PLH25_FORAG
ID PLH25_FORAG Reviewed; 527 AA.
AC T2KNB8;
DT 16-OCT-2019, integrated into UniProtKB/Swiss-Prot.
DT 13-NOV-2013, sequence version 1.
DT 25-MAY-2022, entry version 30.
DE RecName: Full=SusD-like protein P25 {ECO:0000303|PubMed:31285597};
DE Short=P25_SusD {ECO:0000303|PubMed:31285597};
DE AltName: Full=Polysaccharide utilization locus H protein P25 {ECO:0000303|PubMed:31285597};
DE Short=PUL H protein P25;
DE Flags: Precursor;
GN ORFNames=BN863_22140;
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: Polysaccharide-binding protein probably 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). The SusD-like protein may mediate ulvan oligomer-binding
CC before transport in the periplasm for further degradation (By
CC similarity). {ECO:0000250|UniProtKB:Q8A1G2,
CC ECO:0000305|PubMed:31285597}.
CC -!- SUBCELLULAR LOCATION: Cell outer membrane
CC {ECO:0000269|PubMed:31285597}; Lipid-anchor {ECO:0000255|PROSITE-
CC ProRule:PRU00303}.
CC -!- INDUCTION: By ulvan and rhamnose. {ECO:0000269|PubMed:31285597}.
CC -!- SIMILARITY: Belongs to the SusD family. {ECO:0000305}.
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DR EMBL; HG315671; CDF79926.1; -; Genomic_DNA.
DR RefSeq; WP_038530518.1; NZ_HG315671.1.
DR AlphaFoldDB; T2KNB8; -.
DR SMR; T2KNB8; -.
DR STRING; 1347342.BN863_22140; -.
DR EnsemblBacteria; CDF79926; CDF79926; BN863_22140.
DR PATRIC; fig|1347342.6.peg.2221; -.
DR eggNOG; COG0702; Bacteria.
DR HOGENOM; CLU_015553_1_1_10; -.
DR OMA; WELAGEC; -.
DR OrthoDB; 233664at2; -.
DR Proteomes; UP000016160; Chromosome.
DR GO; GO:0009279; C:cell outer membrane; IEA:UniProtKB-SubCell.
DR InterPro; IPR033985; SusD-like_N.
DR InterPro; IPR012944; SusD_RagB_dom.
DR InterPro; IPR011990; TPR-like_helical_dom_sf.
DR Pfam; PF14322; SusD-like_3; 1.
DR Pfam; PF07980; SusD_RagB; 1.
DR SUPFAM; SSF48452; SSF48452; 1.
PE 2: Evidence at transcript level;
KW Cell outer membrane; Lipoprotein; Membrane; Palmitate; Reference proteome;
KW Signal.
FT SIGNAL 1..15
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00303"
FT CHAIN 16..527
FT /note="SusD-like protein P25"
FT /id="PRO_0000448317"
FT LIPID 16
FT /note="N-palmitoyl cysteine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00303"
FT LIPID 16
FT /note="S-diacylglycerol cysteine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00303"
SQ SEQUENCE 527 AA; 60269 MW; 134048A15AD8013A CRC64;
MKIQNIIVYV FLIFSCFSCE EFLEEDPRAL IAPETFYQSE SDVRQAVVGL YSILKNNSIY
GQLGLDLFYD NGADIIEPNR STNVVEPLGN YSLNEAIADV SVQKMSVSDT WKDLYRVIYN
ANIILDNVDG NDAISEEAQI DIMAEVKFIR ALCYWHIVNL WGDAPFYTEP LVLEEIRVLG
RTDEDTILST VVSDLQYAQV HLASVYPEED RGRASKWAAA IVEAKIHMQE QNWQAGLNKC
MEIISQSPHS LLGNYADVFN PNNEYNSEII WSLDFAKDIR GQFEEGTLGA DGSFPSVFGN
GNWRPSMFAP RLRDEPKNSS ERNALAAALQ ANGEAFNGTG LQVASKDFAG KFPRNDYRRA
LNIVDNYLGF DLNFPYMAKI WNLDVDNSPR FNHSDNRIVF RLADVYLMAA ECENELNGPA
NAFQYINKVR ERAFATQTEW ELKGLDQQGF REAIYDERKW ELAGECHRRY DLIRWGILLD
VVQDLEYRFW TPNTNIRPYH VKLPIPLQEL QVNPVLLESD ATNNGYR