ID   A1VLI7_POLNA            Unreviewed;       279 AA.
AC   A1VLI7;
DT   06-FEB-2007, integrated into UniProtKB/TrEMBL.
DT   06-FEB-2007, sequence version 1.
DT   27-MAR-2024, entry version 70.
DE   SubName: Full=Lytic transglycosylase, catalytic {ECO:0000313|EMBL:ABM36515.1};
GN   OrderedLocusNames=Pnap_1200 {ECO:0000313|EMBL:ABM36515.1};
OS   Polaromonas naphthalenivorans (strain CJ2).
OC   Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC   Comamonadaceae; Polaromonas.
OX   NCBI_TaxID=365044 {ECO:0000313|EMBL:ABM36515.1, ECO:0000313|Proteomes:UP000000644};
RN   [1] {ECO:0000313|Proteomes:UP000000644}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CJ2 {ECO:0000313|Proteomes:UP000000644};
RX   PubMed=19453698; DOI=10.1111/j.1462-2920.2009.01947.x;
RA   Yagi J.M., Sims D., Brettin T., Bruce D., Madsen E.L.;
RT   "The genome of Polaromonas naphthalenivorans strain CJ2, isolated from coal
RT   tar-contaminated sediment, reveals physiological and metabolic versatility
RT   and evolution through extensive horizontal gene transfer.";
RL   Environ. Microbiol. 11:2253-2270(2009).
CC   -!- SIMILARITY: Belongs to the transglycosylase Slt family.
CC       {ECO:0000256|ARBA:ARBA00007734}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; CP000529; ABM36515.1; -; Genomic_DNA.
DR   RefSeq; WP_011800608.1; NC_008781.1.
DR   AlphaFoldDB; A1VLI7; -.
DR   STRING; 365044.Pnap_1200; -.
DR   CAZy; GH23; Glycoside Hydrolase Family 23.
DR   KEGG; pna:Pnap_1200; -.
DR   eggNOG; COG0741; Bacteria.
DR   HOGENOM; CLU_065765_1_0_4; -.
DR   OrthoDB; 9815002at2; -.
DR   Proteomes; UP000000644; Chromosome.
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   CDD; cd16896; LT_Slt70-like; 1.
DR   Gene3D; 1.10.530.10; -; 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:UP000000644};
KW   Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..28
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           29..279
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5002639979"
FT   DOMAIN          101..208
FT                   /note="Transglycosylase SLT"
FT                   /evidence="ECO:0000259|Pfam:PF01464"
SQ   SEQUENCE   279 AA;  29874 MW;  99D0DCE7665C89D0 CRC64;
     MRLKLFSLLN LPLLAVLLTA LHAPPARADI WAYIDGQGVT HFSSLQLDER YELFSRGGES
     FTTGKTAGNP AQGAQGVAAT PPRLRAYFEL SPGYKAVRHL LREASDKHGI DYELLQALIA
     TESGFNAQAV SPKGAVGLMQ LIPPTAARYG VKSDKTAQAE QKLTDPRTNI RAGSSYLSDL
     MKLFPGEIEL AIAAYNAGEG AVQRAGNRIP NYPETKNYVK TVMQLYNQLK PASTGRSTSV
     SSGRVRMEMM GGASGRANMP AALAASPSLV LPEVAARLD
//