UL28A_NONUL
ID UL28A_NONUL Reviewed; 534 AA.
AC G8G2V6;
DT 16-OCT-2019, integrated into UniProtKB/Swiss-Prot.
DT 25-JAN-2012, sequence version 1.
DT 03-AUG-2022, entry version 31.
DE RecName: Full=Ulvan lyase NLR42 {ECO:0000305};
DE EC=4.2.2.- {ECO:0000269|PubMed:22009751};
DE Flags: Precursor;
GN ORFNames=IL45_01510, PLR_42 {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 [GENOMIC DNA], PROTEIN SEQUENCE OF 58-66; 72-87;
RP 135-142; 149-169; 174-193; 199-215; 234-242; 249-255; 261-274; 309-322 AND
RP 423-439, FUNCTION, CATALYTIC ACTIVITY, AND BIOPHYSICOCHEMICAL PROPERTIES.
RC STRAIN=DSM 22727 / CIP 110082 / PLR;
RX PubMed=22009751; DOI=10.1074/jbc.m111.271825;
RA Nyvall Collen P., Sassi J.F., Rogniaux H., Marfaing H., Helbert W.;
RT "Ulvan lyases isolated from the Flavobacteria Persicivirga ulvanivorans are
RT the first members of a new polysaccharide lyase family.";
RL J. Biol. Chem. 286:42063-42071(2011).
RN [2]
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 [3]
RP FUNCTION, DOMAIN, AND SUBCELLULAR LOCATION.
RX PubMed=28327560; DOI=10.1038/srep44115;
RA Melcher R.L., Neumann M., Fuenzalida Werner J.P., Groehn F.,
RA Moerschbacher B.M.;
RT "Revised domain structure of ulvan lyase and characterization of the first
RT ulvan binding domain.";
RL Sci. Rep. 7:44115-44115(2017).
CC -!- FUNCTION: Ulvan lyase involved in ulvan degradation (PubMed:22009751,
CC PubMed:28327560). Ulvan is the main polysaccharide component of the
CC Ulvales (green seaweed) cell wall. It is composed of disaccharide
CC building blocks comprising 3-sulfated rhamnose (Rha3S) linked to D-
CC glucuronic acid (GlcA), L-iduronic acid (IduA), or D-xylose (Xyl).
CC Ulvan lyase catalyzes the endolytic cleavage of the glycosidic bond
CC between Rha3S and the uronic acids GlcA or IduA, producing
CC oligosaccharides that have unsaturated 4-deoxy-L-threo-hex-4-
CC enopyranosiduronic acid (deltaUA) at the non-reducing end. This results
CC eventually in the degradation of the ulvan polysaccharide into deltaUA-
CC Rha3S disaccharides and deltaUA-Rha3S-Xyl-Rha3S tetrasaccharides
CC (PubMed:22009751). {ECO:0000269|PubMed:22009751,
CC ECO:0000269|PubMed:28327560}.
CC -!- COFACTOR:
CC Name=Ca(2+); Xref=ChEBI:CHEBI:29108;
CC Evidence={ECO:0000250|UniProtKB:T2KNC2};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=0.0051 mg/ml for ulvan {ECO:0000269|PubMed:22009751};
CC pH dependence:
CC Optimum pH is 9. {ECO:0000269|PubMed:22009751};
CC Temperature dependence:
CC Optimum temperature is 50 degrees Celsius.
CC {ECO:0000269|PubMed:22009751};
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000305|PubMed:28327560}.
CC Note=Secreted via the type IX secretion system (T9SS).
CC {ECO:0000305|PubMed:28327560}.
CC -!- DOMAIN: The ulvan-binding domain binds strongly to ulvan, it does not
CC bind other polymers like alginate, heparin, dextran sulfate or iota
CC carrageenan. Presumably it serves to anchor the enzyme at the
CC substrate, thus improving catalysis. Notably, the catalytic domain
CC alone is more active than the full-length enzyme with the binding
CC domain attached. Possibly, the ulvan-binding domain helps the enzyme to
CC act on ulvan in its insoluble form embedded in the algal cell wall.
CC {ECO:0000269|PubMed:28327560}.
CC -!- SIMILARITY: Belongs to the polysaccharide lyase 28 family.
CC {ECO:0000305}.
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DR EMBL; JN104480; AEN28574.1; -; Genomic_DNA.
DR EMBL; JPJI01000012; KEZ94332.1; -; Genomic_DNA.
DR AlphaFoldDB; G8G2V6; -.
DR SMR; G8G2V6; -.
DR EnsemblBacteria; KEZ94332; KEZ94332; IL45_01510.
DR OrthoDB; 832271at2; -.
DR BioCyc; MetaCyc:MON-19226; -.
DR Proteomes; UP000028531; Unassembled WGS sequence.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0016829; F:lyase activity; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR InterPro; IPR035992; Ricin_B-like_lectins.
DR InterPro; IPR026444; Secre_tail.
DR Pfam; PF18962; Por_Secre_tail; 1.
DR SUPFAM; SSF50370; SSF50370; 1.
DR TIGRFAMs; TIGR04183; Por_Secre_tail; 1.
PE 1: Evidence at protein level;
KW Calcium; Direct protein sequencing; Disulfide bond; Lyase; Metal-binding;
KW Secreted; Signal.
FT SIGNAL 1..47
FT /evidence="ECO:0000255"
FT CHAIN 48..449
FT /note="Ulvan lyase NLR42"
FT /id="PRO_0000448329"
FT PROPEP 450..534
FT /note="Removed by the type IX secretion system (T9SS)"
FT /evidence="ECO:0000255, ECO:0000305|PubMed:28327560"
FT /id="PRO_0000448330"
FT REGION 316..449
FT /note="Ulvan-binding domain"
FT /evidence="ECO:0000269|PubMed:28327560"
FT ACT_SITE 169
FT /note="Proton acceptor"
FT /evidence="ECO:0000250|UniProtKB:A0A084JZF2"
FT ACT_SITE 288
FT /note="Proton donor/acceptor"
FT /evidence="ECO:0000250|UniProtKB:A0A084JZF2"
FT BINDING 63
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_note="structural"
FT /evidence="ECO:0000250|UniProtKB:A0A084JZF2"
FT BINDING 68
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_note="structural"
FT /evidence="ECO:0000250|UniProtKB:A0A084JZF2"
FT BINDING 86
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_note="structural"
FT /evidence="ECO:0000250|UniProtKB:A0A084JZF2"
FT BINDING 88
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_note="structural"
FT /evidence="ECO:0000250|UniProtKB:A0A084JZF2"
FT BINDING 91
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_note="structural"
FT /evidence="ECO:0000250|UniProtKB:A0A084JZF2"
FT BINDING 92
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_note="structural"
FT /evidence="ECO:0000250|UniProtKB:A0A084JZF2"
FT BINDING 164
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:A0A084JZF2"
FT BINDING 218..223
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:A0A084JZF2"
FT BINDING 288..291
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:A0A084JZF2"
FT SITE 167
FT /note="Neutralizes the sugar carboxylate group at subsite
FT +1"
FT /evidence="ECO:0000250|UniProtKB:A0A084JZF2"
FT DISULFID 59..89
FT /evidence="ECO:0000250|UniProtKB:A0A084JZF2"
SQ SEQUENCE 534 AA; 58956 MW; 45A1C9872B2D5646 CRC64;
MVFFKDLFIF KSLIKGSLYS GHMKKKLLNY LPLFALMLFT VSMMAQTAPD EDTNSSIACP
SSGVFQNNTT RDVDIANPDN VGTVDDRTCY ADYYETSVYG ETWGAYNITF NSNHWDAPNT
LQPRIERSLS RSQETGVGSY ARFTGTLRIL EVGNTGTFGS TGSYLMQAKG KHTGGGGSND
PAICLYLARP VYGPDANGNQ VQVSFDIWRE QINFRGGSGA AGRTEVFLRN VLKDEIIDIE
LEVGFRQDPN DPNLKIHYSD AIIGGQVFNW NIPEPERGRE SGIRYGVYRV KGGRAQMRWA
NTTYQKVEVV DNSTIPAADI YRIKNVETGE YLTSSGSSII ASTSGTGSDK EWEIISAGSG
SSYVNIDSQV RGIIRFTGGS SNPGLVSTNF SPPNTDTDKV WTVIDNNDGT VSFETRNLGR
FLYHDTNNMI THSANIDDRS KWNLESTTLS VDSQQIASVG VYPNPTVDGF TISLDNISAE
KVQIFNLLGM LVYEQKTNES SIHIDNMDNF DSGMYIISVT ANDNKVYQTK LIVN
