PLH12_FORAG
ID PLH12_FORAG Reviewed; 498 AA.
AC T2KN71;
DT 16-OCT-2019, integrated into UniProtKB/Swiss-Prot.
DT 13-NOV-2013, sequence version 1.
DT 03-AUG-2022, entry version 33.
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 P12 {ECO:0000303|PubMed:31285597};
DE Short=PUL H protein P12;
DE AltName: Full=Sulfatase family S1 subfamily 8 protein P12 {ECO:0000305};
DE Short=P12_S1_8 {ECO:0000303|PubMed:31285597};
DE Flags: Precursor;
GN ORFNames=BN863_22010;
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, 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).
CC {ECO:0000269|PubMed:31285597, ECO:0000305|PubMed:31285597}.
CC -!- COFACTOR:
CC Name=Ca(2+); Xref=ChEBI:CHEBI:29108;
CC Evidence={ECO:0000250|UniProtKB:P51688};
CC Note=Binds 1 Ca(2+) ion per subunit. {ECO:0000250|UniProtKB:P51688};
CC -!- SUBCELLULAR LOCATION: Periplasm {ECO:0000305|PubMed:31285597}.
CC -!- INDUCTION: By 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:P51688}.
CC -!- SIMILARITY: Belongs to the sulfatase family. {ECO:0000305}.
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DR EMBL; HG315671; CDF79913.1; -; Genomic_DNA.
DR AlphaFoldDB; T2KN71; -.
DR SMR; T2KN71; -.
DR STRING; 1347342.BN863_22010; -.
DR EnsemblBacteria; CDF79913; CDF79913; BN863_22010.
DR PATRIC; fig|1347342.6.peg.2208; -.
DR eggNOG; COG3119; Bacteria.
DR HOGENOM; CLU_006332_7_3_10; -.
DR OMA; MAYPMRM; -.
DR OrthoDB; 1067869at2; -.
DR Proteomes; UP000016160; Chromosome.
DR GO; GO:0042597; C:periplasmic space; 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; -; 1.
DR InterPro; IPR017850; Alkaline_phosphatase_core_sf.
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.
PE 1: Evidence at protein level;
KW Calcium; Hydrolase; Metal-binding; Periplasm; Reference proteome; Signal.
FT SIGNAL 1..22
FT /evidence="ECO:0000255"
FT CHAIN 23..498
FT /note="Ulvan-active sulfatase"
FT /id="PRO_0000448335"
FT ACT_SITE 95
FT /note="Nucleophile"
FT /evidence="ECO:0000250|UniProtKB:P51688"
FT BINDING 55
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250|UniProtKB:P51688"
FT BINDING 56
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250|UniProtKB:P51688"
FT BINDING 95
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /note="via 3-oxoalanine"
FT /evidence="ECO:0000250|UniProtKB:P51688"
FT BINDING 266
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250|UniProtKB:P51688"
FT BINDING 267
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250|UniProtKB:P51688"
FT MOD_RES 95
FT /note="3-oxoalanine (Cys)"
FT /evidence="ECO:0000250|UniProtKB:P51688"
SQ SEQUENCE 498 AA; 56798 MW; 0A13577358B89A00 CRC64;
MNSKKTGVII LGCIAFLHIA CSGDKKTQAQ DTSDSMLEKS SAISEKPNII FYLADDQDVY
DYGCYGNEKV HTPAVDALAK DGILFTNAFT AQAICAPSRS QLFTGKYPLK NGCFANHTGT
RSDIKSVTTH MKKLGYEVVL AGKSHVKPEN VYQWDREWEP VPKQGVPRDY IPLDSIAAYL
KNAKKPFCMF ITSKYPHGKY FDVEHPKASD IKFYPFNENK KTDKTFIKTK AGYYRSIEED
NTQLEEVLKL VDTYLTDNTL FIYSADHGVS GKFTVKDIGL KVPFVARWPK VIKPGSTSNQ
LIHYTDVLPT FMEIAGGKFP EDMDGNSFLP LLQGKDVEVN NYVYGVRTNQ NILNSEIFPS
RMIRDKRYKY IRNFNSIEVV EQNLTGKPNV NYFIERGAKA HKNEPFEELY DLQNDPFEQH
NLASNPDYKS IKEKLIKDMF SWMKAQGDIL SENMIGIPII TPKGNRGFKL DQDTPRRKIP
EARKNTLTKD DYIVIEHW
