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Database: UniProt
Entry: A0A2T0X1X5_9RHOB
LinkDB: A0A2T0X1X5_9RHOB
Original site: A0A2T0X1X5_9RHOB 
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
//
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