PLH13_FORAG
ID PLH13_FORAG Reviewed; 553 AA.
AC T2KPJ9;
DT 16-OCT-2019, integrated into UniProtKB/Swiss-Prot.
DT 13-NOV-2013, sequence version 1.
DT 03-AUG-2022, entry version 32.
DE RecName: Full=Sulfatase {ECO:0000305};
DE EC=3.1.6.- {ECO:0000305|PubMed:31285597};
DE AltName: Full=Arylsulfatase {ECO:0000303|PubMed:31285597};
DE AltName: Full=Polysaccharide utilization locus H protein P13 {ECO:0000303|PubMed:31285597};
DE Short=PUL H protein P13;
DE AltName: Full=Sulfatase family S1 subfamily 16 protein P13 {ECO:0000305};
DE Short=P13_S1_16 {ECO:0000303|PubMed:31285597};
DE Flags: Precursor;
GN ORFNames=BN863_22020;
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, 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 that may be involved in ulvan degradation
CC (Probable). Ulvan is the main polysaccharide component of the Ulvales
CC (green seaweed) cell wall. It is composed of disaccharide building
CC blocks comprising 3-sulfated rhamnose (Rha3S) linked to D-glucuronic
CC acid (GlcA), L-iduronic acid (IduA), or D-xylose (Xyl) (Probable).
CC {ECO:0000305|PubMed:31285597}.
CC -!- COFACTOR:
CC Name=Ca(2+); Xref=ChEBI:CHEBI:29108;
CC Evidence={ECO:0000250|UniProtKB:P15289};
CC Note=Binds 1 Ca(2+) ion per subunit. {ECO:0000250|UniProtKB:P15289};
CC -!- SUBCELLULAR LOCATION: Secreted {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}.
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DR EMBL; HG315671; CDF79914.1; -; Genomic_DNA.
DR AlphaFoldDB; T2KPJ9; -.
DR SMR; T2KPJ9; -.
DR STRING; 1347342.BN863_22020; -.
DR EnsemblBacteria; CDF79914; CDF79914; BN863_22020.
DR PATRIC; fig|1347342.6.peg.2209; -.
DR eggNOG; COG3119; Bacteria.
DR HOGENOM; CLU_006332_10_4_10; -.
DR OMA; WHFPIYL; -.
DR Proteomes; UP000016160; Chromosome.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0008484; F:sulfuric ester hydrolase activity; IEA:InterPro.
DR Gene3D; 3.40.720.10; -; 2.
DR InterPro; IPR017850; Alkaline_phosphatase_core_sf.
DR InterPro; IPR032506; DUF4976.
DR InterPro; IPR000917; Sulfatase_N.
DR Pfam; PF16347; DUF4976; 1.
DR Pfam; PF00884; Sulfatase; 1.
DR SUPFAM; SSF53649; SSF53649; 1.
PE 3: Inferred from homology;
KW Calcium; Hydrolase; Metal-binding; Reference proteome; Secreted; Signal.
FT SIGNAL 1..25
FT /evidence="ECO:0000255"
FT CHAIN 26..553
FT /note="Sulfatase"
FT /id="PRO_5004591149"
FT ACT_SITE 88
FT /note="Nucleophile"
FT /evidence="ECO:0000250|UniProtKB:P15289"
FT ACT_SITE 159
FT /evidence="ECO:0000250|UniProtKB:P15289"
FT BINDING 43
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250|UniProtKB:P15289"
FT BINDING 44
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250|UniProtKB:P15289"
FT BINDING 88
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /note="via 3-oxoalanine"
FT /evidence="ECO:0000250|UniProtKB:P15289"
FT BINDING 350
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250|UniProtKB:P15289"
FT BINDING 351
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250|UniProtKB:P15289"
FT MOD_RES 88
FT /note="3-oxoalanine (Cys)"
FT /evidence="ECO:0000250|UniProtKB:P15289"
SQ SEQUENCE 553 AA; 62087 MW; C4ECF2DA9AD9AC97 CRC64;
MTSEMKKFSK IVLFGLLISP LLASSQTKKD ANQKPNIILI MADDLGWTDL SSPNTSLGYG
SKYYESPNID RLAQQGKSFA YAYTQQNCQP TRAALLSGQY ATGAQNGVYN VGSLKRASKG
VVTPIMPHNQ NNYLQEDCVS MFETLKTAGY HTAWFGKFHA IKLGKQAESY MGVDYNVALH
KETSATVNGV KVKNEFFAQN DDAKGWMFEI DNLKPYAQPY DAAYLQKVLE PIKNGNNPWL
LEGTPKHLTD ALGDAVVGYI KDRSKADSPF FAYIPFHAVH VSILPRLDLE AKYKAKKSLD
PRHTQADYAA FVELLDQTVG RVLNALEDPN GDGNKADGIA ENTMVIFYSD NGGFMGPTNN
SPLRLRKGTY YEGGVRVPLI FKYPGVITPN SVNTTQEVHT IDFYPTLAEI AGAKLPSPKV
QEMDGKSIAS VLREESQVRD DKNELFWHFP GYMDVRNMPQ SVIHYRHSDN QHYKLFYRYE
DESFELYNLS NDLGETTNLL AENPSQQTLD LALKMNNKLR AWLIKNNAPT GIWAKNCEKV
PYPKKDAVKK YIK
