ID   PLH27_FORAG             Reviewed;         592 AA.
AC   T2KN85;
DT   16-OCT-2019, integrated into UniProtKB/Swiss-Prot.
DT   13-NOV-2013, sequence version 1.
DT   25-MAY-2022, entry version 25.
DE   RecName: Full=Beta-xylosidase {ECO:0000303|PubMed:31285597};
DE            EC=3.2.1.- {ECO:0000269|PubMed:31285597};
DE   AltName: Full=Glycosyl hydrolase 43 family protein P27 {ECO:0000305};
DE            Short=P27_GH43 {ECO:0000303|PubMed:31285597};
DE   AltName: Full=Polysaccharide utilization locus H protein P27 {ECO:0000303|PubMed:31285597};
DE            Short=PUL H protein P27;
DE   Flags: Precursor;
GN   ORFNames=BN863_22160;
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: Xylosidase 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). Beta-
CC       xylosidase converts Xyl-Rha3S, a product of alpha-L-rhamnosidase acting
CC       on Rha-Xyl-Rha3S oligosaccharides, further to Xyl and Rha3S
CC       (PubMed:31285597). {ECO:0000269|PubMed:31285597,
CC       ECO:0000305|PubMed:31285597}.
CC   -!- SUBCELLULAR LOCATION: Cell outer membrane
CC       {ECO:0000269|PubMed:31285597}; Lipid-anchor {ECO:0000255|PROSITE-
CC       ProRule:PRU00303}; Periplasmic side {ECO:0000305|PubMed:31285597}.
CC   -!- INDUCTION: By ulvan and rhamnose. {ECO:0000269|PubMed:31285597}.
CC   -!- SIMILARITY: Belongs to the glycosyl hydrolase 43 family. {ECO:0000305}.
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DR   EMBL; HG315671; CDF79928.1; -; Genomic_DNA.
DR   AlphaFoldDB; T2KN85; -.
DR   SMR; T2KN85; -.
DR   STRING; 1347342.BN863_22160; -.
DR   EnsemblBacteria; CDF79928; CDF79928; BN863_22160.
DR   PATRIC; fig|1347342.6.peg.2223; -.
DR   eggNOG; COG3507; Bacteria.
DR   HOGENOM; CLU_016508_1_0_10; -.
DR   OMA; WEDLADN; -.
DR   Proteomes; UP000016160; Chromosome.
DR   GO; GO:0009279; C:cell outer membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0004553; F:hydrolase activity, hydrolyzing O-glycosyl compounds; IEA:InterPro.
DR   GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro.
DR   Gene3D; 2.115.10.20; -; 1.
DR   InterPro; IPR013320; ConA-like_dom_sf.
DR   InterPro; IPR041542; GH43_C2.
DR   InterPro; IPR006710; Glyco_hydro_43.
DR   InterPro; IPR023296; Glyco_hydro_beta-prop_sf.
DR   Pfam; PF17851; GH43_C2; 1.
DR   Pfam; PF04616; Glyco_hydro_43; 1.
DR   SUPFAM; SSF49899; SSF49899; 1.
DR   SUPFAM; SSF75005; SSF75005; 1.
PE   1: Evidence at protein level;
KW   Cell outer membrane; Glycosidase; Hydrolase; Lipoprotein; Membrane;
KW   Palmitate; Reference proteome; Signal.
FT   SIGNAL          1..19
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00303"
FT   CHAIN           20..592
FT                   /note="Beta-xylosidase"
FT                   /id="PRO_5004590959"
FT   LIPID           20
FT                   /note="N-palmitoyl cysteine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00303"
FT   LIPID           20
FT                   /note="S-diacylglycerol cysteine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00303"
SQ   SEQUENCE   592 AA;  67176 MW;  ECBD77E94D2A8BC4 CRC64;
     MYLNACRALT LISVLSLLAC NSEPEKKQAT PSKEIAKAQT GSWGDQGDGT YINPILNADY
     PDSDIEQVGD TYYMITSKQH MSPGMPILES KDMVNWTNVG HVFNSLSWAP EYNWDRMNGY
     SFGTWAGDLA YHEGTWYCYQ IDYQHGLMVA TSKDIKGPWS KPIMMLPKSE VLDDPAVFWD
     EDTHKAYIII NTAGKQKEAS NTIEGNENRI YEMSWDGTKI LDEGKLVYTG MGAEAAKIYK
     IDGTWYIFLA QWTMGDMSTK PGVKNPKNDR KQIVLRSKES IYGPYEVKTV LEKGTVFNNR
     SASQGALMQA PDNSWWYMHQ LIQNDDIPFQ GRPQCLEPVT WVDGWPIIGV DEDNDGIGEP
     VKTYKKPIDG YPVTAPRTDD DFSSPKLGFQ WEWNHNPRNT HWSLTERPGW LRLKASKVLP
     NEKGYGPNIN EWTNNDGSDS DFWRANNTLS QRIMGITTGT AVAKFDVSGM KPHQLAGFVR
     YGGVFNLLGV EVDEHGKKHL FYMEPMGEKT VGPEITVNDL YIRTSNRSNQ AIYEYSFDGK
     NFKRFGPTFT IAFGKWTGDR LGLFSWNDKE DAGYIDVDWF TYDYDGPKAA NQ