UL28B_NONUL
ID UL28B_NONUL Reviewed; 303 AA.
AC A0A084JZF2;
DT 16-OCT-2019, integrated into UniProtKB/Swiss-Prot.
DT 29-OCT-2014, sequence version 1.
DT 03-AUG-2022, entry version 23.
DE RecName: Full=Ulvan lyase NLR48 {ECO:0000303|PubMed:29875159};
DE EC=4.2.2.- {ECO:0000250|UniProtKB:G8G2V6};
DE Flags: Precursor;
GN ORFNames=IL45_01530, PLR_48 {ECO:0000303|PubMed:25125644};
OS Nonlabens ulvanivorans (Persicivirga ulvanivorans).
OC Bacteria; Bacteroidetes; Flavobacteriia; Flavobacteriales;
OC Flavobacteriaceae; Nonlabens.
OX NCBI_TaxID=906888;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 22727 / CIP 110082 / PLR;
RX PubMed=25125644; DOI=10.1128/genomea.00793-14;
RA Kopel M., Helbert W., Henrissat B., Doniger T., Banin E.;
RT "Draft genome sequence of Nonlabens ulvanivorans, an ulvan-degrading
RT bacterium.";
RL Genome Announc. 2:0-0(2014).
RN [2] {ECO:0007744|PDB:6D2C, ECO:0007744|PDB:6D3U}
RP X-RAY CRYSTALLOGRAPHY (1.91 ANGSTROMS) IN COMPLEX WITH CALCIUM IONS,
RP DISULFIDE BOND, AND MUTAGENESIS OF ARG-117; GLN-160; LYS-162 AND ARG-216.
RX PubMed=29875159; DOI=10.1074/jbc.ra118.003659;
RA Ulaganathan T., Banin E., Helbert W., Cygler M.;
RT "Structural and functional characterization of PL28 family ulvan lyase
RT NLR48 from Nonlabens ulvanivorans.";
RL J. Biol. Chem. 293:11564-11573(2018).
CC -!- FUNCTION: Ulvan lyase involved in ulvan degradation (PubMed:29875159).
CC Ulvan is the main polysaccharide component of the Ulvales (green
CC seaweed) cell wall. It is composed of disaccharide building blocks
CC comprising 3-sulfated rhamnose (Rha3S) linked to D-glucuronic acid
CC (GlcA), L-iduronic acid (IduA), or D-xylose (Xyl). Ulvan lyase
CC catalyzes the endolytic cleavage of the glycosidic bond between Rha3S
CC and the uronic acids GlcA or IduA, producing oligosaccharides that have
CC unsaturated 4-deoxy-L-threo-hex-4-enopyranosiduronic acid (deltaUA) at
CC the non-reducing end. This results eventually in the degradation of the
CC ulvan polysaccharide into deltaUA-Rha3S disaccharides and deltaUA-
CC Rha3S-Xyl-Rha3S tetrasaccharides (By similarity).
CC {ECO:0000250|UniProtKB:G8G2V6, ECO:0000269|PubMed:29875159}.
CC -!- COFACTOR:
CC Name=Ca(2+); Xref=ChEBI:CHEBI:29108;
CC Evidence={ECO:0000250|UniProtKB:T2KNC2};
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000255|PROSITE-
CC ProRule:PRU00303}; Lipid-anchor {ECO:0000255|PROSITE-ProRule:PRU00303}.
CC -!- SIMILARITY: Belongs to the polysaccharide lyase 28 family.
CC {ECO:0000305}.
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DR EMBL; JPJI01000012; KEZ94336.1; -; Genomic_DNA.
DR RefSeq; WP_036579443.1; NZ_PVNA01000009.1.
DR PDB; 6D2C; X-ray; 1.91 A; A/B=1-303.
DR PDB; 6D3U; X-ray; 2.21 A; A/B=1-303.
DR PDBsum; 6D2C; -.
DR PDBsum; 6D3U; -.
DR AlphaFoldDB; A0A084JZF2; -.
DR SMR; A0A084JZF2; -.
DR EnsemblBacteria; KEZ94336; KEZ94336; IL45_01530.
DR OrthoDB; 1851253at2; -.
DR Proteomes; UP000028531; Unassembled WGS sequence.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0016829; F:lyase activity; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
PE 1: Evidence at protein level;
KW 3D-structure; Cell membrane; Disulfide bond; Lipoprotein; Lyase; Membrane;
KW Metal-binding; Palmitate; Signal.
FT SIGNAL 1..22
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00303"
FT CHAIN 23..303
FT /note="Ulvan lyase NLR48"
FT /id="PRO_5001777815"
FT REGION 41..74
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 50..68
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 162
FT /note="Proton acceptor"
FT /evidence="ECO:0000305|PubMed:29875159"
FT ACT_SITE 281
FT /note="Proton donor/acceptor"
FT /evidence="ECO:0000305|PubMed:29875159"
FT BINDING 59
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_note="structural"
FT /evidence="ECO:0000269|PubMed:29875159"
FT BINDING 61
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_note="structural"
FT /evidence="ECO:0000269|PubMed:29875159"
FT BINDING 79
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_note="structural"
FT /evidence="ECO:0000269|PubMed:29875159"
FT BINDING 81
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_note="structural"
FT /evidence="ECO:0000269|PubMed:29875159"
FT BINDING 84
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_note="structural"
FT /evidence="ECO:0000269|PubMed:29875159"
FT BINDING 85
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_note="structural"
FT /evidence="ECO:0000269|PubMed:29875159"
FT BINDING 157
FT /ligand="substrate"
FT /evidence="ECO:0000269|PubMed:29875159"
FT BINDING 211..216
FT /ligand="substrate"
FT /evidence="ECO:0000269|PubMed:29875159"
FT BINDING 281..284
FT /ligand="substrate"
FT /evidence="ECO:0000269|PubMed:29875159"
FT SITE 160
FT /note="Neutralizes the sugar carboxylate group at subsite
FT +1"
FT /evidence="ECO:0000305|PubMed:29875159"
FT LIPID 23
FT /note="N-palmitoyl cysteine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00303"
FT LIPID 23
FT /note="S-diacylglycerol cysteine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00303"
FT DISULFID 55..82
FT /evidence="ECO:0007744|PDB:6D2C, ECO:0007744|PDB:6D3U"
FT MUTAGEN 117
FT /note="R->N: Abolishes catalytic activity."
FT /evidence="ECO:0000269|PubMed:29875159"
FT MUTAGEN 160
FT /note="Q->A: Abolishes catalytic activity."
FT /evidence="ECO:0000269|PubMed:29875159"
FT MUTAGEN 162
FT /note="K->M: Abolishes catalytic activity."
FT /evidence="ECO:0000269|PubMed:29875159"
FT MUTAGEN 216
FT /note="R->M: Abolishes catalytic activity."
FT /evidence="ECO:0000269|PubMed:29875159"
FT HELIX 57..59
FT /evidence="ECO:0007829|PDB:6D2C"
FT STRAND 75..80
FT /evidence="ECO:0007829|PDB:6D2C"
FT STRAND 87..91
FT /evidence="ECO:0007829|PDB:6D2C"
FT STRAND 94..102
FT /evidence="ECO:0007829|PDB:6D2C"
FT STRAND 117..121
FT /evidence="ECO:0007829|PDB:6D2C"
FT STRAND 133..144
FT /evidence="ECO:0007829|PDB:6D2C"
FT HELIX 151..153
FT /evidence="ECO:0007829|PDB:6D2C"
FT STRAND 156..162
FT /evidence="ECO:0007829|PDB:6D2C"
FT STRAND 175..187
FT /evidence="ECO:0007829|PDB:6D2C"
FT STRAND 189..191
FT /evidence="ECO:0007829|PDB:6D2C"
FT STRAND 193..207
FT /evidence="ECO:0007829|PDB:6D2C"
FT HELIX 212..215
FT /evidence="ECO:0007829|PDB:6D2C"
FT STRAND 216..225
FT /evidence="ECO:0007829|PDB:6D2C"
FT STRAND 230..240
FT /evidence="ECO:0007829|PDB:6D2C"
FT STRAND 244..246
FT /evidence="ECO:0007829|PDB:6D3U"
FT STRAND 248..256
FT /evidence="ECO:0007829|PDB:6D2C"
FT STRAND 259..261
FT /evidence="ECO:0007829|PDB:6D2C"
FT HELIX 268..270
FT /evidence="ECO:0007829|PDB:6D2C"
FT STRAND 274..281
FT /evidence="ECO:0007829|PDB:6D2C"
FT STRAND 284..300
FT /evidence="ECO:0007829|PDB:6D2C"
SQ SEQUENCE 303 AA; 33425 MW; F3523932BAA618A8 CRC64;
MRKLKYNTTR VILMIAFISL SACSSEDAMI EEEQVIPDPD PVAQTDEDTG PVVDCTNQGT
NPTRDTDIPN PRNIGDIDDR SCYANYSESS ILGKFWGIYN ITDGSNHMDA PNTLQPRIER
SLSRSQATGA GSYARFRGVL RILEVGDTGT FSSSGSYFMQ AKGKHTGGGG SPDPAICLYR
AHPVYGDDGN GNQVQVSFDI WREQINFRGG SGSAGRTEVF LKNVLKNEQI DIELEVGFRD
DPNNPGQTLH YADAKIGGEE FNWNIPEPER GIESGIRYGA YRVKGGRAQF RWANTSYTKD
EVN
