR
ARELFLLGRP YDARSEWALV MDNADPQRLR AAALLVADWG WAGQAILWLA KAGDWNDLAL
RFPLPWRNEV ESAAHTTRLS PAWLYAIARQ ESTFQPEVRS PADARGLMQL LPSTAADVAR
GIGMRLNGSS SLYDPSINLK LGSIHLRQLL DRFDGNMVTA TAAYNAGENR IRDWLPSTDA
VDADIWVETI PFVETRNYVK RVWEYTAVFE YRLGLPVQGL TPNKVSSWSP
//
