ID A0A1B7UFX1_9GAMM Unreviewed; 637 AA.
AC A0A1B7UFX1;
DT 02-NOV-2016, integrated into UniProtKB/TrEMBL.
DT 02-NOV-2016, sequence version 1.
DT 27-MAR-2024, entry version 18.
DE SubName: Full=Murein transglycosylase {ECO:0000313|EMBL:OBP13403.1};
GN ORFNames=A5320_19040 {ECO:0000313|EMBL:OBP13403.1};
OS Rheinheimera sp. SA_1.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Chromatiales; Chromatiaceae;
OC Rheinheimera.
OX NCBI_TaxID=1827365 {ECO:0000313|EMBL:OBP13403.1, ECO:0000313|Proteomes:UP000092258};
RN [1] {ECO:0000313|EMBL:OBP13403.1, ECO:0000313|Proteomes:UP000092258}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SA_1 {ECO:0000313|EMBL:OBP13403.1,
RC ECO:0000313|Proteomes:UP000092258};
RA Lavstsen T., Jespersen J.S.;
RL Submitted (MAY-2016) 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:OBP13403.1}.
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DR EMBL; LXWK01000020; OBP13403.1; -; Genomic_DNA.
DR RefSeq; WP_068069592.1; NZ_LXWK01000020.1.
DR AlphaFoldDB; A0A1B7UFX1; -.
DR STRING; 1827365.A5320_19040; -.
DR OrthoDB; 92254at2; -.
DR Proteomes; UP000092258; 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:UP000092258};
KW Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..23
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 24..637
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5008599143"
FT DOMAIN 402..467
FT /note="Lytic transglycosylase superhelical linker"
FT /evidence="ECO:0000259|Pfam:PF14718"
FT DOMAIN 479..585
FT /note="Transglycosylase SLT"
FT /evidence="ECO:0000259|Pfam:PF01464"
SQ SEQUENCE 637 AA; 73843 MW; 71310F76BC910C9C CRC64;
MLRTRGRLLL CLLTAICSIS TQAAPSDQVL RERFLKAEKS IHKVTPEQAG KMLRDLHQYP
LKPYIELEVL SRSLKDTVKV KEFIKRHQGT PLEWTLKKRW LMYLAGVGLT QPYLKNYAMG
TDVVLDCYAL QLRLINQPPA DVWPEVTQLW TVGKSLPKEC DPLFSRWQKA GQRTPEVIWA
RLSKVADGGD VRIIPYLRTL LPKNLQYLGD KWKHVIENPG LVQRQKFLPL KHRWEREILA
YALKKMIWKQ PEQALRVWQR FESDPQFTKS QRIDVARQFA IALASKDDPR AAKFMPMVPV
ELKDDLFIQW QLTWLLRQNQ WQQVQDLILE LPAESQSDDS LQYWLARAYQ QTGLLEKGDQ
LLAKVAVQRS YYGFMAAAKL GLKPSLAHRP VPISAEQYQA FKKSDSIARM YEWQAIGRPN
AAKRELSFLQ KYGSETQKFG AAKYAYDKGW YDRAIFALAD AGYWDDVDMR FPMVFNQEIQ
KHAKAARVDP AWAMAITRRE STFIPTAKSP VGAHGLMQIM PQTAKHITGR RVPVETLYNP
NTNIDMGTDY LNYLMRQNDN NLVFATASYN AGYSRVKTWL PKNRQMPLDI WIETIPFKET
REYVKAVLAY YQIYNIRMNQ PTDVFVPLST MQVGETT
//
