PLH32_FORAG
ID PLH32_FORAG Reviewed; 596 AA.
AC T2KN90;
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=Polysaccharide utilization locus H protein P32 {ECO:0000303|PubMed:31285597};
DE Short=PUL H protein P32;
DE AltName: Full=Sulfatase family S1 subfamily 8 protein P32 {ECO:0000305};
DE Short=P32_S1_8 {ECO:0000303|PubMed:31285597};
DE Flags: Precursor;
GN ORFNames=BN863_22210;
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). The
CC sulfatase desulfates Xyl2S-Rha3S, product of the degradation of ulvan
CC by endo-acting alpha-1,4-L-rhamnosidase, to Xyl-Rha3S
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: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.
CC {ECO:0000250|UniProtKB:P51688}.
CC -!- SIMILARITY: Belongs to the sulfatase family. {ECO:0000305}.
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DR EMBL; HG315671; CDF79933.1; -; Genomic_DNA.
DR RefSeq; WP_051774719.1; NZ_HG315671.1.
DR AlphaFoldDB; T2KN90; -.
DR SMR; T2KN90; -.
DR STRING; 1347342.BN863_22210; -.
DR EnsemblBacteria; CDF79933; CDF79933; BN863_22210.
DR PATRIC; fig|1347342.6.peg.2228; -.
DR eggNOG; COG3119; Bacteria.
DR HOGENOM; CLU_006332_7_3_10; -.
DR OMA; IIFFYGD; -.
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; IPR000917; Sulfatase_N.
DR Pfam; PF00884; Sulfatase; 2.
DR SUPFAM; SSF53649; SSF53649; 1.
PE 1: Evidence at protein level;
KW Calcium; Hydrolase; Metal-binding; Periplasm; Reference proteome; Signal.
FT SIGNAL 1..27
FT /evidence="ECO:0000255"
FT CHAIN 28..596
FT /note="Ulvan-active sulfatase"
FT /id="PRO_0000448338"
FT ACT_SITE 97
FT /note="Nucleophile"
FT /evidence="ECO:0000250|UniProtKB:P51688"
FT BINDING 58
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250|UniProtKB:P51688"
FT BINDING 59
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250|UniProtKB:P51688"
FT BINDING 97
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /note="via 3-oxoalanine"
FT /evidence="ECO:0000250|UniProtKB:P51688"
FT BINDING 306
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250|UniProtKB:P51688"
FT BINDING 307
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250|UniProtKB:P51688"
FT MOD_RES 97
FT /note="3-oxoalanine (Cys)"
FT /evidence="ECO:0000250|UniProtKB:P51688"
SQ SEQUENCE 596 AA; 68452 MW; ED208609DA3FFF3B CRC64;
MLFLRFKFFN NRLLFVSVLC FVICVSCKRE HKEIKIKGEK ATELKLPERP NILWLVTEDM
GAYIPPFGDS TVVTPHLSKL AKEGVIYPNL YSTSGVCAPS RAAIATGMYP SSIGANHMRT
NSFTKERGLP AYEAVPPSNV RMLSEWLRKA GYYCTNNYKT DYQFKAPVTA WDESSPYAHW
RNRNDDQPFF AVFNFTDTHE SGLFEPYGLR EIETRLYRAG DTTYQWKNYG ASHANNRMSE
AETPQYLSKD TKFNIPPYLP ETDLVKRDMW KLYNNIGEMD NQVGAVLQQL EDDGLLENTI
IFFYGDHGGP LPREKRLIYD SGLNTPMIIR FPNKLEAETS DPQLISFVDF APTLLSIIGE
KPKEYMQGQA FLGQYKNKER SYIHAAADRF DAETDVIRAV RDKRFKYIRN YRPEQGYYLP
IDYRERIPTM QELLRLKAEG KLNEEQMQWF RDVKPEEELF DCKSDPFELK NLANNPEYQN
KLVELRKELD RWLTAIGDDA NLPESELINK LWNGSNTQPV TSDPKVSINN GNITISCDTE
GASVGYKIVT AGNKTSKTWH IYNGPFKMPL GSTLEIIAHR IGFKPSKAIQ ISTSDL
