ID A0A1I1NYL4_9RHOB Unreviewed; 650 AA.
AC A0A1I1NYL4;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 27-MAR-2024, entry version 14.
DE SubName: Full=Soluble lytic murein transglycosylase {ECO:0000313|EMBL:SFD02555.1};
GN ORFNames=SAMN04488094_11388 {ECO:0000313|EMBL:SFD02555.1};
OS Tropicimonas isoalkanivorans.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC Roseobacteraceae; Tropicimonas.
OX NCBI_TaxID=441112 {ECO:0000313|EMBL:SFD02555.1, ECO:0000313|Proteomes:UP000198728};
RN [1] {ECO:0000313|EMBL:SFD02555.1, ECO:0000313|Proteomes:UP000198728}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 19548 {ECO:0000313|EMBL:SFD02555.1,
RC ECO:0000313|Proteomes:UP000198728};
RA de Groot N.N.;
RL Submitted (OCT-2016) 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}.
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DR EMBL; FOLG01000013; SFD02555.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1I1NYL4; -.
DR STRING; 441112.SAMN04488094_11388; -.
DR OrthoDB; 9815002at2; -.
DR Proteomes; UP000198728; 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; SOLUBLE LYTIC MUREIN TRANSGLYCOSYLASE; 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:UP000198728};
KW Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..21
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 22..650
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5011755820"
FT DOMAIN 494..593
FT /note="Transglycosylase SLT"
FT /evidence="ECO:0000259|Pfam:PF01464"
SQ SEQUENCE 650 AA; 71477 MW; EC2FA3E5C3EC99E0 CRC64;
MRRVTPFLLF FIVWLPLQSA AAQSSQAEAL SQALNQVRAA NWRAAAVAAN GAGTVGRDIV
EWHRLRQGGQ ATFDAYRDFI SRHPDWPGLS LLRTRGEGSI PEDAAPSEVL AYFDGDLPET
GTGVVRVVQA HLALGQQGDA EALAVMAWRA RSLSPETEDV LLGLFGDLLK RHNTERLDEL
LWRGETGAAQ RMLPRVPEDW QALAEARMAL ATMAPGVDKR IEAVPAALAE DAGLAYERFN
WRIRKGRGDD AIAFMAQRST SPDSLGRPEK WANWRRIFAR RLMRDGKAPE AYALASQHFL
VEGSDFADLE WLSGFIALRF LADPELALLH FDRFAEAVRT PISLGRAGYW RGRALTALGD
DAGAQEAFAE GAKYQTSYYG LLSAEAAGLP MDPDLAGRET FEDGKAEALT DRAVVKAGLL
LLEAGETALA ERFLTQTAEE WPRQEVGALA AQLMDRGETH IALMLAKRAA GGGVVLPAAY
FPLSRHMDRD LPIPREWALA IARRESEFDP VVVSPAGARG LMQLMPGTAR DVAFEIKVPY
DRDGLTRRPD YNVTLGTKYL SGLFEVFGEA PVLVSVGYNA GPGRSVDWVS RFGDPRSPEV
DIIDWVEMIP FRETRNYVMR VSESILIYRA RLSGKTGEAP VAMTAFLREG
//