ID PA1L_PSEAE Reviewed; 122 AA. AC Q05097; DT 01-FEB-1995, integrated into UniProtKB/Swiss-Prot. DT 23-JAN-2007, sequence version 2. DT 27-MAR-2024, entry version 142. DE RecName: Full=PA-I galactophilic lectin; DE Short=PA-IL; DE AltName: Full=Galactose-binding lectin; GN Name=lecA; Synonyms=pa1L; OrderedLocusNames=PA2570; OS Pseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM OS 14847 / LMG 12228 / 1C / PRS 101 / PAO1). OC Bacteria; Pseudomonadota; Gammaproteobacteria; Pseudomonadales; OC Pseudomonadaceae; Pseudomonas. OX NCBI_TaxID=208964; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND PROTEIN SEQUENCE OF 2-31. RC STRAIN=ATCC 33347; RX PubMed=1429650; DOI=10.1016/s0021-9258(18)50050-8; RA Avichezer D., Katcoff D.J., Garber N.C., Gilboa-Garber N.; RT "Analysis of the amino acid sequence of the Pseudomonas aeruginosa RT galactophilic PA-I lectin."; RL J. Biol. Chem. 267:23023-23027(1992). RN [2] RP SEQUENCE REVISION. RX PubMed=8193158; DOI=10.1016/0167-4781(94)90095-7; RA Avichezer D., Gilboa-Garber N., Garber N.C., Katcoff D.J.; RT "Pseudomonas aeruginosa PA-I lectin gene molecular analysis and expression RT in Escherichia coli."; RL Biochim. Biophys. Acta 1218:11-20(1994). RN [3] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RA Winzer K., Falconer C., Diggle S.P., Garber N.C., Camara M., Williams P.; RT "The Pseudomonas aeruginosa lectins PA-1L and PA-2L are controlled by RT quorum sensing and by RpoS."; RL Submitted (JAN-2000) to the EMBL/GenBank/DDBJ databases. RN [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / RC 1C / PRS 101 / PAO1; RX PubMed=10984043; DOI=10.1038/35023079; RA Stover C.K., Pham X.-Q.T., Erwin A.L., Mizoguchi S.D., Warrener P., RA Hickey M.J., Brinkman F.S.L., Hufnagle W.O., Kowalik D.J., Lagrou M., RA Garber R.L., Goltry L., Tolentino E., Westbrock-Wadman S., Yuan Y., RA Brody L.L., Coulter S.N., Folger K.R., Kas A., Larbig K., Lim R.M., RA Smith K.A., Spencer D.H., Wong G.K.-S., Wu Z., Paulsen I.T., Reizer J., RA Saier M.H. Jr., Hancock R.E.W., Lory S., Olson M.V.; RT "Complete genome sequence of Pseudomonas aeruginosa PAO1, an opportunistic RT pathogen."; RL Nature 406:959-964(2000). CC -!- FUNCTION: D-galactose specific lectin. Binds in decreasing order of CC affinity: melibiose, methyl-alpha-D-galactoside, D-galactose, methyl- CC beta-D-galactoside, N-acetyl-D-galactosamine. Similar to plant lectins CC in its selective (carbohydrate-specific) hemagglutinating activity. CC -!- SUBCELLULAR LOCATION: Cytoplasm. Periplasm. Cell surface. Note=Low CC exposure on the cell surface. CC -!- SIMILARITY: Belongs to the LecA/PllA lectin 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; X65933; CAA46728.1; -; Genomic_DNA. DR EMBL; AF229814; AAF70459.1; -; Genomic_DNA. DR EMBL; AE004091; AAG05958.1; -; Genomic_DNA. DR PIR; S45300; S45300. DR RefSeq; NP_251260.1; NC_002516.2. DR RefSeq; WP_003102492.1; NZ_QZGE01000008.1. DR PDB; 1L7L; X-ray; 1.50 A; A=2-122. DR PDB; 1OKO; X-ray; 1.60 A; A/B/C/D=2-122. DR PDB; 1UOJ; X-ray; 2.40 A; A/B/C/D=2-122. DR PDB; 2VXJ; X-ray; 1.90 A; A/B/C/D/E/F/G/H/I/J/K/L/M/N/O/P/Q/R/S/T/U/V/W/X=2-122. DR PDB; 2WYF; X-ray; 2.40 A; A/B/C/D/E/F/G/H=2-122. DR PDB; 3ZYB; X-ray; 2.29 A; A/B/C/D/E/F/G/H=1-122. DR PDB; 3ZYF; X-ray; 1.94 A; A/B/C/D=1-122. DR PDB; 3ZYH; X-ray; 1.50 A; A/B=1-122. DR PDB; 4A6S; X-ray; 2.15 A; A/B/C/D=2-122. DR PDB; 4AL9; X-ray; 1.75 A; A/B/C/D/E/F/G/H=2-122. DR PDB; 4CP9; X-ray; 1.65 A; A/B/C/D=2-122. DR PDB; 4CPB; X-ray; 1.57 A; A/B/C/D=2-122. DR PDB; 4LJH; X-ray; 1.45 A; A/B/C/D=1-122. DR PDB; 4LK6; X-ray; 2.86 A; A/B/C/D/E/F/G/H/I/J/K/L=2-122. DR PDB; 4LK7; X-ray; 1.76 A; A/B/C/D=2-122. DR PDB; 4LKD; X-ray; 2.31 A; A/B/C/D/E/F/G/H=2-122. DR PDB; 4LKE; X-ray; 1.65 A; A/B/C/D=2-122. DR PDB; 4LKF; X-ray; 1.64 A; A/B=2-122. DR PDB; 4YW6; X-ray; 1.40 A; A/B/C/D=2-122. DR PDB; 4YW7; X-ray; 1.82 A; A/B/C/D/E/F/G/H/I/J/K/L/M/N/O/P=2-122. DR PDB; 4YWA; X-ray; 1.19 A; A/B/C/D=2-122. DR PDB; 5D21; X-ray; 1.90 A; A/B/C/D=2-122. DR PDB; 5MIH; X-ray; 1.80 A; A/B/C/D=2-122. DR PDB; 6YO3; X-ray; 1.84 A; A/B/C/D=2-122. DR PDB; 6YOH; X-ray; 1.84 A; A/B/C/D=2-122. DR PDB; 7FIO; X-ray; 1.50 A; A/B/C/D=2-122. DR PDB; 7FJH; X-ray; 1.79 A; A/B/C/D=2-122. DR PDB; 7Z62; X-ray; 1.53 A; AAA/BBB=2-122. DR PDB; 7Z63; X-ray; 1.75 A; AAA/BBB/CCC/DDD=2-122. DR PDB; 8GUV; X-ray; 1.32 A; A/B=2-122. DR PDBsum; 1L7L; -. DR PDBsum; 1OKO; -. DR PDBsum; 1UOJ; -. DR PDBsum; 2VXJ; -. DR PDBsum; 2WYF; -. DR PDBsum; 3ZYB; -. DR PDBsum; 3ZYF; -. DR PDBsum; 3ZYH; -. DR PDBsum; 4A6S; -. DR PDBsum; 4AL9; -. DR PDBsum; 4CP9; -. DR PDBsum; 4CPB; -. DR PDBsum; 4LJH; -. DR PDBsum; 4LK6; -. DR PDBsum; 4LK7; -. DR PDBsum; 4LKD; -. DR PDBsum; 4LKE; -. DR PDBsum; 4LKF; -. DR PDBsum; 4YW6; -. DR PDBsum; 4YW7; -. DR PDBsum; 4YWA; -. DR PDBsum; 5D21; -. DR PDBsum; 5MIH; -. DR PDBsum; 6YO3; -. DR PDBsum; 6YOH; -. DR PDBsum; 7FIO; -. DR PDBsum; 7FJH; -. DR PDBsum; 7Z62; -. DR PDBsum; 7Z63; -. DR PDBsum; 8GUV; -. DR AlphaFoldDB; Q05097; -. DR SMR; Q05097; -. DR STRING; 208964.PA2570; -. DR BindingDB; Q05097; -. DR ChEMBL; CHEMBL3351196; -. DR UniLectin; Q05097; -. DR PaxDb; 208964-PA2570; -. DR GeneID; 882335; -. DR KEGG; pae:PA2570; -. DR PseudoCAP; PA2570; -. DR HOGENOM; CLU_162760_0_0_6; -. DR InParanoid; Q05097; -. DR OrthoDB; 6444532at2; -. DR BioCyc; PAER208964:G1FZ6-2606-MONOMER; -. DR EvolutionaryTrace; Q05097; -. DR PRO; PR:Q05097; -. DR Proteomes; UP000002438; Chromosome. DR GO; GO:0009986; C:cell surface; IEA:UniProtKB-SubCell. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0042597; C:periplasmic space; IEA:UniProtKB-SubCell. DR GO; GO:0030246; F:carbohydrate binding; IEA:UniProtKB-KW. DR GO; GO:0007157; P:heterophilic cell-cell adhesion via plasma membrane cell adhesion molecules; IDA:PseudoCAP. DR Gene3D; 2.60.120.430; Galactose-binding lectin; 1. 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; Galactose-binding domain-like; 1. PE 1: Evidence at protein level; KW 3D-structure; Cytoplasm; Direct protein sequencing; Lectin; Periplasm; KW Reference proteome. FT INIT_MET 1 FT /note="Removed" FT /evidence="ECO:0000269|PubMed:1429650" FT CHAIN 2..122 FT /note="PA-I galactophilic lectin" FT /id="PRO_0000058158" FT STRAND 3..8 FT /evidence="ECO:0007829|PDB:4YWA" FT STRAND 15..21 FT /evidence="ECO:0007829|PDB:4YWA" FT STRAND 27..41 FT /evidence="ECO:0007829|PDB:4YWA" FT STRAND 46..48 FT /evidence="ECO:0007829|PDB:4LKF" FT STRAND 65..70 FT /evidence="ECO:0007829|PDB:4YWA" FT STRAND 81..85 FT /evidence="ECO:0007829|PDB:4YWA" FT STRAND 93..99 FT /evidence="ECO:0007829|PDB:4YWA" FT HELIX 106..108 FT /evidence="ECO:0007829|PDB:4YWA" FT STRAND 110..119 FT /evidence="ECO:0007829|PDB:4YWA" SQ SEQUENCE 122 AA; 12893 MW; 1DC739390388A451 CRC64; MAWKGEVLAN NEAGQVTSII YNPGDVITIV AAGWASYGPT QKWGPQGDRE HPDQGLICHD AFCGALVMKI GNSGTIPVNT GLFRWVAPNN VQGAITLIYN DVPGTYGNNS GSFSVNIGKD QS //