PLH14_FORAG
ID PLH14_FORAG Reviewed; 507 AA.
AC T2KMG4;
DT 16-OCT-2019, integrated into UniProtKB/Swiss-Prot.
DT 16-OCT-2019, sequence version 2.
DT 03-AUG-2022, entry version 31.
DE RecName: Full=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 P14 {ECO:0000303|PubMed:31285597};
DE Short=PUL H protein P14;
DE AltName: Full=Sulfatase family S1 subfamily 7 protein P14 {ECO:0000305};
DE Short=P14_S1_7 {ECO:0000303|PubMed:31285597};
DE Flags: Precursor;
GN ORFNames=BN863_22030 {ECO:0000312|EMBL:CDF79915.1};
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 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 that may be involved in ulvan degradation
CC (PubMed:31285597). 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 (Probable). Has no activity on different ulvan polymers
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:0000250|UniProtKB:T2KPK5};
CC Note=Binds 1 Ca(2+) ion per subunit. {ECO:0000250|UniProtKB:T2KPK5};
CC -!- SUBCELLULAR LOCATION: Periplasm {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}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CDF79915.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305|Ref.2};
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DR EMBL; HG315671; CDF79915.1; ALT_INIT; Genomic_DNA.
DR RefSeq; WP_051774709.1; NZ_HG315671.1.
DR AlphaFoldDB; T2KMG4; -.
DR SMR; T2KMG4; -.
DR STRING; 1347342.BN863_22030; -.
DR EnsemblBacteria; CDF79915; CDF79915; BN863_22030.
DR PATRIC; fig|1347342.6.peg.2210; -.
DR eggNOG; COG3119; Bacteria.
DR HOGENOM; CLU_006332_9_0_10; -.
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; PS00523; SULFATASE_1; 1.
DR PROSITE; PS00149; SULFATASE_2; 1.
PE 1: Evidence at protein level;
KW Calcium; Hydrolase; Metal-binding; Periplasm; Reference proteome; Signal.
FT SIGNAL 1..18
FT /evidence="ECO:0000255"
FT CHAIN 19..507
FT /note="Sulfatase"
FT /id="PRO_0000448336"
FT ACT_SITE 79
FT /note="Nucleophile"
FT /evidence="ECO:0000250|UniProtKB:P15289"
FT ACT_SITE 139
FT /evidence="ECO:0000250|UniProtKB:P15289"
FT BINDING 39
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250|UniProtKB:T2KPK5"
FT BINDING 40
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250|UniProtKB:T2KPK5"
FT BINDING 79
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /note="via 3-oxoalanine"
FT /evidence="ECO:0000250|UniProtKB:T2KPK5"
FT BINDING 325
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250|UniProtKB:T2KPK5"
FT BINDING 326
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250|UniProtKB:T2KPK5"
FT MOD_RES 79
FT /note="3-oxoalanine (Cys)"
FT /evidence="ECO:0000250|UniProtKB:P15289"
SQ SEQUENCE 507 AA; 57440 MW; 47EFEBFB8F2BF938 CRC64;
MKTRYFLLLG ICMLSCRTDE KKQVQKEVDK PNVLFIAVDD LNNMISPIAN FSNIQTPNFD
RLAAMGVTFT DAHCPAPLCG PSRSAIMTGL RPSTTGIYGM TPDNKIRRDD NEATKDIIFL
PEYFKKNGYH SMGIGKLFHN YAPDGMFDEG GGRVKGFGPF PEKRFVWDGF GTSKSRKGQY
GRTNTDWGAF PESDTLMPDH QAVNWVLERF NKNYKQPFFL ALGFQRPHVP LYVPQKWFDL
YPLESIQTPP YQSDDLNDIP PVGLKINDLP MMPSTEWAIN SGEWKKIIQA YLACVSFVDY
ELGRVLDALK NSPYAKNTII VLWSDHGYRL GEKGTFAKHA LWESATKAPL FFAGPNLPKG
KKIDAPVEML SIYPTLLELS GLQAYARNEA KSLVRMMQKN EGLKDTYAIT TYGKNNHAVK
VDGYRYIQYE DGTEEFYDNA SDPNEWINEA NNFKFKSKIE ALKALLPKTN ATWDAESNYT
FQPYFVEQKT RGNVNAAKAV KVIGAER
