PLH28_FORAG
ID PLH28_FORAG Reviewed; 952 AA.
AC T2KPL4;
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=Alpha-L-rhamnosidase {ECO:0000303|PubMed:31285597};
DE EC=3.2.1.40 {ECO:0000250|UniProtKB:T2KNB2};
DE AltName: Full=Glycosyl hydrolase 78 family protein P28 {ECO:0000305};
DE Short=P28_GH78 {ECO:0000303|PubMed:31285597};
DE AltName: Full=Polysaccharide utilization locus H protein P28 {ECO:0000303|PubMed:31285597};
DE Short=PUL H protein P28;
DE Flags: Precursor;
GN ORFNames=BN863_22170;
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-L-rhamnosidase that may be involved in ulvan
CC degradation (Probable). Ulvan is the main polysaccharide component of
CC the 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). {ECO:0000305|PubMed:31285597}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Hydrolysis of terminal non-reducing alpha-L-rhamnose residues
CC in alpha-L-rhamnosides.; EC=3.2.1.40;
CC Evidence={ECO:0000250|UniProtKB:T2KNB2};
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:31285597};
CC Lipid-anchor {ECO:0000255|PROSITE-ProRule:PRU00303}; Periplasmic side
CC {ECO:0000305|PubMed:31285597}.
CC -!- INDUCTION: By ulvan and rhamnose. {ECO:0000269|PubMed:31285597}.
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 78 family. {ECO:0000305}.
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DR EMBL; HG315671; CDF79929.1; -; Genomic_DNA.
DR RefSeq; WP_038530525.1; NZ_HG315671.1.
DR AlphaFoldDB; T2KPL4; -.
DR SMR; T2KPL4; -.
DR STRING; 1347342.BN863_22170; -.
DR EnsemblBacteria; CDF79929; CDF79929; BN863_22170.
DR PATRIC; fig|1347342.6.peg.2224; -.
DR eggNOG; COG3408; Bacteria.
DR HOGENOM; CLU_002926_1_1_10; -.
DR OMA; FFTAYPR; -.
DR OrthoDB; 170130at2; -.
DR Proteomes; UP000016160; Chromosome.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0030596; F:alpha-L-rhamnosidase activity; IEA:UniProtKB-EC.
DR GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro.
DR Gene3D; 1.50.10.10; -; 1.
DR Gene3D; 2.60.40.10; -; 1.
DR InterPro; IPR008928; 6-hairpin_glycosidase_sf.
DR InterPro; IPR012341; 6hp_glycosidase-like_sf.
DR InterPro; IPR016007; Alpha_rhamnosid.
DR InterPro; IPR035396; Bac_rhamnosid6H.
DR InterPro; IPR035398; Bac_rhamnosid_C.
DR InterPro; IPR013737; Bac_rhamnosid_N.
DR InterPro; IPR013783; Ig-like_fold.
DR InterPro; IPR008902; Rhamnosid_concanavalin.
DR Pfam; PF05592; Bac_rhamnosid; 1.
DR Pfam; PF17389; Bac_rhamnosid6H; 1.
DR Pfam; PF17390; Bac_rhamnosid_C; 1.
DR Pfam; PF08531; Bac_rhamnosid_N; 1.
DR PIRSF; PIRSF010631; A-rhamnsds; 1.
DR SUPFAM; SSF48208; SSF48208; 1.
PE 2: Evidence at transcript level;
KW Cell membrane; Glycosidase; Hydrolase; Lipoprotein; Membrane;
KW Reference proteome; Signal.
FT SIGNAL 1..21
FT /evidence="ECO:0000255"
FT CHAIN 22..952
FT /note="Alpha-L-rhamnosidase"
FT /id="PRO_5004591130"
FT ACT_SITE 525
FT /note="Proton donor"
FT /evidence="ECO:0000250|UniProtKB:Q82PP4"
FT ACT_SITE 809
FT /note="Proton acceptor"
FT /evidence="ECO:0000250|UniProtKB:Q82PP4"
FT BINDING 520
FT /ligand="alpha-L-rhamnose"
FT /ligand_id="ChEBI:CHEBI:27907"
FT /evidence="ECO:0000250|UniProtKB:Q82PP4"
FT BINDING 524..525
FT /ligand="alpha-L-rhamnose"
FT /ligand_id="ChEBI:CHEBI:27907"
FT /evidence="ECO:0000250|UniProtKB:Q82PP4"
FT BINDING 532
FT /ligand="alpha-L-rhamnose"
FT /ligand_id="ChEBI:CHEBI:27907"
FT /evidence="ECO:0000250|UniProtKB:Q82PP4"
FT BINDING 594
FT /ligand="alpha-L-rhamnose"
FT /ligand_id="ChEBI:CHEBI:27907"
FT /evidence="ECO:0000250|UniProtKB:Q82PP4"
FT BINDING 826
FT /ligand="alpha-L-rhamnose"
FT /ligand_id="ChEBI:CHEBI:27907"
FT /evidence="ECO:0000250|UniProtKB:Q82PP4"
SQ SEQUENCE 952 AA; 108674 MW; 4EF328B1CC2E1EA2 CRC64;
MKYNKLLFSL LLLAVFCFSC KEEQKLQTSL DFDKVLLNAK SNPIAIESES PLFSWIIKAE
GFGKSQSAYH ILVASSLDKL DETHADVWNS NKVESSKSTF VKYEGKELKA ATRYYWKVKV
WDKSNQESNW SEPQYFQMGL LDESNWGEAK WITLTNDTRT SEYRFREYKT GRMEQPIQVD
GFAASYFRNK INLNKEVDNA QVYICGLGYY EFFLNGEKVG DHVLDPAPSN YDKQAYYVNY
DITEQLNSGE NALGIILGNG FYGQNISWKN DPESDRDLAY GPPTVRVLLK LKYKDGTESE
FFSDETWKES TGPIVFNNIY GGDTYDARFE LGDWTSTNYD DSSWGFAKET APEIKNISAQ
QIPAIKKLQD YEPQNVFKGS DGEWIVDFGQ NIAGWVKLNV SEKEGQLIEV ITTEALLTNG
RDIFPGSTGG GANGMAQIYQ YICKGDGQES WEPKFSYHGF RYAKIKGVST KPDADMIKAV
LVATDIQETG SFECSDDLFN KMHNISKWTI VDNVHGIPED CPHREKCGWL GDAHAFCEYA
LYNYDMYDFY KKYMEDIRTQ MLPTKGHNNP ELKFQVPTMI APGKRTSSYA KIDWGVATMY
LPWYNYLYYG DDAIVNEYYP EMKDLTNFYL NFKGENGIMQ DGMGDWCPPR WDRRTNPEAM
ECDPIISANA YFYDVLGIME TFAKMNNDGA FQSEMKAEKE ALKDAFNKAF LVEIPNTDFK
WYQSQTATVQ ALQFGMVPEE EIENVVNGLE YDIVEVKGGH HSTGIHGNRY IYTVLSKYGK
ADLAYRILTT PDFPSQTYIM NSGFTTWPER QFEWETMEGP TNSLNHPMHS GFSAYFFESL
GGIKSSTKEA GYKQFIVNPE FPSQITQTKV SVPTPYGDIK NDWSFEEGKL SMTLEIPFNT
EANLVLNQAE LESLIINGKT FQNLQKNTKS VTLQGSNVIL GSGKYKILYN KR
