ID A0A0D6MMS5_9PROT Unreviewed; 642 AA.
AC A0A0D6MMS5;
DT 27-MAY-2015, integrated into UniProtKB/TrEMBL.
DT 27-MAY-2015, sequence version 1.
DT 27-MAR-2024, entry version 24.
DE RecName: Full=Transglycosylase SLT domain-containing protein {ECO:0000259|Pfam:PF01464};
GN ORFNames=Tasa_025_024 {ECO:0000313|EMBL:GAN54593.1};
OS Tanticharoenia sakaeratensis NBRC 103193.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodospirillales;
OC Acetobacteraceae; Tanticharoenia.
OX NCBI_TaxID=1231623 {ECO:0000313|EMBL:GAN54593.1, ECO:0000313|Proteomes:UP000032679};
RN [1] {ECO:0000313|EMBL:GAN54593.1, ECO:0000313|Proteomes:UP000032679}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NBRC 103193 {ECO:0000313|EMBL:GAN54593.1,
RC ECO:0000313|Proteomes:UP000032679};
RA Azuma Y., Hadano H., Hirakawa H., Matsushita K.;
RT "Genome sequencing of Tanticharoenia sakaeratensis NBRC 103193.";
RL Submitted (OCT-2012) 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:GAN54593.1}.
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DR EMBL; BALE01000025; GAN54593.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0D6MMS5; -.
DR STRING; 1231623.Tasa_025_024; -.
DR Proteomes; UP000032679; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:InterPro.
DR GO; GO:0008933; F:lytic transglycosylase activity; IEA:InterPro.
DR GO; GO:0000270; P:peptidoglycan metabolic process; IEA:InterPro.
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; 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 SUPFAM; SSF53955; Lysozyme-like; 1.
DR PROSITE; PS00922; TRANSGLYCOSYLASE; 1.
PE 3: Inferred from homology;
KW Reference proteome {ECO:0000313|Proteomes:UP000032679};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..20
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 21..642
FT /note="Transglycosylase SLT domain-containing protein"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5002308013"
FT DOMAIN 456..574
FT /note="Transglycosylase SLT"
FT /evidence="ECO:0000259|Pfam:PF01464"
FT REGION 19..66
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 19..46
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 642 AA; 68296 MW; FEBCF740E1D35656 CRC64;
MLVSAAILAG AAFLPARAQA SSSSMRSDGA TTEGATTQST GSPVPGSEET AFAPQRGSGP
NGYAVPLPRP LKPSVAAHLR AIFAAQRASD FATAEQLSDH LDDDTLLGDI LADRYLNPAY
HPTAAQLRQW LHSFPSLADA PQILARLSAV SPRGTVPSQS FPQPLSPSTV ADQTEAALDP
LSHLVIRNPL LDHTVAERTG WGPNGARSAL KLIAATPGMT PLYAAQLRAE IALAMLSSGE
DALAYEIANT AFAQDGQLAF AGFVAGLAAW HRDMIDTAGH LFETASRAPI AQNEIRAASR
FWAARARARV HDHRGYTAWM SRAAAAPGTF YGILATRALE VAHHPHGDAQ TTLAASEPVP
VLSEIDVDAV AATAQGARLF ALLQVGETDR AEALLRRLWP DIKGDAALCR SVQLVAQEAG
YRDLSEQIAT ILAARDGDLA HVSGFPMPQL KPRHGFRMDP ALVYAMTRLE SNFDARASSG
AGAHGLMQIM PVTAAFVTAP HGAGARVIAS PDIVDRLHVP AINLEIGQLY MLYLADLSRN
ARGTVEPPTG GDMVRMLASY NAGPSAISRW ASIQTHIADP LMFIETLPNP ETRNYVHRAF
TYLWIYADKL DLPAPSLASL ADAHWPAFSE ETALAGRTVT LH
//
