ID   PLH8_FORAG              Reviewed;         824 AA.
AC   T2KPJ7;
DT   16-OCT-2019, integrated into UniProtKB/Swiss-Prot.
DT   13-NOV-2013, sequence version 1.
DT   03-AUG-2022, entry version 34.
DE   RecName: Full=Putative beta-glucuronidase {ECO:0000305};
DE            EC=3.2.1.31 {ECO:0000250|UniProtKB:P05804};
DE   AltName: Full=Glycosyl hydrolase 2 family protein P8 {ECO:0000305};
DE            Short=P8_GH2 {ECO:0000303|PubMed:31285597};
DE   AltName: Full=Polysaccharide utilization locus H protein P8 {ECO:0000303|PubMed:31285597};
DE            Short=PUL H protein P8;
GN   ORFNames=BN863_21970;
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 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: Glycoside hydrolase 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   -!- CATALYTIC ACTIVITY:
CC       Reaction=a beta-D-glucuronoside + H2O = an alcohol + D-glucuronate;
CC         Xref=Rhea:RHEA:17633, ChEBI:CHEBI:15377, ChEBI:CHEBI:30879,
CC         ChEBI:CHEBI:58720, ChEBI:CHEBI:83411; EC=3.2.1.31;
CC         Evidence={ECO:0000250|UniProtKB:P05804};
CC   -!- SUBCELLULAR LOCATION: Membrane {ECO:0000255}; Single-pass membrane
CC       protein {ECO:0000255}.
CC   -!- INDUCTION: By ulvan and rhamnose. {ECO:0000269|PubMed:31285597}.
CC   -!- SIMILARITY: Belongs to the glycosyl hydrolase 2 family. {ECO:0000305}.
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DR   EMBL; HG315671; CDF79909.1; -; Genomic_DNA.
DR   AlphaFoldDB; T2KPJ7; -.
DR   SMR; T2KPJ7; -.
DR   STRING; 1347342.BN863_21970; -.
DR   EnsemblBacteria; CDF79909; CDF79909; BN863_21970.
DR   PATRIC; fig|1347342.6.peg.2204; -.
DR   eggNOG; COG3250; Bacteria.
DR   HOGENOM; CLU_006501_5_0_10; -.
DR   OMA; PWCRGGL; -.
DR   Proteomes; UP000016160; Chromosome.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0004566; F:beta-glucuronidase activity; IEA:UniProtKB-EC.
DR   GO; GO:0016052; P:carbohydrate catabolic process; IEA:UniProt.
DR   Gene3D; 2.60.40.10; -; 2.
DR   InterPro; IPR036156; Beta-gal/glucu_dom_sf.
DR   InterPro; IPR032311; DUF4982.
DR   InterPro; IPR008979; Galactose-bd-like_sf.
DR   InterPro; IPR006101; Glyco_hydro_2.
DR   InterPro; IPR006103; Glyco_hydro_2_cat.
DR   InterPro; IPR006102; Glyco_hydro_2_Ig-like.
DR   InterPro; IPR006104; Glyco_hydro_2_N.
DR   InterPro; IPR017853; Glycoside_hydrolase_SF.
DR   InterPro; IPR013783; Ig-like_fold.
DR   Pfam; PF16355; DUF4982; 1.
DR   Pfam; PF00703; Glyco_hydro_2; 1.
DR   Pfam; PF02836; Glyco_hydro_2_C; 1.
DR   Pfam; PF02837; Glyco_hydro_2_N; 1.
DR   PRINTS; PR00132; GLHYDRLASE2.
DR   SUPFAM; SSF49303; SSF49303; 1.
DR   SUPFAM; SSF49785; SSF49785; 1.
DR   SUPFAM; SSF51445; SSF51445; 1.
PE   2: Evidence at transcript level;
KW   Glycosidase; Hydrolase; Membrane; Reference proteome; Transmembrane;
KW   Transmembrane helix.
FT   CHAIN           1..824
FT                   /note="Putative beta-glucuronidase"
FT                   /id="PRO_0000448299"
FT   TRANSMEM        26..43
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   ACT_SITE        430
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000250|UniProtKB:P05804"
SQ   SEQUENCE   824 AA;  93897 MW;  3013B5FA502418B4 CRC64;
     MGFCMKDSKQ YYKSSIGKSL KRSNGYLKLV LVLYLIMVSW SGYSKEVFNS RTKENINANW
     LYLEKNIKDI NLALNDANWE SINLPHTWNA LDATDLNPGY RRSGSWYKKE LAISNIENNK
     LYQLYFEGVN INSEVYVNGQ KAGGHIGGYI GFTIDITEFI KSGKNDIVIR VDNSYDPEVI
     PSQKSDFFIF GGITRDVWLE TIPKQHLSEL KITTPKVSEN EAELLATVAI NNLNNSNLKV
     QANLLDAQGV TVVSSVFKIK NNTAKIHFRN IKNPKLWDTE HPNLYTLKVA LLEKGDVIDS
     VQNRVGFRWF EFKDHGAFYL NGKRVLLRGT HRHEEHAGVG AAMSNMQHRK DMELIKDMGA
     NFVRLAHYPQ DPEVYKACDE LGLLIWDELP WCRGGLGNET WKTNTKNMLT EIINQNYNHP
     SIIIWSLGNE MYWLPDFENG DDTDKMNSFL TELNDLAHQL DPSRKTAIRK YYEGSHIVDV
     FSPSIWSGWY SGSYKSYQKA IDTYKKEYPH FLHAEYGGSS HVGRHTENPV TGEGKIQSDG
     WEEEIVQTDV ANIAQIGDWS ENYIVDLFDW HLRISENDEN FVGNVQWAFK DFGTPLRPEN
     AIPYMNQKGL VDRAGNPKDA FYVFKSYWSK EPFTYIESHT WTERQGPKDL ARDISVYSNC
     PEVELFLNGK SLGVKKRDLK VFPAAGLNWN LNFKEGKNTL VAVGKTKENK TVKDELAINY
     RFTKNGKAVG LKLESELLEN GNYLVTAIAY DKNGLRCLDY EDQVYFQCLS GGETLKSQGT
     PTGSESIAMA NGKAAIEVKR DGKNIPVVMM VLNQNFKGTY LTIE