PLH11_FORAG
ID PLH11_FORAG Reviewed; 479 AA.
AC T2KM04;
DT 16-OCT-2019, integrated into UniProtKB/Swiss-Prot.
DT 13-NOV-2013, sequence version 1.
DT 03-AUG-2022, entry version 36.
DE RecName: Full=Ulvan-active sulfatase {ECO:0000305};
DE EC=3.1.6.- {ECO:0000269|PubMed:31285597};
DE AltName: Full=Iduronate 2-sulfatase {ECO:0000303|PubMed:31285597};
DE AltName: Full=Polysaccharide utilization locus H protein P11 {ECO:0000303|PubMed:31285597};
DE Short=PUL H protein P11;
DE AltName: Full=Sulfatase family S1 subfamily 7 protein P11 {ECO:0000305};
DE Short=P11_S1_7 {ECO:0000303|PubMed:31285597};
DE Flags: Precursor;
GN ORFNames=BN863_22000;
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 FUNCTION, CATALYTIC ACTIVITY, AND SUBCELLULAR LOCATION.
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).
CC {ECO:0000269|PubMed:31285597, ECO:0000305|PubMed:31285597}.
CC -!- COFACTOR:
CC Name=Ca(2+); Xref=ChEBI:CHEBI:29108;
CC Evidence={ECO:0000250|UniProtKB:T2KPK5};
CC Note=Binds 1 Ca(2+) ion per subunit. {ECO:0000250|UniProtKB:T2KPK5};
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000255|PROSITE-
CC ProRule:PRU00303}; Lipid-anchor {ECO:0000255|PROSITE-ProRule:PRU00303};
CC Periplasmic side {ECO:0000305|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}.
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DR EMBL; HG315671; CDF79912.1; -; Genomic_DNA.
DR RefSeq; WP_038530501.1; NZ_HG315671.1.
DR AlphaFoldDB; T2KM04; -.
DR SMR; T2KM04; -.
DR STRING; 1347342.BN863_22000; -.
DR EnsemblBacteria; CDF79912; CDF79912; BN863_22000.
DR PATRIC; fig|1347342.6.peg.2207; -.
DR eggNOG; COG3119; Bacteria.
DR HOGENOM; CLU_006332_9_0_10; -.
DR OMA; PHLDAFA; -.
DR OrthoDB; 1067869at2; -.
DR Proteomes; UP000016160; Chromosome.
DR GO; GO:0005886; C:plasma membrane; 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; IPR000917; Sulfatase_N.
DR Pfam; PF00884; Sulfatase; 1.
DR SUPFAM; SSF53649; SSF53649; 1.
DR PROSITE; PS51257; PROKAR_LIPOPROTEIN; 1.
PE 1: Evidence at protein level;
KW Calcium; Cell membrane; Hydrolase; Lipoprotein; Membrane; Metal-binding;
KW Palmitate; Reference proteome; Signal.
FT SIGNAL 1..17
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00303"
FT CHAIN 18..479
FT /note="Ulvan-active sulfatase"
FT /id="PRO_0000448334"
FT ACT_SITE 81
FT /note="Nucleophile"
FT /evidence="ECO:0000250|UniProtKB:P15289"
FT ACT_SITE 135
FT /evidence="ECO:0000250|UniProtKB:P15289"
FT BINDING 42
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250|UniProtKB:T2KPK5"
FT BINDING 43
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250|UniProtKB:T2KPK5"
FT BINDING 81
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /note="via 3-oxoalanine"
FT /evidence="ECO:0000250|UniProtKB:T2KPK5"
FT BINDING 321
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250|UniProtKB:T2KPK5"
FT BINDING 322
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250|UniProtKB:T2KPK5"
FT MOD_RES 81
FT /note="3-oxoalanine (Cys)"
FT /evidence="ECO:0000250|UniProtKB:P15289"
FT LIPID 18
FT /note="N-palmitoyl cysteine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00303"
FT LIPID 18
FT /note="S-diacylglycerol cysteine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00303"
SQ SEQUENCE 479 AA; 54229 MW; 6EBC8D3897426D23 CRC64;
MKRLFIYTLG LVLTVSACKE KQQKTTVTQE QKPMNVLFIA VDDLRPELNF YGASHIKSPN
LDKLASQSLV FNRSYCNVPV CGASRASLLT GTRPTRHRFF DYKARADTDA PEAVSLPMTF
KQNGYTTISN GKIYHNIDDD SLAWNTIWFP KGNIRNYQLE KNILKNADAN LAMGGASAFE
NADVNDEAYF DGEIARKGIA DLQHLKKSKQ PFFLAMGFMK PHLPFNAPKK YWDLYDREQI
KLPETYVQPE STPKKAFPNY GELRNYGNIP KKGDLPEDLA KELIHGYYAC VSYVDAQIGL
VLDALEKTGL ADNTIVVLWG DHGWNLGDHK LWCKHVNFET ALSAPLVVKV PGKTNGERSN
AITEFIDIYP TLCELTGLEV PDTAEGVSFL PLINGEKQIK NWAVSKFKDG VTLVKDDLFY
TEWTDDDGVA YERMLFDHKT DSLELDNLAE KPEFQELVKQ LALELRQKWG KDFLTQNTK
