PLH10_FORAG
ID PLH10_FORAG Reviewed; 816 AA.
AC T2KNA3;
DT 16-OCT-2019, integrated into UniProtKB/Swiss-Prot.
DT 13-NOV-2013, sequence version 1.
DT 25-MAY-2022, entry version 32.
DE RecName: Full=Endo-acting ulvan lyase {ECO:0000303|PubMed:31285597};
DE EC=4.2.2.- {ECO:0000269|PubMed:31285597};
DE AltName: Full=Endolytic ulvan lyase;
DE AltName: Full=P10_PLnc {ECO:0000303|PubMed:31285597};
DE AltName: Full=Polysaccharide utilization locus H protein P10 {ECO:0000303|PubMed:31285597};
DE Short=PUL H protein P10;
DE Flags: Precursor;
GN ORFNames=BN863_21990;
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, INDUCTION, AND SUBCELLULAR LOCATION.
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: Ulvan lyase 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). Ulvan
CC lyase catalyzes the endolytic cleavage of the glycosidic bond between
CC Rha3S and the uronic acids GlcA or IduA, producing oligosaccharides
CC that have unsaturated 4-deoxy-L-threo-hex-4-enopyranosiduronic acid
CC (deltaUA) at the non-reducing end. This results eventually in the
CC degradation of the ulvan polysaccharide into deltaUA-Rha3S
CC disaccharides and deltaUA-Rha3S-Xyl-Rha3S tetrasaccharides
CC (PubMed:31285597). {ECO:0000269|PubMed:31285597,
CC ECO:0000305|PubMed:31285597}.
CC -!- SUBCELLULAR LOCATION: Cell surface {ECO:0000269|PubMed:31285597}.
CC Periplasm {ECO:0000269|PubMed:31285597}.
CC -!- INDUCTION: By ulvan and rhamnose. {ECO:0000269|PubMed:31285597}.
CC -!- SIMILARITY: Belongs to the polysaccharide lyase family. {ECO:0000305}.
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DR EMBL; HG315671; CDF79911.1; -; Genomic_DNA.
DR RefSeq; WP_038530499.1; NZ_HG315671.1.
DR AlphaFoldDB; T2KNA3; -.
DR SMR; T2KNA3; -.
DR STRING; 1347342.BN863_21990; -.
DR EnsemblBacteria; CDF79911; CDF79911; BN863_21990.
DR PATRIC; fig|1347342.6.peg.2206; -.
DR eggNOG; ENOG502Z862; Bacteria.
DR HOGENOM; CLU_014479_0_0_10; -.
DR OrthoDB; 442785at2; -.
DR Proteomes; UP000016160; Chromosome.
DR GO; GO:0009986; C:cell surface; IEA:UniProtKB-SubCell.
DR GO; GO:0042597; C:periplasmic space; IEA:UniProtKB-SubCell.
DR GO; GO:0016829; F:lyase activity; IEA:UniProtKB-KW.
DR Gene3D; 1.50.10.100; -; 1.
DR InterPro; IPR008929; Chondroitin_lyas.
DR SUPFAM; SSF48230; SSF48230; 1.
PE 1: Evidence at protein level;
KW Lyase; Periplasm; Reference proteome; Signal.
FT SIGNAL 1..23
FT /evidence="ECO:0000255"
FT CHAIN 24..816
FT /note="Endo-acting ulvan lyase"
FT /id="PRO_5004590961"
SQ SEQUENCE 816 AA; 92871 MW; DA8E9A102D00DE27 CRC64;
MGTSVRRISV VLMMLFGTNF CWSQSMQHPV IWVTQDEKQD ILNLIEKYDW AKKMEHDLHA
VVDKKVEAHQ KKPSVILSHI PEIPADNSLT EFEAVTVGDH AAVLTDASYA AMLYFLTDDE
KYAQFSADVL WHYVTVLSDR SPKNTTICGN HFYDPRTSYA QFALAYDFIY NFLNKPTTKV
YKASANKQQT FDRDLFQKVL LNMVGSSLQE YGRPDTHGKF ISNHPILTAP GVLYGILCIE
DDKERERLFD VFWEKGTAHQ NSFKNTILPM FGKQGIWPES TSYSFMPAVT LVLNIIDRVY
PEMQVTQNYK NIYKGNFLFD NLRMPDGRFV RYGDSKRNHD GTEQLYRYTL NLAQRRGYSN
LENQAKIALS QAYQRQGGYQ SKISPATFNS SEPLKLFWGT PIPKGIDSKI DFKKPTVLVE
HAGIALQRNY VETDNELYGL CGIIGGAHYV HSHVTGITME LYGAGYVMAP NGGLPKTVKE
RRIPLHENYF RLYAGNNTVI VNGTSHGIQP GSWKDGAYVW QNTVVNIAAE PKHLEDPISE
HFNFATQFLK DTINNCDQER TLSTIRTSEK TGYYLDVFRS KSLTENKFQD YIYHNIGDAT
LLETENGETL RTEPTTRYKT DIGDPVQSPG WRYFEDTKST KPIHKGVHAT FKIDYDERFM
HMFVPQGVNR SYTTALAPPT REAKNGYEEK PTQVLAIRQD GEAWEKPFIA VFEPSVKASS
SVQTVTPLQD ADKVVGVTVI SKVNGKLITD YIISLDSKDG VYENKILKIK FEGRFGIIRV
EGEQKTISLY IGEGKTLKYN NYTLDSETAT TAYKVF