PLH18_FORAG
ID PLH18_FORAG Reviewed; 488 AA.
AC T2KPK5;
DT 16-OCT-2019, integrated into UniProtKB/Swiss-Prot.
DT 16-OCT-2019, sequence version 2.
DT 03-AUG-2022, entry version 38.
DE RecName: Full=Ulvan-active sulfatase {ECO:0000305};
DE EC=3.1.6.- {ECO:0000269|PubMed:31285597};
DE AltName: Full=Arylsulfatase {ECO:0000303|PubMed:31285597};
DE AltName: Full=Polysaccharide utilization locus H protein P18 {ECO:0000303|PubMed:31285597};
DE Short=PUL H protein P18;
DE AltName: Full=Sulfatase family S1 subfamily 7 protein P18 {ECO:0000305};
DE Short=P18_S1_7 {ECO:0000303|PubMed:31285597};
DE Flags: Precursor;
GN ORFNames=BN863_22070;
OS Formosa agariphila (strain DSM 15362 / KCTC 12365 / LMG 23005 / KMM 3901 /
OS M-2Alg 35-1).
OC Bacteria; Bacteroidetes; Flavobacteriia; Flavobacteriales;
OC Flavobacteriaceae; Formosa.
OX NCBI_TaxID=1347342;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 15362 / KCTC 12365 / LMG 23005 / KMM 3901 / M-2Alg 35-1;
RX PubMed=23995932; DOI=10.1128/aem.01937-13;
RA Mann A.J., Hahnke R.L., Huang S., Werner J., Xing P., Barbeyron T.,
RA Huettel B., Stueber K., Reinhardt R., Harder J., Gloeckner F.O.,
RA Amann R.I., Teeling H.;
RT "The genome of the alga-associated marine flavobacterium Formosa agariphila
RT KMM 3901T reveals a broad potential for degradation of algal
RT polysaccharides.";
RL Appl. Environ. Microbiol. 79:6813-6822(2013).
RN [2]
RP REVISION OF GENE MODEL.
RX DOI=10.1016/j.algal.2017.09.025;
RA Salinas A., French C.E.;
RT "The enzymatic ulvan depolymerisation system from the alga-associated
RT marine flavobacterium Formosa agariphila.";
RL Algal Res. 27:335-344(2017).
RN [3]
RP X-RAY CRYSTALLOGRAPHY (1.23 ANGSTROMS) IN COMPLEX WITH CALCIUM ION,
RP FUNCTION, CATALYTIC ACTIVITY, SUBCELLULAR LOCATION, AND INDUCTION.
RX PubMed=31285597; DOI=10.1038/s41589-019-0311-9;
RA Reisky L., Prechoux A., Zuehlke M.K., Baeumgen M., Robb C.S., Gerlach N.,
RA Roret T., Stanetty C., Larocque R., Michel G., Song T., Markert S.,
RA Unfried F., Mihovilovic M.D., Trautwein-Schult A., Becher D., Schweder T.,
RA Bornscheuer U.T., Hehemann J.H.;
RT "A marine bacterial enzymatic cascade degrades the algal polysaccharide
RT ulvan.";
RL Nat. Chem. Biol. 15:803-812(2019).
CC -!- FUNCTION: Sulfatase involved in ulvan degradation (PubMed:31285597).
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) (Probable). The
CC sulfatase is most active on ulvan polymers, particularly on xylose-rich
CC ulvan. It can desulfate oligosaccharides containing the motif Rha3S-
CC Xyl2S-Rha3S and thus likely proceeds in an endolytic mode of action,
CC removing sulfates from xylose residues in periplasmic oligosaccharides
CC (PubMed:31285597). {ECO:0000269|PubMed:31285597,
CC ECO:0000305|PubMed:31285597}.
CC -!- COFACTOR:
CC Name=Ca(2+); Xref=ChEBI:CHEBI:29108;
CC Evidence={ECO:0000269|PubMed:31285597};
CC Note=Binds 1 Ca(2+) ion per subunit. {ECO:0000269|PubMed:31285597};
CC -!- SUBCELLULAR LOCATION: Periplasm {ECO:0000305|PubMed:31285597}.
CC -!- INDUCTION: By ulvan and rhamnose. {ECO:0000269|PubMed:31285597}.
CC -!- PTM: The conversion to 3-oxoalanine (also known as C-formylglycine,
CC FGly), of a serine or cysteine residue in prokaryotes and of a cysteine
CC residue in eukaryotes, is critical for catalytic activity. This post-
CC translational modification is severely defective in multiple sulfatase
CC deficiency (MSD). {ECO:0000250|UniProtKB:P15289}.
CC -!- SIMILARITY: Belongs to the sulfatase family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CDF79919.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305|Ref.2};
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DR EMBL; HG315671; CDF79919.1; ALT_INIT; Genomic_DNA.
DR PDB; 6HHM; X-ray; 1.23 A; A=28-486.
DR PDBsum; 6HHM; -.
DR AlphaFoldDB; T2KPK5; -.
DR SMR; T2KPK5; -.
DR STRING; 1347342.BN863_22070; -.
DR EnsemblBacteria; CDF79919; CDF79919; BN863_22070.
DR PATRIC; fig|1347342.6.peg.2214; -.
DR eggNOG; COG3119; Bacteria.
DR HOGENOM; CLU_006332_9_0_10; -.
DR OrthoDB; 1067869at2; -.
DR Proteomes; UP000016160; Chromosome.
DR GO; GO:0042597; C:periplasmic space; IEA:UniProtKB-SubCell.
DR GO; GO:0004423; F:iduronate-2-sulfatase activity; IEA:InterPro.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR CDD; cd16030; iduronate-2-sulfatase; 1.
DR Gene3D; 3.40.720.10; -; 1.
DR InterPro; IPR017850; Alkaline_phosphatase_core_sf.
DR InterPro; IPR035874; IDS.
DR InterPro; IPR024607; Sulfatase_CS.
DR InterPro; IPR000917; Sulfatase_N.
DR Pfam; PF00884; Sulfatase; 1.
DR SUPFAM; SSF53649; SSF53649; 1.
DR PROSITE; PS00149; SULFATASE_2; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Calcium; Hydrolase; Metal-binding; Periplasm;
KW Reference proteome; Signal.
FT SIGNAL 1..25
FT /evidence="ECO:0000255"
FT CHAIN 26..488
FT /note="Ulvan-active sulfatase"
FT /id="PRO_5004602763"
FT ACT_SITE 77
FT /note="Nucleophile"
FT /evidence="ECO:0000250|UniProtKB:P15289"
FT ACT_SITE 131
FT /evidence="ECO:0000250|UniProtKB:P15289"
FT BINDING 38
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000269|PubMed:31285597"
FT BINDING 39
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000269|PubMed:31285597"
FT BINDING 77
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /note="via 3-oxoalanine"
FT /evidence="ECO:0000269|PubMed:31285597"
FT BINDING 315
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000269|PubMed:31285597"
FT BINDING 316
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000269|PubMed:31285597"
FT MOD_RES 77
FT /note="3-oxoalanine (Cys)"
FT /evidence="ECO:0000250|UniProtKB:P15289"
FT STRAND 31..37
FT /evidence="ECO:0007829|PDB:6HHM"
FT HELIX 45..47
FT /evidence="ECO:0007829|PDB:6HHM"
FT HELIX 55..62
FT /evidence="ECO:0007829|PDB:6HHM"
FT STRAND 64..71
FT /evidence="ECO:0007829|PDB:6HHM"
FT STRAND 73..76
FT /evidence="ECO:0007829|PDB:6HHM"
FT HELIX 77..86
FT /evidence="ECO:0007829|PDB:6HHM"
FT HELIX 90..93
FT /evidence="ECO:0007829|PDB:6HHM"
FT STRAND 97..99
FT /evidence="ECO:0007829|PDB:6HHM"
FT HELIX 102..104
FT /evidence="ECO:0007829|PDB:6HHM"
FT STRAND 107..109
FT /evidence="ECO:0007829|PDB:6HHM"
FT HELIX 112..118
FT /evidence="ECO:0007829|PDB:6HHM"
FT STRAND 122..132
FT /evidence="ECO:0007829|PDB:6HHM"
FT TURN 133..136
FT /evidence="ECO:0007829|PDB:6HHM"
FT HELIX 137..139
FT /evidence="ECO:0007829|PDB:6HHM"
FT STRAND 141..144
FT /evidence="ECO:0007829|PDB:6HHM"
FT HELIX 154..164
FT /evidence="ECO:0007829|PDB:6HHM"
FT TURN 165..167
FT /evidence="ECO:0007829|PDB:6HHM"
FT STRAND 173..176
FT /evidence="ECO:0007829|PDB:6HHM"
FT HELIX 182..184
FT /evidence="ECO:0007829|PDB:6HHM"
FT HELIX 186..200
FT /evidence="ECO:0007829|PDB:6HHM"
FT TURN 201..203
FT /evidence="ECO:0007829|PDB:6HHM"
FT STRAND 206..212
FT /evidence="ECO:0007829|PDB:6HHM"
FT STRAND 216..220
FT /evidence="ECO:0007829|PDB:6HHM"
FT HELIX 223..226
FT /evidence="ECO:0007829|PDB:6HHM"
FT HELIX 231..233
FT /evidence="ECO:0007829|PDB:6HHM"
FT HELIX 254..257
FT /evidence="ECO:0007829|PDB:6HHM"
FT HELIX 271..301
FT /evidence="ECO:0007829|PDB:6HHM"
FT HELIX 305..307
FT /evidence="ECO:0007829|PDB:6HHM"
FT STRAND 308..315
FT /evidence="ECO:0007829|PDB:6HHM"
FT STRAND 319..321
FT /evidence="ECO:0007829|PDB:6HHM"
FT HELIX 322..324
FT /evidence="ECO:0007829|PDB:6HHM"
FT HELIX 333..336
FT /evidence="ECO:0007829|PDB:6HHM"
FT STRAND 340..343
FT /evidence="ECO:0007829|PDB:6HHM"
FT STRAND 354..357
FT /evidence="ECO:0007829|PDB:6HHM"
FT HELIX 363..365
FT /evidence="ECO:0007829|PDB:6HHM"
FT HELIX 366..373
FT /evidence="ECO:0007829|PDB:6HHM"
FT HELIX 387..391
FT /evidence="ECO:0007829|PDB:6HHM"
FT STRAND 401..407
FT /evidence="ECO:0007829|PDB:6HHM"
FT TURN 408..410
FT /evidence="ECO:0007829|PDB:6HHM"
FT STRAND 411..417
FT /evidence="ECO:0007829|PDB:6HHM"
FT STRAND 419..428
FT /evidence="ECO:0007829|PDB:6HHM"
FT TURN 429..431
FT /evidence="ECO:0007829|PDB:6HHM"
FT STRAND 434..441
FT /evidence="ECO:0007829|PDB:6HHM"
FT HELIX 456..458
FT /evidence="ECO:0007829|PDB:6HHM"
FT HELIX 459..472
FT /evidence="ECO:0007829|PDB:6HHM"
FT STRAND 475..477
FT /evidence="ECO:0007829|PDB:6HHM"
SQ SEQUENCE 488 AA; 55412 MW; 7C34178481ADE052 CRC64;
MTNMNLKHKI FIMLLLVFCS SKIIAQQSQP NVLVFYVDDL RAELGCYGSK TAITPNIDKL
ATEGVQFNKA YVQQAICAPS RMSTLTGLRP ETLGIYSIFT PLRSVHKDVV SVPQLFKENG
YKTVSIGKVY HHGTDDKNQW TNYFTKEPNT YNKPENIALL EQFKKEGKKA NGPAFENADV
ADEAYKDGRA AKYAVETLKK LKNDKFIMFV GFSKPHLPFN APKKYWDLYD KNNFEIPERK
KPENMYRLAL TNWGELKGYH GIPNDVEYLD DNLTRDLIHG YHASISYVDA QVGKVMEALE
ALGLRKNTTV IFMSDHGYKI GEYGAWCKHS NEEIDVRVPL IVSRETSYKG RVAGKTSDAL
VENVDIFPTL VELCGLEGPK TDGKSILQVI DRPNTPWDQV ATAVYARGKN IMGCTATDGE
WRYTEWRDAK TQDILGAELY EHKNSLLSFK NLSGNTKYKK EEARMKGLLE TQFPRNQGPF
LQHDTPRN
