Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

PA-I galactophilic lectin

Gene

lecA

Organism
Pseudomonas aeruginosa (strain ATCC 15692 / PAO1 / 1C / PRS 101 / LMG 12228)
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Experimental evidence at protein leveli

Functioni

D-galactose specific lectin. Binds in decreasing order of affinity: melibiose, methyl-alpha-D-galactoside, D-galactose, methyl-beta-D-galactoside, N-acetyl-D-galactosamine. Similar to plant lectins in its selective (carbohydrate-specific) hemagglutinating activity.

GO - Molecular functioni

  1. carbohydrate binding Source: UniProtKB-KW

GO - Biological processi

  1. heterophilic cell-cell adhesion via plasma membrane cell adhesion molecules Source: PseudoCAP
Complete GO annotation...

Keywords - Ligandi

Lectin

Names & Taxonomyi

Protein namesi
Recommended name:
PA-I galactophilic lectin
Short name:
PA-IL
Alternative name(s):
Galactose-binding lectin
Gene namesi
Name:lecA
Synonyms:pa1L
Ordered Locus Names:PA2570
OrganismiPseudomonas aeruginosa (strain ATCC 15692 / PAO1 / 1C / PRS 101 / LMG 12228)
Taxonomic identifieri208964 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaPseudomonadalesPseudomonadaceaePseudomonas
ProteomesiUP000002438 Componenti: Chromosome

Organism-specific databases

PseudoCAPiPA2570.

Subcellular locationi

Cytoplasm. Periplasm. Cell surface
Note: Low exposure on the cell surface.

GO - Cellular componenti

  1. cell surface Source: UniProtKB-SubCell
  2. cytoplasm Source: UniProtKB-SubCell
  3. periplasmic space Source: UniProtKB-SubCell
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Periplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11Removed1 Publication
Chaini2 – 122121PA-I galactophilic lectinPRO_0000058158Add
BLAST

Interactioni

Protein-protein interaction databases

STRINGi208964.PA2570.

Structurei

Secondary structure

1
122
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi3 – 86Combined sources
Beta strandi15 – 217Combined sources
Beta strandi27 – 4115Combined sources
Beta strandi46 – 483Combined sources
Beta strandi65 – 706Combined sources
Beta strandi81 – 855Combined sources
Beta strandi93 – 997Combined sources
Helixi106 – 1083Combined sources
Beta strandi110 – 11910Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1L7LX-ray1.50A2-122[»]
1OKOX-ray1.60A/B/C/D2-122[»]
1UOJX-ray2.40A/B/C/D2-122[»]
2VXJX-ray1.90A/B/C/D/E/F/G/H/I/J/K/L/M/N/O/P/Q/R/S/T/U/V/W/X2-122[»]
2WYFX-ray2.40A/B/C/D/E/F/G/H2-122[»]
3ZYBX-ray2.29A/B/C/D/E/F/G/H1-122[»]
3ZYFX-ray1.94A/B/C/D1-122[»]
3ZYHX-ray1.50A/B1-122[»]
4A6SX-ray2.15A/B/C/D2-122[»]
4AL9X-ray1.75A/B/C/D/E/F/G/H2-122[»]
4CP9X-ray1.65A/B/C/D2-122[»]
4CPBX-ray1.57A/B/C/D2-122[»]
4LJHX-ray1.45A/B/C/D1-122[»]
4LK6X-ray2.86A/B/C/D/E/F/G/H/I/J/K/L2-122[»]
4LK7X-ray1.76A/B/C/D2-122[»]
4LKDX-ray2.31A/B/C/D/E/F/G/H2-122[»]
4LKEX-ray1.65A/B/C/D2-122[»]
4LKFX-ray1.64A/B2-122[»]
SMRiQ05097. Positions 2-122.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ05097.

Family & Domainsi

Phylogenomic databases

eggNOGiNOG123349.
HOGENOMiHOG000247286.
OMAiIVAKGWI.
OrthoDBiEOG6PZXD0.

Family and domain databases

Gene3Di2.60.120.430. 1 hit.
InterProiIPR008979. Galactose-bd-like.
IPR012905. PA-IL.
[Graphical view]
PfamiPF07828. PA-IL. 1 hit.
[Graphical view]
PIRSFiPIRSF020485. PA-IL. 1 hit.
SUPFAMiSSF49785. SSF49785. 1 hit.

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

Q05097-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MAWKGEVLAN NEAGQVTSII YNPGDVITIV AAGWASYGPT QKWGPQGDRE
60 70 80 90 100
HPDQGLICHD AFCGALVMKI GNSGTIPVNT GLFRWVAPNN VQGAITLIYN
110 120
DVPGTYGNNS GSFSVNIGKD QS
Length:122
Mass (Da):12,893
Last modified:January 23, 2007 - v2
Checksum:i1DC739390388A451
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X65933 Genomic DNA. Translation: CAA46728.1.
AF229814 Genomic DNA. Translation: AAF70459.1.
AE004091 Genomic DNA. Translation: AAG05958.1.
PIRiS45300.
RefSeqiNP_251260.1. NC_002516.2.

Genome annotation databases

EnsemblBacteriaiAAG05958; AAG05958; PA2570.
GeneIDi882335.
KEGGipae:PA2570.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X65933 Genomic DNA. Translation: CAA46728.1.
AF229814 Genomic DNA. Translation: AAF70459.1.
AE004091 Genomic DNA. Translation: AAG05958.1.
PIRiS45300.
RefSeqiNP_251260.1. NC_002516.2.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1L7LX-ray1.50A2-122[»]
1OKOX-ray1.60A/B/C/D2-122[»]
1UOJX-ray2.40A/B/C/D2-122[»]
2VXJX-ray1.90A/B/C/D/E/F/G/H/I/J/K/L/M/N/O/P/Q/R/S/T/U/V/W/X2-122[»]
2WYFX-ray2.40A/B/C/D/E/F/G/H2-122[»]
3ZYBX-ray2.29A/B/C/D/E/F/G/H1-122[»]
3ZYFX-ray1.94A/B/C/D1-122[»]
3ZYHX-ray1.50A/B1-122[»]
4A6SX-ray2.15A/B/C/D2-122[»]
4AL9X-ray1.75A/B/C/D/E/F/G/H2-122[»]
4CP9X-ray1.65A/B/C/D2-122[»]
4CPBX-ray1.57A/B/C/D2-122[»]
4LJHX-ray1.45A/B/C/D1-122[»]
4LK6X-ray2.86A/B/C/D/E/F/G/H/I/J/K/L2-122[»]
4LK7X-ray1.76A/B/C/D2-122[»]
4LKDX-ray2.31A/B/C/D/E/F/G/H2-122[»]
4LKEX-ray1.65A/B/C/D2-122[»]
4LKFX-ray1.64A/B2-122[»]
SMRiQ05097. Positions 2-122.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi208964.PA2570.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAG05958; AAG05958; PA2570.
GeneIDi882335.
KEGGipae:PA2570.

Organism-specific databases

PseudoCAPiPA2570.

Phylogenomic databases

eggNOGiNOG123349.
HOGENOMiHOG000247286.
OMAiIVAKGWI.
OrthoDBiEOG6PZXD0.

Miscellaneous databases

EvolutionaryTraceiQ05097.

Family and domain databases

Gene3Di2.60.120.430. 1 hit.
InterProiIPR008979. Galactose-bd-like.
IPR012905. PA-IL.
[Graphical view]
PfamiPF07828. PA-IL. 1 hit.
[Graphical view]
PIRSFiPIRSF020485. PA-IL. 1 hit.
SUPFAMiSSF49785. SSF49785. 1 hit.
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Analysis of the amino acid sequence of the Pseudomonas aeruginosa galactophilic PA-I lectin."
    Avichezer D., Katcoff D.J., Garber N.C., Gilboa-Garber N.
    J. Biol. Chem. 267:23023-23027(1991) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 2-31.
    Strain: ATCC 33347.
  2. "Pseudomonas aeruginosa PA-I lectin gene molecular analysis and expression in Escherichia coli."
    Avichezer D., Gilboa-Garber N., Garber N.C., Katcoff D.J.
    Biochim. Biophys. Acta 1218:11-20(1993) [PubMed] [Europe PMC] [Abstract]
    Cited for: SEQUENCE REVISION.
  3. "The Pseudomonas aeruginosa lectins PA-1L and PA-2L are controlled by quorum sensing and by RpoS."
    Winzer K., Falconer C., Diggle S.P., Garber N.C., Camara M., Williams P.
    Submitted (DEC-1999) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  4. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: ATCC 15692 / PAO1 / 1C / PRS 101 / LMG 12228.

Entry informationi

Entry nameiPA1L_PSEAE
AccessioniPrimary (citable) accession number: Q05097
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 1, 1995
Last sequence update: January 23, 2007
Last modified: April 1, 2015
This is version 103 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.