ID   PLH2_FORAG              Reviewed;         505 AA.
AC   T2KN63;
DT   16-OCT-2019, integrated into UniProtKB/Swiss-Prot.
DT   13-NOV-2013, sequence version 1.
DT   25-MAY-2022, entry version 28.
DE   RecName: Full=SusD-like protein P2 {ECO:0000303|PubMed:31285597};
DE            Short=P2_SusD {ECO:0000303|PubMed:31285597};
DE   AltName: Full=Polysaccharide utilization locus H protein P2 {ECO:0000303|PubMed:31285597};
DE            Short=PUL H protein P2;
DE   Flags: Precursor;
GN   ORFNames=BN863_21910;
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; CDF79903.1; -; Genomic_DNA.
DR   RefSeq; WP_038530477.1; NZ_HG315671.1.
DR   AlphaFoldDB; T2KN63; -.
DR   SMR; T2KN63; -.
DR   STRING; 1347342.BN863_21910; -.
DR   EnsemblBacteria; CDF79903; CDF79903; BN863_21910.
DR   PATRIC; fig|1347342.6.peg.2198; -.
DR   eggNOG; COG0702; Bacteria.
DR   HOGENOM; CLU_015553_1_4_10; -.
DR   OMA; EAKWVID; -.
DR   OrthoDB; 554994at2; -.
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..17
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00303"
FT   CHAIN           18..505
FT                   /note="SusD-like protein P2"
FT                   /id="PRO_0000448316"
FT   LIPID           18
FT                   /note="N-palmitoyl cysteine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00303"
FT   LIPID           18
FT                   /note="S-diacylglycerol cysteine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00303"
SQ   SEQUENCE   505 AA;  56245 MW;  C52ADCB84357E550 CRC64;
     MKKYKITFIV LLLTLVGCSD LEENPVGILA PESFFKTTAD LQAAINGSYA SMSTESFWGR
     KLTLTLLLRG DLADIGDQGT SGRRKEVNNF TMGDDNGMVS AFWPQAYAII GTANQAISNA
     GLINDDENKV NAVAAQAYFC RAFTYYHLVR LFGDIPYIDF AVSDASEIDA ISKTPENEVY
     EGIIADLQYA KEWLPDTQFS RALPSKATAA AYLASVYLTR GDFQKAAEEA QFVINNEARF
     DLRLEPDFQN LFDANQTAGL KEPLFTIDYM GQISSSGYGQ DYVASVTGIR GDATHEYGEG
     WSVAVPSLKV YQDWDAKDYR RAVSLDTTAT SKSGEVYPYT QFEEYSDLAV NRPHIAKYYR
     YAGLAGNNGR ESSTNYIPMR YAEVLLIAAE ALNEISAGSS EAVSYVNRLR ERARLGSGSM
     HPLNISEGLL QDELRNIIIE ERKIELAFEF KRWYDIKRLK LGNEVFGPNG LEPQPNFDAN
     RDYLLPLPGP ELVRNSNLMP NNPGY