PLH7_FORAG
ID PLH7_FORAG Reviewed; 395 AA.
AC T2KN67;
DT 16-OCT-2019, integrated into UniProtKB/Swiss-Prot.
DT 16-OCT-2019, sequence version 2.
DT 25-MAY-2022, entry version 20.
DE RecName: Full=Uncharacterized protein P7 {ECO:0000303|PubMed:31285597};
DE AltName: Full=Polysaccharide utilization locus H protein P7 {ECO:0000303|PubMed:31285597};
DE Short=PUL H protein P7;
DE Flags: Precursor;
GN ORFNames=BN863_21960;
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 REVISION OF GENE MODEL.
RX DOI=10.1016/j.algal.2017.09.025;
RA Salinas A., French C.E.;
RT "The enzymatic ulvan depolymerisation system from the alga-associated
RT marine flavobacterium Formosa agariphila.";
RL Algal Res. 27:335-344(2017).
RN [3]
RP FUNCTION, AND SUBCELLULAR LOCATION.
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: May be involved in ulvan degradation (Probable). Ulvan is the
CC main polysaccharide component of the Ulvales (green seaweed) cell wall.
CC It is composed of disaccharide building blocks comprising 3-sulfated
CC rhamnose (Rha3S) linked to D-glucuronic acid (GlcA), L-iduronic acid
CC (IduA), or D-xylose (Xyl) (Probable). {ECO:0000305|PubMed:31285597}.
CC -!- SUBCELLULAR LOCATION: Cell outer membrane
CC {ECO:0000269|PubMed:31285597}; Lipid-anchor {ECO:0000255|PROSITE-
CC ProRule:PRU00303}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CDF79908.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305|Ref.2};
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DR EMBL; HG315671; CDF79908.1; ALT_INIT; Genomic_DNA.
DR AlphaFoldDB; T2KN67; -.
DR STRING; 1347342.BN863_21960; -.
DR EnsemblBacteria; CDF79908; CDF79908; BN863_21960.
DR PATRIC; fig|1347342.6.peg.2203; -.
DR eggNOG; COG4677; Bacteria.
DR HOGENOM; CLU_696291_0_0_10; -.
DR Proteomes; UP000016160; Chromosome.
DR GO; GO:0009279; C:cell outer membrane; IEA:UniProtKB-SubCell.
DR InterPro; IPR032342; DUF4861.
DR Pfam; PF16153; DUF4861; 1.
DR PROSITE; PS51257; PROKAR_LIPOPROTEIN; 1.
PE 3: Inferred from homology;
KW Cell outer membrane; Lipoprotein; Membrane; Palmitate; Reference proteome;
KW Signal.
FT SIGNAL 1..18
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00303"
FT CHAIN 19..395
FT /note="Uncharacterized protein P7"
FT /id="PRO_0000448318"
FT LIPID 19
FT /note="N-palmitoyl cysteine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00303"
FT LIPID 19
FT /note="S-diacylglycerol cysteine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00303"
SQ SEQUENCE 395 AA; 44858 MW; B0397E0366318F85 CRC64;
MKHVIMLYFI AAATLFSSCA KQDSEHRLIT VKNSLDLPRA FETIEISKSD IQLHTGERFE
DFSIQDVATK AILTSQFVDE DQDGTADVLL FQPELNPNSE KQFELVKVDG GVEVDSTVYC
YSRFVPERTD DYTWENNKVA FRTYGPVAQK MVEDSLPGGT LSSGIDAWLK KVEYSIIDNW
YAKNDKDPGY YHIDHGEGLD NFHVGSSRGV GGSAVKVDTS YYISKNFTDY KTITTGPIRT
SFILKYADWD ANEKTISEEK HISLDYGNNF SRFEIHVDGT DELSVGLTLH DNKGEITQNV
DQGWIAYWES EYFDSELGTA IVAPKGVMTA SEYYVTSMKD RSNLYAQLNV DNNKVVYYAG
FAWKESKQYP TKASWEKYIQ EFSEKLNTPL EVSIQ