PLH39_FORAG
ID PLH39_FORAG Reviewed; 1038 AA.
AC T2KMI3;
DT 16-OCT-2019, integrated into UniProtKB/Swiss-Prot.
DT 13-NOV-2013, sequence version 1.
DT 25-MAY-2022, entry version 37.
DE RecName: Full=TonB-dependent receptor P39 {ECO:0000303|PubMed:31285597};
DE Short=P39_TBDR {ECO:0000303|PubMed:31285597};
DE AltName: Full=Polysaccharide utilization locus H protein P39 {ECO:0000303|PubMed:31285597};
DE Short=PUL H protein P39;
DE Flags: Precursor;
GN ORFNames=BN863_22280;
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: TonB-dependent receptor 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 TonB-dependent receptor may mediate transport of ulvan
CC oligosaccharides from the surface of the outer membrane to the
CC periplasm for subsequent degradation (By similarity).
CC {ECO:0000250|UniProtKB:Q8A1G2, ECO:0000305|PubMed:31285597}.
CC -!- SUBCELLULAR LOCATION: Cell outer membrane
CC {ECO:0000269|PubMed:31285597}; Multi-pass membrane protein
CC {ECO:0000250|UniProtKB:Q8A1G2}.
CC -!- INDUCTION: By ulvan and rhamnose. {ECO:0000269|PubMed:31285597}.
CC -!- SIMILARITY: Belongs to the TonB-dependent receptor family.
CC {ECO:0000305}.
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DR EMBL; HG315671; CDF79940.1; -; Genomic_DNA.
DR AlphaFoldDB; T2KMI3; -.
DR SMR; T2KMI3; -.
DR STRING; 1347342.BN863_22280; -.
DR EnsemblBacteria; CDF79940; CDF79940; BN863_22280.
DR PATRIC; fig|1347342.6.peg.2235; -.
DR eggNOG; COG4771; Bacteria.
DR HOGENOM; CLU_004317_1_1_10; -.
DR OrthoDB; 71288at2; -.
DR Proteomes; UP000016160; Chromosome.
DR GO; GO:0009279; C:cell outer membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR Gene3D; 2.170.130.10; -; 1.
DR Gene3D; 2.40.170.20; -; 1.
DR InterPro; IPR008969; CarboxyPept-like_regulatory.
DR InterPro; IPR012910; Plug_dom.
DR InterPro; IPR037066; Plug_dom_sf.
DR InterPro; IPR023996; TonB-dep_OMP_SusC/RagA.
DR InterPro; IPR023997; TonB-dep_OMP_SusC/RagA_CS.
DR InterPro; IPR000531; TonB-dep_rcpt_b-brl.
DR InterPro; IPR036942; TonB_rcpt_b-brl_sf.
DR Pfam; PF07715; Plug; 1.
DR Pfam; PF00593; TonB_dep_Rec; 1.
DR SUPFAM; SSF49464; SSF49464; 1.
DR TIGRFAMs; TIGR04056; OMP_RagA_SusC; 1.
DR TIGRFAMs; TIGR04057; SusC_RagA_signa; 1.
PE 2: Evidence at transcript level;
KW Cell outer membrane; Membrane; Receptor; Reference proteome; Signal;
KW TonB box; Transmembrane; Transmembrane beta strand.
FT SIGNAL 1..39
FT /evidence="ECO:0000255"
FT CHAIN 40..1038
FT /note="TonB-dependent receptor P39"
FT /id="PRO_5004591063"
FT MOTIF 120..127
FT /note="TonB box"
FT /evidence="ECO:0000255"
FT MOTIF 1021..1038
FT /note="TonB C-terminal box"
FT /evidence="ECO:0000255"
SQ SEQUENCE 1038 AA; 115935 MW; 256E317B6AA0A8E0 CRC64;
MFKQKLKMKP KIKRNCTFSG LAFILMLLFS SFTVNNLNAQ SEVTGTIMGE DGIPIPGVNV
IQKGTKNGTV TDFDGRYSVT LVPGQLVLVY SYIGYETQEV PIKSRKVIDL TLKAELQSLD
EVVVIGYGEQ KRADVIGAVG SVDSEELSSV SPVDALQGIQ GRVAGVQVTT NGGPGGDSEI
IIRGISTFGA GSSPLYVVDG QQVNDITNIN PADIESMDIL KDGASAAIYG SKSANGVVLI
TTKQGKPGFP KMTVDYISSV SFLNNLVPVS NTRQWNKFES LRTGSTDASG QVEDSLGIRS
QLVVDVQDAI KQLGVKNQVN LAFSGGGEKS KFYWNTGYLD ETGIVKGSGY NRITSNLKID
FDLNKFITAG TRMTGTYQMQ DGINEGSVFR NLSYRQPNVL LVDFDGSYIR ERYARNNPLA
RAELQVNDNR QFSSTIFNYI SVKLAPGLTF KTTLGFNYRN QKLNQFNPQE TVNIDNGKIN
GRERVNTFYD FQNENFFNYN KTFNDKHTVT GLAGFSIQRW WYEYSDLNAI EFNNDYIQTF
NNVKEYNLNT TGTDATTHAL SSLYARIGYD YKSKYLITAS IRRDGSSRFG ENRIWGNFPA
IQLGWKISEE NFMKSLGFIN LLKLRASYAI TGNERIGDFE SIALYNPGFF YNSVNGFAPV
QLGNGDLGWE ETAQQNYGID LSLFKRRLNV SVDRYVKTTD DLLYNVPIPQ ETGFSNIRAN
IGSVENRGWE VSIAAKPIRN ERFTWTTSFN FSYNENEVLE LADEDGFETG GYLIEEGESL
GNMYGYKNLG VFQYDESNAF TPDGIRLTPN FDANQNFVNY TLNGQAYNGD IERLKFANKV
LRGGDIIFQD QNGDFNIDAA NDRTIIGNGL SDFAGGFSNR FDYNGFFFSF LFNYNFGNDI
YRDYDHIRDK ASNAVYAPSP DRIDGAWVNP GDITKYPSLE VSRANNRSGY ESNYVSSADF
ISLRNIQLGY SFNPDTLNKL GFINRLSLNA SINNVFMFTN YEGYNPELGN RGNALEPGWD
SLRYPNQTEI VIGLNVEF