ID   PLH31_FORAG             Reviewed;         487 AA.
AC   T2KM23;
DT   16-OCT-2019, integrated into UniProtKB/Swiss-Prot.
DT   13-NOV-2013, sequence version 1.
DT   25-MAY-2022, entry version 22.
DE   RecName: Full=Alpha-1,4-L-rhamnosidase {ECO:0000303|PubMed:31285597};
DE            EC=3.2.1.- {ECO:0000269|PubMed:31285597};
DE   AltName: Full=Glycosyl hydrolase 39 family protein P31 {ECO:0000305};
DE            Short=P31_GH39 {ECO:0000303|PubMed:31285597};
DE   AltName: Full=Polysaccharide utilization locus H protein P31 {ECO:0000303|PubMed:31285597};
DE            Short=PUL H protein P31;
DE   Flags: Precursor;
GN   ORFNames=BN863_22200;
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, 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: Alpha-rhamnosidase involved in ulvan degradation
CC       (PubMed:31285597). Ulvan is the main polysaccharide component of the
CC       Ulvales (green seaweed) cell wall. It is composed of disaccharide
CC       building blocks comprising 3-sulfated rhamnose (Rha3S) linked to D-
CC       glucuronic acid (GlcA), L-iduronic acid (IduA), or D-xylose (Xyl)
CC       (Probable). Endo-acting alpha-1,4-L-rhamnosidase cleaves rhamnose
CC       sections interspersed between xylose residues within the polymer,
CC       degrading larger oligomers with consecutive Xyl-Rha3S units that are
CC       resistant to the ulvan lyases and producing dimers Xyl-Rha3S and Xyl2S-
CC       Rha3S as the smallest products (PubMed:31285597).
CC       {ECO:0000269|PubMed:31285597, ECO:0000305|PubMed:31285597}.
CC   -!- SUBCELLULAR LOCATION: Periplasm {ECO:0000269|PubMed:31285597}.
CC   -!- INDUCTION: By ulvan and rhamnose. {ECO:0000269|PubMed:31285597}.
CC   -!- SIMILARITY: Belongs to the glycosyl hydrolase 39 family. {ECO:0000305}.
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DR   EMBL; HG315671; CDF79932.1; -; Genomic_DNA.
DR   RefSeq; WP_038530534.1; NZ_HG315671.1.
DR   AlphaFoldDB; T2KM23; -.
DR   STRING; 1347342.BN863_22200; -.
DR   EnsemblBacteria; CDF79932; CDF79932; BN863_22200.
DR   PATRIC; fig|1347342.6.peg.2227; -.
DR   eggNOG; COG3664; Bacteria.
DR   HOGENOM; CLU_559913_0_0_10; -.
DR   OrthoDB; 654705at2; -.
DR   Proteomes; UP000016160; Chromosome.
DR   GO; GO:0042597; C:periplasmic space; 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   InterPro; IPR000514; Glyco_hydro_39.
DR   InterPro; IPR017853; Glycoside_hydrolase_SF.
DR   Pfam; PF01229; Glyco_hydro_39; 1.
DR   SUPFAM; SSF51445; SSF51445; 1.
PE   2: Evidence at transcript level;
KW   Glycosidase; Hydrolase; Periplasm; Reference proteome; Signal.
FT   SIGNAL          1..30
FT                   /evidence="ECO:0000255"
FT   CHAIN           31..487
FT                   /note="Alpha-1,4-L-rhamnosidase"
FT                   /id="PRO_0000448310"
FT   ACT_SITE        199
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10068"
SQ   SEQUENCE   487 AA;  55825 MW;  8A478D160D12C66F CRC64;
     MKNKKRLCHI LKYIITCFLF GVIFIIPIQA QIVLQTDFTD SENARQNIDY HFNVFNRITP
     LNGVKIKTPL GKPRVCIVRP LGGIVKNGKP DISKDSYKWD KKSKTFYTDF TVLKNQIDGV
     INSGYAIHQI VLDNPSWAFQ RNKNGELVAD SLKVSTYGNA EPPKDYNAWS NYLKDVLKFL
     VNTYGEESML KIQFNIGREI GTPSHWSGSK EAFFEFYKIS SSAIREVLPT AKVGTHFLWG
     SSKNAWGTDF IKWSKANNVH YDFIGVSFYP FYNKPDRTLF KEVYAKDFAV IKDIPEWHKN
     AKLEMHEYAL IKSLNKAGNA FENAPKAQQN SFIVGLMKMF YEHNMQNVFQ WGQGTNFEAA
     QEALFSIQGQ TYYTSTKNGK PLLETNDVDA IFIKDVSNNI YNIMAYNYNA NPNATTDEHL
     NLKAKLDVPP GTKVKVRFAL YNKEKDTMSW SEWKEEATQG NEKSKSVISL NAELPVFSFL
     KYEVKVQ