ID A0A7U4DNF3_DESPD Unreviewed; 615 AA.
AC A0A7U4DNF3;
DT 02-JUN-2021, integrated into UniProtKB/TrEMBL.
DT 02-JUN-2021, sequence version 1.
DT 28-JAN-2026, entry version 12.
DE SubName: Full=Lytic transglycosylase catalytic {ECO:0000313|EMBL:ADW17056.1};
GN OrderedLocusNames=Despr_0882 {ECO:0000313|EMBL:ADW17056.1};
OS Desulfobulbus propionicus (strain ATCC 33891 / DSM 2032 / VKM B-1956 /
OS 1pr3).
OC Bacteria; Pseudomonadati; Thermodesulfobacteriota; Desulfobulbia;
OC Desulfobulbales; Desulfobulbaceae; Desulfobulbus.
OX NCBI_TaxID=577650 {ECO:0000313|EMBL:ADW17056.1, ECO:0000313|Proteomes:UP000006365};
RN [1] {ECO:0000313|EMBL:ADW17056.1, ECO:0000313|Proteomes:UP000006365}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 33891 / DSM 2032 / 1pr3
RC {ECO:0000313|Proteomes:UP000006365};
RX PubMed=21475592; DOI=10.4056/sigs.1613929;
RA Pagani I., Lapidus A., Nolan M., Lucas S., Hammon N., Deshpande S.,
RA Cheng J.F., Chertkov O., Davenport K., Tapia R., Han C., Goodwin L.,
RA Pitluck S., Liolios K., Mavromatis K., Ivanova N., Mikhailova N., Pati A.,
RA Chen A., Palaniappan K., Land M., Hauser L., Chang Y.J., Jeffries C.D.,
RA Detter J.C., Brambilla E., Kannan K.P., Djao O.D., Rohde M., Pukall R.,
RA Spring S., Goker M., Sikorski J., Woyke T., Bristow J., Eisen J.A.,
RA Markowitz V., Hugenholtz P., Kyrpides N.C., Klenk H.P.;
RT "Complete genome sequence of Desulfobulbus propionicus type strain
RT (1pr3).";
RL Stand. Genomic Sci. 4:100-110(2011).
CC -!- SIMILARITY: Belongs to the transglycosylase Slt family.
CC {ECO:0000256|ARBA:ARBA00007734}.
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DR EMBL; CP002364; ADW17056.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A7U4DNF3; -.
DR KEGG; dpr:Despr_0882; -.
DR Proteomes; UP000006365; Chromosome.
DR GO; GO:0016020; C:membrane; IEA:InterPro.
DR GO; GO:0008932; F:lytic endotransglycosylase activity; IEA:TreeGrafter.
DR GO; GO:0000270; P:peptidoglycan metabolic process; IEA:InterPro.
DR CDD; cd00118; LysM; 3.
DR CDD; cd16894; MltD-like; 1.
DR Gene3D; 1.10.530.10; -; 1.
DR Gene3D; 3.10.350.10; LysM domain; 3.
DR InterPro; IPR018392; LysM.
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; PTHR33734; LYSM DOMAIN-CONTAINING GPI-ANCHORED PROTEIN 2; 1.
DR PANTHER; PTHR33734:SF22; MEMBRANE-BOUND LYTIC MUREIN TRANSGLYCOSYLASE D; 1.
DR Pfam; PF01476; LysM; 3.
DR Pfam; PF01464; SLT; 1.
DR SMART; SM00257; LysM; 3.
DR SUPFAM; SSF54106; LysM domain; 3.
DR SUPFAM; SSF53955; Lysozyme-like; 1.
DR PROSITE; PS51782; LYSM; 3.
DR PROSITE; PS51257; PROKAR_LIPOPROTEIN; 1.
DR PROSITE; PS00922; TRANSGLYCOSYLASE; 1.
PE 3: Inferred from homology;
KW Reference proteome {ECO:0000313|Proteomes:UP000006365};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..24
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 25..615
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5030792662"
FT DOMAIN 355..398
FT /note="LysM"
FT /evidence="ECO:0000259|PROSITE:PS51782"
FT DOMAIN 438..482
FT /note="LysM"
FT /evidence="ECO:0000259|PROSITE:PS51782"
FT DOMAIN 569..612
FT /note="LysM"
FT /evidence="ECO:0000259|PROSITE:PS51782"
SQ SEQUENCE 615 AA; 68286 MW; E4BF7C14017407D2 CRC64;
MKILPVLLNS CCIALLCISL SACSSHPKRS ALHRSPTPVT DADIQDEEIA SAEPEETAQE
ELEALNKPGA WEYGVKTTYS LEKLGIDPSK YDFPITVNKQ VLYYLELFQG KQRNYFTQWL
ARSTIYRPYI ERELKRAGLP LDLVYLAMIE SGFNPSAYSP AEACGLWQFM EGTAQTYKLR
VDSWVDERRE PEKATKAAIR YLSRLYSQFG DWYLAVAAYN AGEGKIDTAM KTYNASDFWE
VAASEGIFME TKRYVPKLIA AIIIARNPEK YGFTDIAYKT PHEYETITVP GGVALEAVAL
TANTSIKQLR SLNNELRKNQ TPPKNEYTLR IPVGCKELIA ANLDKLRPVT RTVYTTHTVK
KGETLTEICN LYKISKTSLL KANNLRTAQL KRGLRLQIPS TSTKYVLLNS EDQAEDRVAK
VDKPGKMVKV EPAKQQAVSH RVKQGETVAS IAKQYQVSTK DILRWNKIAN SSTIKSGQKL
SLYPERPQPE PVTVAAKAVK IAAAKTAAIP TLDPSTKKQS VQNVAKAPSG NKPEVIKPTA
TKTSIAKTAK AEPAAKVSVA IAKSTKPHTW YVVKNGDTLT AIAKKFQTST QDIRAWNKLS
TNTVQTGNKL LVKKG
//
