P04960 (PLYE1_ERWCH) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Pectate lyase E
EC=4.2.2.2

Gene names

Name:

pelE

Organism

Erwinia chrysanthemi

Taxonomic identifier

556 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Gammaproteobacteria › Enterobacteriales › Enterobacteriaceae › Dickeya

Protein attributes

Sequence length	385 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Involved in maceration and soft-rotting of plant tissue.
Catalytic activity	Eliminative cleavage of (1->4)-alpha-D-galacturonan to give oligosaccharides with 4-deoxy-alpha-D-galact-4-enuronosyl groups at their non-reducing ends.
Cofactor	Binds 1 calcium ion per subunit.
Pathway	Glycan metabolism; pectin degradation; 2-dehydro-3-deoxy-D-gluconate from pectin: step 2/5.
Subcellular location	Secreted.
Miscellaneous	Pectate lyases have been implicated as pathogenicity factors which induce maceration or rotting of plant tissue. PelE is sufficient to induce these effects under laboratory conditions.
Sequence similarities	Belongs to the polysaccharide lyase 1 family. PLBC subfamily.

Ontologies

Keywords
Cellular component	Secreted
Domain	Repeat Signal
Ligand	Calcium Metal-binding
Molecular function	Lyase
Technical term	3D-structure
Gene Ontology (GO)
Cellular component	extracellular region Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular function	metal ion binding Inferred from electronic annotation. Source: UniProtKB-KW pectate lyase activity Inferred from electronic annotation. Source: EC
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Signal peptide	1 – 30	30
	Chain	31 – 385	355	Pectate lyase E		PRO_0000024857
Regions
	Repeat	177 – 182	6	1
	Repeat	213 – 218	6	2
	Region	177 – 218	42	2 X 6 AA approximate repeats
Sites
	Active site	260	1	Potential
	Metal binding	164	1	Calcium By similarity
	Metal binding	207	1	Calcium By similarity

Sequences

	Sequence		Length	Mass (Da)
	P04960 [UniParc]. Last modified August 13, 1987. Version 1. Checksum: 23325AA3D5D810EA	FASTA	385	41,250
	10 20 30 40 50 60 MKNTRVRSIG TKSLLAAVVT AALMATSAYA AVETDAATTG WATQNGGTTG GAKAAKAVEV 70 80 90 100 110 120 KNISDFKKAL NGTDSSAKII KVTGPIDISG GKAYTSFDDQ KARSQISIPS NTTIIGVGSN 130 140 150 160 170 180 GKFTNGSLVI KGVKNVILRN LYIETPVDVA PHYESGDGWN AEWDAAVIDN STNVWVDHVT 190 200 210 220 230 240 ISDGSFTDDK YTTKDGEKYV QHDGALDIKK GSDYVTISYS RFELHDKTIL IGHSDSNGSQ 250 260 270 280 290 300 DSGKLRVTFH NNVFDRVTER APRVRFGSIH AYNNVYLGDV KHSVYPYLYS FGLGTSGSIL 310 320 330 340 350 360 SESNSFTLSN LKSIDGKNPE CSIVKQFNSK VFSDKGSLVN GSTTTKLDTC GLTAYKPTLP 370 380 YKYSAQTMTS SLATSINNNA GYGKL

References

[1]	"Structure of two pectate lyase genes from Erwinia chrysanthemi EC16 and their high-level expression in Escherichia coli." Keen N.T., Tamaki S. J. Bacteriol. 168:595-606(1986) [PubMed: 3536853] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: EC16.
[2]	"Unusual structural features in the parallel beta-helix in pectate lyases." Yoder M.D., Lietzke S.E., Jurnak F. Structure 1:241-251(1993) [PubMed: 8081738] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS).
[3]	"The three-dimensional structure of pectate lyase E, a plant virulence factor from Erwinia chrysanthemi." Lietzke S.E., Yoder M.D., Keen N.T., Jurnak F.A. Plant Physiol. 106:849-862(1994) [PubMed: 12232373] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS).
[4]	"The refined three-dimensional structure of pectate lyase E from Erwinia chrysanthemi at 2.2-A resolution." Lietzke S.E., Scavetta R.D., Yoder M.D., Jurnak F.A. Plant Physiol. 111:73-92(1996) [PubMed: 12226275] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS).
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

M14509 Genomic DNA. Translation: AAA24844.1.

PIR

WZWC6E. A25158.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1PCL	X-ray	2.20	A	31-385	[»]

ProteinModelPortal

P04960.

SMR

P04960. Positions 36-385.

ModBase

Search...

Protein family/group databases

CAZy

PL1. Polysaccharide Lyase Family 1.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Family and domain databases

InterPro

IPR002022. Amb_allergen.
IPR012334. Pectin_lyas_fold.
IPR011050. Pectin_lyase_fold/virulence.
[Graphical view]

Gene3D

G3DSA:2.160.20.10. Pectin_lyas_fold. 1 hit.

Pfam

PF00544. Pec_lyase_C. 1 hit.
[Graphical view]

SMART

SM00656. Amb_all. 1 hit.
[Graphical view]

SUPFAM

SSF51126. Pectin_lyas_like. 1 hit.

ProtoNet

Search...

Entry information

Entry name

PLYE1_ERWCH

Accession

Primary (citable) accession number: P04960

Entry history

Integrated into UniProtKB/Swiss-Prot:	August 13, 1987
Last sequence update:	August 13, 1987
Last modified:	May 31, 2011
This is version 74 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program