PLH34_FORAG
ID PLH34_FORAG Reviewed; 756 AA.
AC T2KMH9;
DT 16-OCT-2019, integrated into UniProtKB/Swiss-Prot.
DT 13-NOV-2013, sequence version 1.
DT 25-MAY-2022, entry version 29.
DE RecName: Full=Putative beta-xylosidase {ECO:0000303|PubMed:31285597};
DE EC=3.2.1.- {ECO:0000305|PubMed:31285597};
DE AltName: Full=Glycosyl hydrolase 3 family protein P34 {ECO:0000305};
DE Short=P34_GH3 {ECO:0000303|PubMed:31285597};
DE AltName: Full=Polysaccharide utilization locus H protein P34 {ECO:0000303|PubMed:31285597};
DE Short=PUL H protein P34;
DE Flags: Precursor;
GN ORFNames=BN863_22230;
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: Glycoside hydrolase probably involved in ulvan degradation
CC (Probable). Ulvan is the main polysaccharide component of the Ulvales
CC (green seaweed) cell wall. It is composed of disaccharide building
CC blocks comprising 3-sulfated rhamnose (Rha3S) linked to D-glucuronic
CC acid (GlcA), L-iduronic acid (IduA), or D-xylose (Xyl) (Probable).
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 3 family. {ECO:0000305}.
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DR EMBL; HG315671; CDF79935.1; -; Genomic_DNA.
DR RefSeq; WP_038530543.1; NZ_HG315671.1.
DR AlphaFoldDB; T2KMH9; -.
DR SMR; T2KMH9; -.
DR STRING; 1347342.BN863_22230; -.
DR EnsemblBacteria; CDF79935; CDF79935; BN863_22230.
DR PATRIC; fig|1347342.6.peg.2230; -.
DR eggNOG; COG1472; Bacteria.
DR HOGENOM; CLU_004542_5_1_10; -.
DR OMA; PHSNYTH; -.
DR OrthoDB; 419160at2; -.
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; 2.60.40.10; -; 1.
DR Gene3D; 3.20.20.300; -; 1.
DR Gene3D; 3.40.50.1700; -; 1.
DR InterPro; IPR026891; Fn3-like.
DR InterPro; IPR002772; Glyco_hydro_3_C.
DR InterPro; IPR036881; Glyco_hydro_3_C_sf.
DR InterPro; IPR001764; Glyco_hydro_3_N.
DR InterPro; IPR036962; Glyco_hydro_3_N_sf.
DR InterPro; IPR017853; Glycoside_hydrolase_SF.
DR InterPro; IPR013783; Ig-like_fold.
DR Pfam; PF14310; Fn3-like; 1.
DR Pfam; PF00933; Glyco_hydro_3; 1.
DR Pfam; PF01915; Glyco_hydro_3_C; 1.
DR PRINTS; PR00133; GLHYDRLASE3.
DR SMART; SM01217; Fn3_like; 1.
DR SUPFAM; SSF51445; SSF51445; 1.
DR SUPFAM; SSF52279; SSF52279; 1.
DR PROSITE; PS51257; PROKAR_LIPOPROTEIN; 1.
PE 2: Evidence at transcript level;
KW Cell outer membrane; Glycosidase; Hydrolase; Lipoprotein; Membrane;
KW Palmitate; Reference proteome; Signal.
FT SIGNAL 1..18
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00303"
FT CHAIN 19..756
FT /note="Putative beta-xylosidase"
FT /id="PRO_0000448302"
FT LIPID 19
FT /note="N-palmitoyl cysteine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00303"
FT LIPID 19
FT /note="S-diacylglycerol cysteine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00303"
SQ SEQUENCE 756 AA; 83797 MW; 6DA6E6DF6D66D5DA CRC64;
MKKLLFTFLV STGTIFFSCQ RTYTQSKDYK NASLTIEERV DALLPKMSLE EKVAQMRIFH
ANIGVEAEGN GNLKLSDKVI EKLKLGIAGI KNPGEHMDPV AAAKFNNDLQ KYIIENNRWG
IPALFVTESY NGVDAAGSTR FGRPLTSAAS FNPQLVNRIW DVVGREARLR GMHMCHSPEA
DLVRDPRFGR MSEAFGEDTY LTTQMVVNAI NGVQGNYDGL GNGTHIGAVA KHFAGYGQVL
GGSNFAAIEI SPRTLIDEIY PPFEAAVKEA KTLGIMASHG DINGVASHGN PELLTGVLRD
QWGFKGYVVS DSNDIARLFY FMNVAESPEE AAQMGLEAGI DIDLYAEDSY AYLPEMVKKN
PNLEKLIDRS VRRVLRTKFI LGLFDNPYID IEEVKKGVRA NSSLTLAKES DLESIILLKN
ENKILPLNKN KTTKIALLGP LVKDDTKSMF ETVASKHISF VAEKGFHLTD EKGGAPKLLE
RDENAISKMV NMAKNSDLSI LFLGGDEFTS KEAFFNNALG DRATIEPVGA QDELIEKIKA
LGKPVIVVLK HRRTLAINTI SEQADAILDT WDLSEFGDES TARIIFGEVS PSGKLPVTVP
RSIGQIPFHY SMKEINYKKG YLFMEDGPLY PFGYGLSYSN FEYSDIKKSN SEMTKDSEIE
VSVTIKNTGN VKAKEVVQMY IKDVKGSVIR PDKELKGFEK ISLNPGESKK VSFKITPEML
KFTGLKMEKV LESGEYTVMI GTSSVDYKKT SFQLKK
