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PLLA_PHOLL
ID   PLLA_PHOLL              Reviewed;         122 AA.
AC   Q7N561;
DT   31-JAN-2018, integrated into UniProtKB/Swiss-Prot.
DT   15-DEC-2003, sequence version 1.
DT   03-AUG-2022, entry version 89.
DE   RecName: Full=Lectin A {ECO:0000303|PubMed:28972138};
DE   AltName: Full=Alpha-galactoside-binding lectin {ECO:0000305|PubMed:28972138};
DE   AltName: Full=Galactose-binding lectin PllA {ECO:0000303|PubMed:28972138};
GN   Name=pllA {ECO:0000303|PubMed:28972138};
GN   OrderedLocusNames=plu2096 {ECO:0000312|EMBL:CAE14389.1};
OS   Photorhabdus laumondii subsp. laumondii (strain DSM 15139 / CIP 105565 /
OS   TT01).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Morganellaceae; Photorhabdus.
OX   NCBI_TaxID=243265;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 15139 / CIP 105565 / TT01;
RX   PubMed=14528314; DOI=10.1038/nbt886;
RA   Duchaud E., Rusniok C., Frangeul L., Buchrieser C., Givaudan A.,
RA   Taourit S., Bocs S., Boursaux-Eude C., Chandler M., Charles J.-F.,
RA   Dassa E., Derose R., Derzelle S., Freyssinet G., Gaudriault S., Medigue C.,
RA   Lanois A., Powell K., Siguier P., Vincent R., Wingate V., Zouine M.,
RA   Glaser P., Boemare N., Danchin A., Kunst F.;
RT   "The genome sequence of the entomopathogenic bacterium Photorhabdus
RT   luminescens.";
RL   Nat. Biotechnol. 21:1307-1313(2003).
RN   [2] {ECO:0007744|PDB:5ODU, ECO:0007744|PDB:5OFI, ECO:0007744|PDB:5OFX, ECO:0007744|PDB:5OFZ}
RP   X-RAY CRYSTALLOGRAPHY (1.56 ANGSTROMS) OF APOPROTEIN AND IN COMPLEX WITH
RP   VARIOUS CARBOHYDRATES, FUNCTION, CARBOHYDRATE SPECIFICITY, BIOTECHNOLOGY,
RP   AND SUBUNIT.
RC   STRAIN=DSM 15139 / CIP 105565 / TT01;
RX   PubMed=28972138; DOI=10.1074/jbc.m117.812792;
RA   Beshr G., Sikandar A., Jemiller E.M., Klymiuk N., Hauck D., Wagner S.,
RA   Wolf E., Koehnke J., Titz A.;
RT   "Photorhabdus luminescens lectin A (PllA) - a new probe for detecting
RT   alpha-galactoside-terminating glycoconjugates.";
RL   J. Biol. Chem. 292:19935-19951(2017).
CC   -!- FUNCTION: Lectin that specifically binds alpha-galactoside-terminating
CC       glycoconjugates. Shows high apparent binding to the alpha-Gal epitope
CC       (Gal-alpha-1,3-Gal-beta-1,4-GlcNAc terminating glycans) as well as to
CC       Gal-alpha-1,4-GlcNAc and Gal-alpha-1,3-GalNAc. Gal-alpha-1,3-GalNAc may
CC       be one natural ligand bound by PllA both in the nematode symbiont and
CC       in infected insects. {ECO:0000269|PubMed:28972138}.
CC   -!- SUBUNIT: Homotetramer. {ECO:0000269|PubMed:28972138}.
CC   -!- BIOTECHNOLOGY: Can be used as a fluorescent probe for the specific
CC       detection and visualization of the alpha-Gal epitope present on porcine
CC       tissues. This epitope is mainly responsible for hyperacute rejection of
CC       porcine organ transplants in humans during xenotransplantation.
CC       {ECO:0000269|PubMed:28972138}.
CC   -!- SIMILARITY: Belongs to the LecA/PllA lectin family. {ECO:0000305}.
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DR   EMBL; BX571866; CAE14389.1; -; Genomic_DNA.
DR   RefSeq; WP_011146351.1; NC_005126.1.
DR   PDB; 5ODU; X-ray; 1.56 A; A/B/C/D/E/F/G/H=1-122.
DR   PDB; 5OFI; X-ray; 2.00 A; A/B/C/D/E/F/G/H=1-122.
DR   PDB; 5OFX; X-ray; 1.75 A; A/B/C/D/E/F/G/H=1-122.
DR   PDB; 5OFZ; X-ray; 1.75 A; A/B/C/D=1-122.
DR   PDBsum; 5ODU; -.
DR   PDBsum; 5OFI; -.
DR   PDBsum; 5OFX; -.
DR   PDBsum; 5OFZ; -.
DR   AlphaFoldDB; Q7N561; -.
DR   SMR; Q7N561; -.
DR   STRING; 243265.plu2096; -.
DR   UniLectin; Q7N561; -.
DR   EnsemblBacteria; CAE14389; CAE14389; plu2096.
DR   GeneID; 24166541; -.
DR   KEGG; plu:plu2096; -.
DR   eggNOG; ENOG50330FC; Bacteria.
DR   HOGENOM; CLU_162760_0_0_6; -.
DR   OMA; KIESRYD; -.
DR   OrthoDB; 1831069at2; -.
DR   BioCyc; PLUM243265:PLU_RS10475-MON; -.
DR   Proteomes; UP000002514; Chromosome.
DR   GO; GO:0030246; F:carbohydrate binding; IEA:UniProtKB-KW.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   InterPro; IPR008979; Galactose-bd-like_sf.
DR   InterPro; IPR012905; PA-IL.
DR   Pfam; PF07828; PA-IL; 1.
DR   PIRSF; PIRSF020485; PA-IL; 1.
DR   SUPFAM; SSF49785; SSF49785; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Calcium; Lectin; Metal-binding; Reference proteome.
FT   CHAIN           1..122
FT                   /note="Lectin A"
FT                   /id="PRO_0000443107"
FT   BINDING         38
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /evidence="ECO:0000269|PubMed:28972138,
FT                   ECO:0007744|PDB:5ODU"
FT   BINDING         44
FT                   /ligand="an alpha-D-galactoside"
FT                   /ligand_id="ChEBI:CHEBI:46953"
FT                   /evidence="ECO:0000269|PubMed:28972138,
FT                   ECO:0007744|PDB:5ODU"
FT   BINDING         57
FT                   /ligand="an alpha-D-galactoside"
FT                   /ligand_id="ChEBI:CHEBI:46953"
FT                   /evidence="ECO:0000269|PubMed:28972138,
FT                   ECO:0007744|PDB:5ODU"
FT   BINDING         96
FT                   /ligand="an alpha-D-galactoside"
FT                   /ligand_id="ChEBI:CHEBI:46953"
FT                   /evidence="ECO:0000269|PubMed:28972138,
FT                   ECO:0007744|PDB:5ODU"
FT   BINDING         96
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /evidence="ECO:0000269|PubMed:28972138,
FT                   ECO:0007744|PDB:5ODU"
FT   BINDING         100
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /evidence="ECO:0000269|PubMed:28972138,
FT                   ECO:0007744|PDB:5ODU"
FT   BINDING         103
FT                   /ligand="an alpha-D-galactoside"
FT                   /ligand_id="ChEBI:CHEBI:46953"
FT                   /evidence="ECO:0000269|PubMed:28972138,
FT                   ECO:0007744|PDB:5ODU"
FT   BINDING         103
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /evidence="ECO:0000269|PubMed:28972138,
FT                   ECO:0007744|PDB:5ODU"
FT   BINDING         104
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /evidence="ECO:0000269|PubMed:28972138,
FT                   ECO:0007744|PDB:5ODU"
FT   STRAND          4..9
FT                   /evidence="ECO:0007829|PDB:5ODU"
FT   STRAND          16..22
FT                   /evidence="ECO:0007829|PDB:5ODU"
FT   STRAND          27..33
FT                   /evidence="ECO:0007829|PDB:5ODU"
FT   STRAND          36..41
FT                   /evidence="ECO:0007829|PDB:5ODU"
FT   STRAND          45..47
FT                   /evidence="ECO:0007829|PDB:5ODU"
FT   TURN            59..62
FT                   /evidence="ECO:0007829|PDB:5ODU"
FT   STRAND          63..68
FT                   /evidence="ECO:0007829|PDB:5ODU"
FT   STRAND          71..74
FT                   /evidence="ECO:0007829|PDB:5ODU"
FT   STRAND          78..83
FT                   /evidence="ECO:0007829|PDB:5ODU"
FT   STRAND          88..94
FT                   /evidence="ECO:0007829|PDB:5ODU"
FT   HELIX           101..103
FT                   /evidence="ECO:0007829|PDB:5ODU"
FT   STRAND          105..116
FT                   /evidence="ECO:0007829|PDB:5ODU"
SQ   SEQUENCE   122 AA;  12958 MW;  E2DF54B97D8F1461 CRC64;
     MSDWSGSVPA NAENGKSTGL ILKQGDTISV VAHGWVKYGR DNVEWAAPDG PVPNNPQPSS
     IATLVAKIAN KKFAIGNGVL HKTVPVDGEL ILLFNDVPGT FGDNSGEFQV EVIIESRYSP
     LK
 
 
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