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}.
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; 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
//