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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
 
 
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