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Database: UniProt
Entry: A0A0P0NBH7_9SPHI
LinkDB: A0A0P0NBH7_9SPHI
Original site: A0A0P0NBH7_9SPHI 
ID   A0A0P0NBH7_9SPHI        Unreviewed;       407 AA.
AC   A0A0P0NBH7;
DT   20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT   20-JAN-2016, sequence version 1.
DT   27-MAR-2024, entry version 23.
DE   SubName: Full=Lytic murein transglycosylase {ECO:0000313|EMBL:ALL04441.1};
GN   ORFNames=AQ505_02380 {ECO:0000313|EMBL:ALL04441.1};
OS   Pedobacter sp. PACM 27299.
OC   Bacteria; Bacteroidota; Sphingobacteriia; Sphingobacteriales;
OC   Sphingobacteriaceae; Pedobacter.
OX   NCBI_TaxID=1727164 {ECO:0000313|EMBL:ALL04441.1, ECO:0000313|Proteomes:UP000062859};
RN   [1] {ECO:0000313|EMBL:ALL04441.1, ECO:0000313|Proteomes:UP000062859}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=PAMC 27299 {ECO:0000313|EMBL:ALL04441.1,
RC   ECO:0000313|Proteomes:UP000062859};
RA   Gilbert D.G.;
RL   Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
CC   -!- SIMILARITY: Belongs to the transglycosylase Slt family.
CC       {ECO:0000256|ARBA:ARBA00007734}.
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DR   EMBL; CP012996; ALL04441.1; -; Genomic_DNA.
DR   RefSeq; WP_062546703.1; NZ_CP012996.1.
DR   AlphaFoldDB; A0A0P0NBH7; -.
DR   STRING; 1727164.AQ505_02380; -.
DR   KEGG; pep:AQ505_02380; -.
DR   OrthoDB; 9815002at2; -.
DR   Proteomes; UP000062859; 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; cd00118; LysM; 1.
DR   CDD; cd16894; MltD-like; 1.
DR   Gene3D; 1.10.530.10; -; 1.
DR   Gene3D; 3.10.350.10; LysM domain; 1.
DR   InterPro; IPR018392; LysM_dom.
DR   InterPro; IPR036779; LysM_dom_sf.
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; PF01476; LysM; 1.
DR   Pfam; PF01464; SLT; 1.
DR   SMART; SM00257; LysM; 1.
DR   SUPFAM; SSF54106; LysM domain; 1.
DR   SUPFAM; SSF53955; Lysozyme-like; 1.
DR   PROSITE; PS51782; LYSM; 1.
DR   PROSITE; PS00922; TRANSGLYCOSYLASE; 1.
PE   3: Inferred from homology;
KW   Reference proteome {ECO:0000313|Proteomes:UP000062859};
KW   Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..21
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           22..407
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5006051791"
FT   DOMAIN          349..392
FT                   /note="LysM"
FT                   /evidence="ECO:0000259|PROSITE:PS51782"
SQ   SEQUENCE   407 AA;  45738 MW;  A36AB2A01EFCE473 CRC64;
     MKINVLFASC IIALTSFSAA AQQPQGSLQI IDTLALPVLP ETPTFHNHNY VFKARLDSIQ
     KMVPLSYNEH VQKYIDVYSS RKDMMGKMIG LSDYYFPVFE KALKFYNIPE EIKYLPIIES
     SMNAHAVSRV GATGLWQFMF ATAKDYGLNM DNFVDERKDP IQASYAAAAY FKDAYQELGD
     WLLAIAAYNC GMGNVKRAII KADSHDFWEI RPYLPLETRN YVPAFIAALY VMKCSGQHQI
     KAQASPFVKN TDTIHVNRFV SLPQLAMALS IEEDALCSLN PSYKKKIVNG TELEPKRIVI
     PKVNMAQFAE IYEVLNNAEL DVNQNVYLAS NDDRRVKKKI TAKPAAAVSY HKVTPGQTLS
     AIANKYNVEV QDLKVWNGLK SSSIVPGQKL KIHNPEPAKR KKSAIHG
//
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