PLH19_FORAG
ID PLH19_FORAG Reviewed; 511 AA.
AC T2KMG7;
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=Ulvan-active sulfatase {ECO:0000305};
DE EC=3.1.6.- {ECO:0000269|PubMed:31285597};
DE AltName: Full=Polysaccharide utilization locus H protein P19 {ECO:0000303|PubMed:31285597};
DE Short=PUL H protein P19;
DE AltName: Full=Sulfatase family S1 subfamily 27 protein P19 {ECO:0000305};
DE Short=P19_S1_27 {ECO:0000303|PubMed:31285597};
DE Flags: Precursor;
GN ORFNames=BN863_22080;
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:P15289};
CC Note=Binds 1 Ca(2+) ion per subunit. {ECO:0000250|UniProtKB:P15289};
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 -!- INDUCTION: By ulvan. {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; CDF79920.1; -; Genomic_DNA.
DR RefSeq; WP_051774714.1; NZ_HG315671.1.
DR AlphaFoldDB; T2KMG7; -.
DR SMR; T2KMG7; -.
DR STRING; 1347342.BN863_22080; -.
DR EnsemblBacteria; CDF79920; CDF79920; BN863_22080.
DR PATRIC; fig|1347342.6.peg.2215; -.
DR eggNOG; COG3119; Bacteria.
DR HOGENOM; CLU_006332_9_3_10; -.
DR OMA; KDAGAWD; -.
DR OrthoDB; 1067869at2; -.
DR Proteomes; UP000016160; Chromosome.
DR GO; GO:0005886; C:plasma membrane; 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; 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..34
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00303"
FT CHAIN 35..511
FT /note="Ulvan-active sulfatase"
FT /id="PRO_0000448337"
FT ACT_SITE 99
FT /note="Nucleophile"
FT /evidence="ECO:0000250|UniProtKB:P15289"
FT ACT_SITE 149
FT /evidence="ECO:0000250|UniProtKB:P15289"
FT BINDING 59
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250|UniProtKB:P15289"
FT BINDING 99
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /note="via 3-oxoalanine"
FT /evidence="ECO:0000250|UniProtKB:P15289"
FT BINDING 305
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250|UniProtKB:P15289"
FT MOD_RES 99
FT /note="3-oxoalanine (Cys)"
FT /evidence="ECO:0000250|UniProtKB:P15289"
FT LIPID 35
FT /note="N-palmitoyl cysteine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00303"
FT LIPID 35
FT /note="S-diacylglycerol cysteine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00303"
SQ SEQUENCE 511 AA; 57783 MW; 5E4A57A849B9FCB3 CRC64;
MNFKQNIVYK KMAISMKITA IRPIALVISF TLLSCKDKVK TVEQQDEPTK PNIVYILTDQ
WRGAALGYAG DPNVKTPHLD ALAKEAVNFT NAVSVTPVCT PHRASLLTGK YPITTGMFLN
DLYLPSEELC MAEIFKAEGY NTAYWGKWHL DGHRRSAYTP KERRQGFDYW KALECSHDYN
KMPYYDNDNP EVKYWGKYSP FAIVEDANTY LEKQAKDDTP FLAVVSIATP HFPHGSAPQK
YKDMYSPESL ILNPNVSPKF EARSREELQG YYAHATATDE AIGLLLKQMD ALGLNENTIV
VFSSDHGEMM GANDVRPFQK QVAWDESIRV PFLIKYPGID KQKGVTVNAP INTPDILPSL
LGLSNIKIPD GIEGEDLSEL IKNPDPEADR EALVMNVAPF AGGYPNLPYR AIRTKQYTYA
RTTEGPSMFF DNVADPYQQN NLLGKPEFET LQNELDAKLN KKLAELGDEF KSRDYYLKKY
NYVFGKNKPA IPYWEFNNGK GEVQSPIPVT Q
