ID   PLH15_FORAG             Reviewed;        1163 AA.
AC   T2KNA8;
DT   16-OCT-2019, integrated into UniProtKB/Swiss-Prot.
DT   13-NOV-2013, sequence version 1.
DT   25-MAY-2022, entry version 28.
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 P15 {ECO:0000305};
DE            Short=P15_GH2 {ECO:0000303|PubMed:31285597};
DE   AltName: Full=Polysaccharide utilization locus H protein P15 {ECO:0000303|PubMed:31285597};
DE            Short=PUL H protein P15;
DE   Flags: Precursor;
GN   ORFNames=BN863_22040;
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.
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, 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: Glycoside hydrolase involved in ulvan degradation (Ref.2).
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|Ref.2, ECO:0000305|Ref.2}.
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: Periplasm {ECO:0000305|PubMed:31285597}.
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; CDF79916.1; -; Genomic_DNA.
DR   AlphaFoldDB; T2KNA8; -.
DR   SMR; T2KNA8; -.
DR   STRING; 1347342.BN863_22040; -.
DR   EnsemblBacteria; CDF79916; CDF79916; BN863_22040.
DR   PATRIC; fig|1347342.6.peg.2211; -.
DR   eggNOG; COG3940; Bacteria.
DR   HOGENOM; CLU_003772_2_1_10; -.
DR   OMA; ECGSQNW; -.
DR   Proteomes; UP000016160; Chromosome.
DR   GO; GO:0042597; C:periplasmic space; IEA:UniProtKB-SubCell.
DR   GO; GO:0004566; F:beta-glucuronidase activity; IEA:UniProtKB-EC.
DR   GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro.
DR   InterPro; IPR008979; Galactose-bd-like_sf.
DR   InterPro; IPR006104; Glyco_hydro_2_N.
DR   Pfam; PF02837; Glyco_hydro_2_N; 1.
DR   SUPFAM; SSF49785; SSF49785; 1.
PE   2: Evidence at transcript level;
KW   Hydrolase; Periplasm; Reference proteome; Signal.
FT   SIGNAL          1..20
FT                   /evidence="ECO:0000255"
FT   CHAIN           21..1163
FT                   /note="Putative beta-glucuronidase"
FT                   /id="PRO_5004602864"
SQ   SEQUENCE   1163 AA;  130222 MW;  697B06A1A3758E9B CRC64;
     MPRFLKYILG LFLISISAFG QNLVPEVTEL ESGFNSPPNQ AKARTWWHWI SGNVSKSGIT
     KDLEAMKAVG IQEAQLFNVD LGFPAGPVDY LSEDWLDLFH FSALEAKRIG LELTFHNTAG
     WSSSGGPWIS PEYAMQTVVY SEIIVKGGKA IKKQLPQPET KLNFYKDIAV LAFPKPKQTM
     KIDDLDFKSL SGRIRNHLLP DTKIIPSEAV IQKQEIINLT AHLNDAGILE WKVPKGEWVI
     LRLGHTPTGK KNHPAPKGGH GLEVDKMSTK AVDVYWEGGI QPILNKLGDL VGTTVNNCLI
     DSYEVGTANW TAGFDAEFET LRGYSLVSYL PTLAGYYVES GEITERFLWD FRRTIGDLMA
     KNYYAHFRDL CHKNGLKFSV EPYWGPFDNM QVGATGDIVM CEFWSGGYPF FDSPKFVSSI
     AHLNGSSIVG AESFTGIGGW DEHPAELKSI GDRAWAEGIT RFIFHTYVHQ PWDVAPGLAL
     SYHGTDFNRL NTWWRQGKAF MDYIARSQFM LQQGKNVADV LVFTGESSPN TAFLLPEIKQ
     LGYDYDLIGS NKLSDLFVKN GKICTPVGGQ YDVLMLPESD WIKPETLHKI EDLVKDGAKV
     IGSKPKKSPS LEHYSTCDAE VKRLSDFLWG KGLVKEISIV DFLKGNNLLA DFKIESDDVS
     DISFIHRKTD EADIYFIANA RKESREIKVR FRVSNKQPEI WQAESGTIKK PAVWQNHADG
     TTSLPLQLGM EEAVFVVFKN ASKEKSQLVS AKMELENPKS EPLSNLQIIK AEYGTFLQEG
     LVDITDKVAA EVKDNQLHIQ ASRAFCDCDP AMGYIKEFRM EYQIGEDIKT ISAQEKEYVN
     INAGDKKLTV LKAVFGKFKP ETKGVPKHYP VHDVTEKIKQ EIASGNLVIP VNNQLIGGKT
     PEGDNTTIKI TFTTDGEEQT LFVPKGRPLN LSKDRSKPEI VLNDGETQWI TPYPGTLSYK
     NLSGKVMATT VKSVPQPIML AGTWDVEFPS DLVTINKVRF DELKSWSAVE NEGIKYFSGT
     ASYHKTFQVS KKLLKSNNKL ELDLGSVAVI AEVILNGKPV GTLWKAPFRL DVTNDVKTGE
     NKLEVKVTNL WPNRLIGDEK LPLDFERKGP KIKSVPDWLL NNTKRPSERT TFPAWKHWDK
     EDELLSSGLL GPVKINVLVE KSL