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Database: UniProt
Entry: A0A432VLT3_9SPHN
LinkDB: A0A432VLT3_9SPHN
Original site: A0A432VLT3_9SPHN 
ID   A0A432VLT3_9SPHN        Unreviewed;       606 AA.
AC   A0A432VLT3;
DT   08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT   08-MAY-2019, sequence version 1.
DT   27-MAR-2024, entry version 11.
DE   SubName: Full=Lytic transglycosylase domain-containing protein {ECO:0000313|EMBL:RUN77760.1};
GN   ORFNames=EJC47_05085 {ECO:0000313|EMBL:RUN77760.1};
OS   Sphingomonas sp. TF3.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Sphingomonadales;
OC   Sphingomonadaceae; Sphingomonas.
OX   NCBI_TaxID=2495580 {ECO:0000313|EMBL:RUN77760.1, ECO:0000313|Proteomes:UP000275325};
RN   [1] {ECO:0000313|EMBL:RUN77760.1, ECO:0000313|Proteomes:UP000275325}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=TF3 {ECO:0000313|EMBL:RUN77760.1,
RC   ECO:0000313|Proteomes:UP000275325};
RA   Afonin A., Vasilieva E., Akhtemova G., Zhukov V.;
RT   "The Draft Genome Sequence of a Sphingomonas sp strain TF3.";
RL   Submitted (DEC-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:RUN77760.1}.
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DR   EMBL; RWKS01000004; RUN77760.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A432VLT3; -.
DR   Proteomes; UP000275325; Unassembled WGS sequence.
DR   GO; GO:0042597; C:periplasmic space; IEA:InterPro.
DR   GO; GO:0004553; F:hydrolase activity, hydrolyzing O-glycosyl compounds; 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; 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.
PE   3: Inferred from homology;
KW   Reference proteome {ECO:0000313|Proteomes:UP000275325};
KW   Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..22
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           23..606
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5019114479"
FT   DOMAIN          411..516
FT                   /note="Transglycosylase SLT"
FT                   /evidence="ECO:0000259|Pfam:PF01464"
FT   REGION          586..606
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   606 AA;  64967 MW;  5798C6EDAC6ED71A CRC64;
     MSAKLALSAA VAAFLTPAAA NAAIEPPAIQ NAPVRATIPP QLDAEQREGY RAVFASIRSQ
     RWQDAQLQLA ALKPGPLHAI AQAELLTAKG SPKADLDPLM KLLADAPELP QAKQILTMAA
     SRGGVGLPPL PEARALTWID GAPARKRAKS FGKGDLLAVE LALKMQPFIK DDRGAEAQAL
     LESTPGLSSD LQTEWQRKIA WMYFLAGDDT NARLMAQKAA SGYGDFAVEG QWVGALAAWR
     QHDCAAAGTL FEGVAARAND VDLRAAALYW AARADMQCAR PDRVENRLKS AAQYRETFYG
     LLARQALGIR ETTPHPATVA VANDWQILGR RPNVRVAAAL VEIGENGLAD SVIRQQARIG
     DPSEYPALVR LTAALDLPAT QIWLSHNGPV GATPPLEARF PAPNWAPDGG WRVDKALVFA
     HTLQESRFRT DVVSPAGAYG LMQVRPGAAT DIARKQGRTF DRSALSRPGT NFEVGQSYLE
     QLRDQHCTDG LLPKVIAAYN AGPGPVEAWN AQARDGGDPL LYIESIPYWE TRGYVTTVLR
     NYWIYETQTG KTASVSRAAL SQGLWPRFPG LPGAAAVRLT SSASSGRTMA STTATSPAGR
     AIARAD
//
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