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Database: UniProt
Entry: S9QJJ4_9RHOB
LinkDB: S9QJJ4_9RHOB
Original site: S9QJJ4_9RHOB 
ID   S9QJJ4_9RHOB            Unreviewed;       445 AA.
AC   S9QJJ4;
DT   16-OCT-2013, integrated into UniProtKB/TrEMBL.
DT   16-OCT-2013, sequence version 1.
DT   24-JAN-2024, entry version 31.
DE   SubName: Full=Membrane-bound lytic murein transglycosylase B {ECO:0000313|EMBL:EPX79768.1};
DE            EC=3.2.1.- {ECO:0000313|EMBL:EPX79768.1};
GN   ORFNames=Salmuc_05126 {ECO:0000313|EMBL:EPX79768.1};
OS   Salipiger mucosus DSM 16094.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC   Roseobacteraceae; Salipiger.
OX   NCBI_TaxID=1123237 {ECO:0000313|EMBL:EPX79768.1, ECO:0000313|Proteomes:UP000015347};
RN   [1] {ECO:0000313|Proteomes:UP000015347}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 16094 {ECO:0000313|Proteomes:UP000015347};
RX   PubMed=25197501; DOI=10.4056/sigs.4909790;
RA   Riedel T., Spring S., Fiebig A., Petersen J., Kyrpides N.C., Goker M.,
RA   Klenk H.P.;
RT   "Genome sequence of the exopolysaccharide-producing Salipiger mucosus type
RT   strain (DSM 16094(T)), a moderately halophilic member of the Roseobacter
RT   clade.";
RL   Stand. Genomic Sci. 9:1331-1343(2014).
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:EPX79768.1}.
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DR   EMBL; APVH01000034; EPX79768.1; -; Genomic_DNA.
DR   AlphaFoldDB; S9QJJ4; -.
DR   STRING; 1123237.Salmuc_05126; -.
DR   eggNOG; COG2951; Bacteria.
DR   eggNOG; COG3409; Bacteria.
DR   HOGENOM; CLU_035402_0_2_5; -.
DR   Proteomes; UP000015347; Unassembled WGS sequence.
DR   GO; GO:0016798; F:hydrolase activity, acting on glycosyl bonds; IEA:UniProtKB-KW.
DR   GO; GO:0008152; P:metabolic process; IEA:UniProtKB-KW.
DR   CDD; cd13399; Slt35-like; 1.
DR   Gene3D; 1.10.530.10; -; 1.
DR   Gene3D; 1.10.8.350; Bacterial muramidase; 1.
DR   Gene3D; 1.10.101.10; PGBD-like superfamily/PGBD; 1.
DR   InterPro; IPR023346; Lysozyme-like_dom_sf.
DR   InterPro; IPR043426; MltB-like.
DR   InterPro; IPR011970; MltB_2.
DR   InterPro; IPR002477; Peptidoglycan-bd-like.
DR   InterPro; IPR036365; PGBD-like_sf.
DR   InterPro; IPR036366; PGBDSf.
DR   InterPro; IPR031304; SLT_2.
DR   NCBIfam; TIGR02283; MltB_2; 1.
DR   PANTHER; PTHR30163; MEMBRANE-BOUND LYTIC MUREIN TRANSGLYCOSYLASE B; 1.
DR   PANTHER; PTHR30163:SF8; MEMBRANE-BOUND LYTIC MUREIN TRANSGLYCOSYLASE B; 1.
DR   Pfam; PF01471; PG_binding_1; 1.
DR   Pfam; PF13406; SLT_2; 1.
DR   SUPFAM; SSF53955; Lysozyme-like; 1.
DR   SUPFAM; SSF47090; PGBD-like; 1.
PE   4: Predicted;
KW   Glycosidase {ECO:0000313|EMBL:EPX79768.1};
KW   Hydrolase {ECO:0000313|EMBL:EPX79768.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000015347};
KW   Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..22
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           23..445
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5004568084"
FT   DOMAIN          76..367
FT                   /note="Transglycosylase SLT"
FT                   /evidence="ECO:0000259|Pfam:PF13406"
FT   DOMAIN          389..443
FT                   /note="Peptidoglycan binding-like"
FT                   /evidence="ECO:0000259|Pfam:PF01471"
FT   REGION          24..57
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   445 AA;  48765 MW;  51AFE4950F6F901D CRC64;
     MQRIASLAAI AVAAVTAGAT LAQGTAPAAP GARPPGPATE NTRLPPQASP RPEQRPETLA
     SAEKAVAERD ASAADFRRWV EDFRPRALAQ GIDARIFDRA FEGVSYDPAV IRRDRSQNEF
     TKTVWVYLDS AVSDARVAAG REAHEENRAL LDEIEARYDV DKRVLLAIWG LESAYGTFRG
     SERVIRSLAT LAYDTRRADF FEGQLLDALH ILQNGHTTPA QMRGSWAGAM GHTQFMPSSF
     RELAVDWDGD GKRDIWSDDP ADALASAANY LQENGWQHGL PWGVEVTLPE DFDYTLAARE
     ITKMPSDWAG LGVTATDGSP VPDHGPASVL LPGGHRGAAF LIFDNFEVIE SYNTADAYVI
     GVGHLGDRIM GGPPVQHDWP REDRALTLEE RLELQRRLRE AGFDPEKIDG RIGPLTINAV
     RDYQQSEGMV PDGYPSLQVL EALRS
//
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