PLH20_FORAG
ID PLH20_FORAG Reviewed; 926 AA.
AC T2KNB2;
DT 16-OCT-2019, integrated into UniProtKB/Swiss-Prot.
DT 16-OCT-2019, sequence version 2.
DT 03-AUG-2022, entry version 35.
DE RecName: Full=Alpha-L-rhamnosidase {ECO:0000303|PubMed:31285597};
DE EC=3.2.1.40 {ECO:0000269|PubMed:31285597};
DE AltName: Full=Glycosyl hydrolase 78 family protein P20 {ECO:0000305};
DE Short=P20_GH78 {ECO:0000303|PubMed:31285597};
DE AltName: Full=Polysaccharide utilization locus H protein P20 {ECO:0000303|PubMed:31285597};
DE Short=PUL H protein P20;
DE Flags: Precursor;
GN ORFNames=BN863_22090;
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 REVISION OF GENE MODEL, AND 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, 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: Alpha-L-rhamnosidase involved in ulvan degradation (Ref.2,
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). Alpha-L-rhamnosidase converts Rha-Xyl-Rha3S, the product of
CC a sulfatase acting on Rha3S-Xyl-Rha3S oligosaccharides, to Rha and Xyl-
CC Rha3S (PubMed:31285597). The enzyme is able to degrade p-nitrophenyl-
CC alpha-L-rhamnopyranoside (PNP-Rha) in vitro (Ref.2).
CC {ECO:0000269|PubMed:31285597, ECO:0000269|Ref.2, ECO:0000305|Ref.2}.
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:0000269|PubMed:31285597};
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000255|PROSITE-
CC ProRule:PRU00303}; Lipid-anchor {ECO:0000255|PROSITE-ProRule:PRU00303};
CC Periplasmic side {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}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CDF79921.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305|Ref.2};
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DR EMBL; HG315671; CDF79921.1; ALT_INIT; Genomic_DNA.
DR AlphaFoldDB; T2KNB2; -.
DR SMR; T2KNB2; -.
DR STRING; 1347342.BN863_22090; -.
DR EnsemblBacteria; CDF79921; CDF79921; BN863_22090.
DR PATRIC; fig|1347342.6.peg.2216; -.
DR eggNOG; COG3408; Bacteria.
DR HOGENOM; CLU_002926_1_1_10; -.
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 1: Evidence at protein level;
KW Cell membrane; Glycosidase; Hydrolase; Lipoprotein; Membrane; Palmitate;
KW Reference proteome; Signal.
FT SIGNAL 1..25
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00303"
FT CHAIN 26..926
FT /note="Alpha-L-rhamnosidase"
FT /id="PRO_0000448311"
FT ACT_SITE 510
FT /note="Proton donor"
FT /evidence="ECO:0000250|UniProtKB:Q82PP4"
FT ACT_SITE 779
FT /note="Proton acceptor"
FT /evidence="ECO:0000250|UniProtKB:Q82PP4"
FT BINDING 504
FT /ligand="alpha-L-rhamnose"
FT /ligand_id="ChEBI:CHEBI:27907"
FT /evidence="ECO:0000250|UniProtKB:Q82PP4"
FT BINDING 508..510
FT /ligand="alpha-L-rhamnose"
FT /ligand_id="ChEBI:CHEBI:27907"
FT /evidence="ECO:0000250|UniProtKB:Q82PP4"
FT BINDING 517
FT /ligand="alpha-L-rhamnose"
FT /ligand_id="ChEBI:CHEBI:27907"
FT /evidence="ECO:0000250|UniProtKB:Q82PP4"
FT BINDING 569
FT /ligand="alpha-L-rhamnose"
FT /ligand_id="ChEBI:CHEBI:27907"
FT /evidence="ECO:0000250|UniProtKB:Q82PP4"
FT BINDING 800
FT /ligand="alpha-L-rhamnose"
FT /ligand_id="ChEBI:CHEBI:27907"
FT /evidence="ECO:0000250|UniProtKB:Q82PP4"
FT LIPID 26
FT /note="N-palmitoyl cysteine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00303"
FT LIPID 26
FT /note="S-diacylglycerol cysteine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00303"
SQ SEQUENCE 926 AA; 104841 MW; FCD19270BDEBAA69 CRC64;
MILHKSVFKS YIYVLTYFVF FSVMSCENSS VLQEAKHLTI SEGFKNPLGF YDAKPTFSWE
LPVVEGVISQ SAYQIVVASS PDLLPNNPDL WDSNKQSSSQ SVWINYEGKP LVSRQKVFWQ
VKYWNQDDKA SNWSPVQNFE LGLLNNSDWK AKWIGLPTKE EGVLGSQDNI IHRPQYLRKV
FELSNDVANA RLYITAKGVF DVAINGEDVS DDVMPPGYTP YKKRIETITY DVTDLIESGQ
NTIGVEVAAG WHSGRLGWMK SYWSDTESPK ILCQLEVTMK DGSKASIISD DTWKATTQGP
IRISEIYDGE TYDAHLEMPH WTTNSFDDKN WKAVQAFPVT STIKLEPKRH TTVKSKIVLE
SKEIILKADA AIFDLQQNMV GVPLLKVPMK MGDTLKIRFA EMLSPDGTFY TDNYRSAQST
DYYIAAKEGT IEWMPKFTFH GFRYVELSGF DASKTPSKNW VKGVVQYSNF NENGSFTSSH
EKLNQLQSNI VWGLRGNFFD IPTDCPQRDE RMGWTGDAQV FGPTSMFNAD VYKFWASWMQ
SVRESQYDNG GIPFVVPDVL HNGKVSSGWG DVCTIIPWKI YYRTGDVGIL EENYDMMKKW
VAHHQATSKD FISHMNSFAD WLQPYPENGN NKGDTSHSLI GTAFFAHSAK LTAKTAEVLG
KKEEQATYEA LYKSVAKAFE NAFFKNGKVK DVTATQTSYL LALAFDLLSE ENKENAKQQL
LEKISEADNH LRTGFLGTPL LSEVLDETGE IDLMYKLLFN ETYPSWFYSI NQGATTIWER
WNSYSKAEGF NPMKMNSLNH YAYGAIGEWM YERITGIAPL QAGYKIISIA PIPKAPLTSA
SATLNTPYGE VASSWEIKNE TLFLEVVVPP NTTAEIEIPT DNSESLKVDN ENFTNGKNLK
LIKNEKRKIK ILAQPGTYEF QAKYSL
