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Database: UniProt
Entry: A0A1I7PHX3_9BACT
LinkDB: A0A1I7PHX3_9BACT
Original site: A0A1I7PHX3_9BACT 
ID   A0A1I7PHX3_9BACT        Unreviewed;       174 AA.
AC   A0A1I7PHX3;
DT   18-JAN-2017, integrated into UniProtKB/TrEMBL.
DT   18-JAN-2017, sequence version 1.
DT   27-MAR-2024, entry version 25.
DE   SubName: Full=Di-glucose binding within endoplasmic reticulum {ECO:0000313|EMBL:AOS43221.1};
GN   ORFNames=Verru16b_00264 {ECO:0000313|EMBL:AOS43221.1};
OS   Lacunisphaera limnophila.
OC   Bacteria; Verrucomicrobiota; Opitutae; Opitutales; Opitutaceae;
OC   Lacunisphaera.
OX   NCBI_TaxID=1838286 {ECO:0000313|EMBL:AOS43221.1, ECO:0000313|Proteomes:UP000095228};
RN   [1] {ECO:0000313|EMBL:AOS43221.1, ECO:0000313|Proteomes:UP000095228}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=IG16b {ECO:0000313|EMBL:AOS43221.1,
RC   ECO:0000313|Proteomes:UP000095228};
RA   Rast P., Gloeckner I., Jogler M., Boedeker C., Jeske O., Wiegand S.,
RA   Reinhardt R., Schumann P., Rohde M., Spring S., Gloeckner F.O., Jogler C.;
RT   "Three novel species with peptidoglycan cell walls form the new genus
RT   Lacunisphaera gen. nov. in the family Opitutaceae of the verrucomicrobial
RT   subdivision 4.";
RL   Submitted (JUN-2016) to the EMBL/GenBank/DDBJ databases.
CC   -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC       {ECO:0000256|ARBA:ARBA00004115}; Single-pass type I membrane protein
CC       {ECO:0000256|ARBA:ARBA00004115}.
CC   -!- SIMILARITY: Belongs to the malectin family.
CC       {ECO:0000256|ARBA:ARBA00009141}.
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DR   EMBL; CP016094; AOS43221.1; -; Genomic_DNA.
DR   RefSeq; WP_069960597.1; NZ_CP016094.1.
DR   AlphaFoldDB; A0A1I7PHX3; -.
DR   STRING; 1838286.Verru16b_00264; -.
DR   KEGG; obg:Verru16b_00264; -.
DR   OrthoDB; 194430at2; -.
DR   Proteomes; UP000095228; Chromosome.
DR   GO; GO:0030246; F:carbohydrate binding; IEA:InterPro.
DR   GO; GO:0005975; P:carbohydrate metabolic process; IEA:UniProtKB-KW.
DR   Gene3D; 2.60.120.430; Galactose-binding lectin; 1.
DR   InterPro; IPR008979; Galactose-bd-like_sf.
DR   InterPro; IPR021720; Malectin_dom.
DR   InterPro; IPR039155; MLEC.
DR   PANTHER; PTHR13460:SF0; MALECTIN; 1.
DR   PANTHER; PTHR13460; UNCHARACTERIZED; 1.
DR   Pfam; PF11721; Malectin; 1.
DR   SUPFAM; SSF49785; Galactose-binding domain-like; 1.
PE   3: Inferred from homology;
KW   Carbohydrate metabolism {ECO:0000256|ARBA:ARBA00023277};
KW   Endoplasmic reticulum {ECO:0000256|ARBA:ARBA00022824};
KW   Membrane {ECO:0000256|ARBA:ARBA00023136};
KW   Reference proteome {ECO:0000313|Proteomes:UP000095228};
KW   Signal {ECO:0000256|SAM:SignalP};
KW   Transmembrane {ECO:0000256|ARBA:ARBA00022692};
KW   Transmembrane helix {ECO:0000256|ARBA:ARBA00022989}.
FT   SIGNAL          1..24
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           25..174
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5009304132"
FT   DOMAIN          29..167
FT                   /note="Malectin"
FT                   /evidence="ECO:0000259|Pfam:PF11721"
SQ   SEQUENCE   174 AA;  18587 MW;  4870E4AE219AA161 CRC64;
     MSLTTPARTL LASLALALVG PALAADAIRI RAGTTQDHTD ESGVVWLADQ GFSGGDTIDR
     TGLKVAKTST PSIYTTERYG MGGFSRALAN GKYTVKLHFA ETYEGIYGKG ERVFSFNVEG
     KEFKDFDVTA RAGAVLTAYV ETVEVEVTDG KLDITFTSQI ENPEINALEI IPAG
//
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