ID   PLH38_FORAG             Reviewed;         503 AA.
AC   T2KPM5;
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=SusD-like protein P38 {ECO:0000303|PubMed:31285597};
DE            Short=P38_SusD {ECO:0000303|PubMed:31285597};
DE   AltName: Full=Polysaccharide utilization locus H protein P38 {ECO:0000303|PubMed:31285597};
DE            Short=PUL H protein P38;
DE   Flags: Precursor;
GN   ORFNames=BN863_22270;
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}.
CC   -!- INDUCTION: By ulvan and rhamnose. {ECO:0000269|PubMed:31285597}.
CC   -!- SIMILARITY: Belongs to the SusD family. {ECO:0000305}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; HG315671; CDF79939.1; -; Genomic_DNA.
DR   RefSeq; WP_038530552.1; NZ_HG315671.1.
DR   AlphaFoldDB; T2KPM5; -.
DR   SMR; T2KPM5; -.
DR   STRING; 1347342.BN863_22270; -.
DR   EnsemblBacteria; CDF79939; CDF79939; BN863_22270.
DR   PATRIC; fig|1347342.6.peg.2234; -.
DR   eggNOG; COG0702; Bacteria.
DR   HOGENOM; CLU_015553_1_4_10; -.
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; Coiled coil; Membrane; Reference proteome; Signal.
FT   SIGNAL          1..21
FT                   /evidence="ECO:0000255"
FT   CHAIN           22..503
FT                   /note="SusD-like protein P38"
FT                   /id="PRO_5004602767"
SQ   SEQUENCE   503 AA;  57949 MW;  E26E68E767FA8B9D CRC64;
     MKKFKNISIT FLILISLGVL NSCESVLEVE PESSISDEQF WKTNEDAKLG LAAAYDALQK
     AYRTKRFYWG EFRADNYVNS EKPQPDTQDL INNNLTPESS TEYLQWDEFY SLIFRANLAI
     EKIPEIPYYD TQYLGEAYAL RAFAYFDAYR VWGGVPLFTK AELTFSDDAI KPRSSAQEVL
     DLVLSDIEEA EKNLTVVSSD YTFSKLSLLA FKAQVHMYLN EYEAANTALT SLIASNQFSL
     TTNRKQWRDL FLNDEINYPG EGQEGPELIM SIRYDFEEDG NRASGIYQVF FPGVPSYYVA
     PNLVEEWETK FPTDSTAWAT KYPNVPPHVF EENEDTGELN AKYGDYRYYE SIAAPGTQEE
     DLRISKYHKV NISPSIDDTN IILFRYADML LLKAEALNQL GQPTEAIELV NQIREARELP
     LVNSGTIPDV VNINDKDELE DFILSERRLE LLAEGYRWWD LVRTNKAVEV MGPINGLTQD
     RIIWPLWFRH LIDNPKLEQN VPY