ID A0A2T0X1X5_9RHOB Unreviewed; 677 AA.
AC A0A2T0X1X5;
DT 18-JUL-2018, integrated into UniProtKB/TrEMBL.
DT 18-JUL-2018, sequence version 1.
DT 24-JAN-2024, entry version 11.
DE SubName: Full=Soluble lytic murein transglycosylase {ECO:0000313|EMBL:PRY92917.1};
GN ORFNames=BCF33_1780 {ECO:0000313|EMBL:PRY92917.1};
OS Hasllibacter halocynthiae.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC Roseobacteraceae; Hasllibacter.
OX NCBI_TaxID=595589 {ECO:0000313|EMBL:PRY92917.1, ECO:0000313|Proteomes:UP000238801};
RN [1] {ECO:0000313|EMBL:PRY92917.1, ECO:0000313|Proteomes:UP000238801}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 29318 {ECO:0000313|EMBL:PRY92917.1,
RC ECO:0000313|Proteomes:UP000238801};
RA Goeker M.;
RT "Genomic Encyclopedia of Archaeal and Bacterial Type Strains, Phase II
RT (KMG-II): from individual species to whole genera.";
RL Submitted (MAR-2018) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the transglycosylase Slt family.
CC {ECO:0000256|ARBA:ARBA00007734}.
CC -!- SIMILARITY: Belongs to the virb1 family.
CC {ECO:0000256|ARBA:ARBA00009387}.
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:PRY92917.1}.
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DR EMBL; PVTT01000002; PRY92917.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2T0X1X5; -.
DR OrthoDB; 9815002at2; -.
DR Proteomes; UP000238801; 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 InterPro; IPR023346; Lysozyme-like_dom_sf.
DR InterPro; IPR008939; Lytic_TGlycosylase_superhlx_U.
DR InterPro; IPR000189; Transglyc_AS.
DR InterPro; IPR008258; Transglycosylase_SLT_dom_1.
DR PANTHER; PTHR37423:SF2; CELL DIVISION COORDINATOR CPOB-RELATED; 1.
DR PANTHER; PTHR37423; SOLUBLE LYTIC MUREIN TRANSGLYCOSYLASE-RELATED; 1.
DR Pfam; PF01464; SLT; 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:UP000238801};
KW Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..19
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 20..677
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5015407783"
FT DOMAIN 521..618
FT /note="Transglycosylase SLT"
FT /evidence="ECO:0000259|Pfam:PF01464"
SQ SEQUENCE 677 AA; 73473 MW; FAE592D31D844203 CRC64;
MSRALAIVML CLGAAPLAAQ DLAPVSSLRP EARGEGPSAR VASMGTQAPA RFAGAALERA
MEHVRARRWG DALSAAGGDG TAARDVVLWH ALRARQGTWD QAADFVARNG EWPGMPLLKA
RAERLMPAGL PAAEVLRWFE DHEPQTATGA LRYAAALREA GEAEAADAVL AIGWSEGLPM
SPGTERQYLF AAGDILDGLH EARMDALLWA GHSESATRQM ARVGEGWQAL ARARMALRAG
QRDGVNALIA AVPGSHADDA GLAYERFVWR LDRGLEETAL DLMLERSDSA ERLGRPELWS
EVRLDEARAL MIRGEARDAY RMASRHRIPE DTEEGVRRAT LEWLAGYVAL RQLGDAETAL
RHFREAARTV ETPVSVARMG YWQGRALDAL GRADEAREAY AAAARFQTAF YGQLAAEAAG
LPVDPALAGD LSAEDGALPD TDMLGTVELL LAAGERRLAA RFVAHLAESQ DRAGMIALGE
WVQRRDPYLE VIFGKRAARY GAVLPEFYFP VHPMAEADIP IPTEMALAVA RQESEFHPGA
GSPVGAQGLM QLMPGTAQDV TRDLGLSYSH ARLTSDPEYN ATLGAEYLRQ LEARFGFNVP
MIAAGYNAGP GRPLRWARPG FDPRGATVEE AVDWVERIPF DETRNYVMRV TEGMGVYRQR
LAGEPVPLST GEMLTGR
//