P11073 (PLYC_ERWCH) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Pectate lyase C
EC=4.2.2.2

Gene names

Name:

pelC

Organism

Erwinia chrysanthemi

Taxonomic identifier

556 [NCBI]

Taxonomic lineage

cellular organisms › Bacteria › Proteobacteria › Gammaproteobacteria › Enterobacteriales › Enterobacteriaceae › Dickeya

Protein attributes

Sequence length	375 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.
Sequence similarities	Belongs to the polysaccharide lyase 1 family. PLADES subfamily.

Ontologies

Keywords
Biological process	Virulence
Cellular component	Secreted
Domain	Signal
Ligand	Calcium Metal-binding
Molecular function	Lyase
PTM	Disulfide bond
Technical term	3D-structure
Gene Ontology (GO)
Biological_process	pathogenesis Inferred from electronic annotation. Source: UniProtKB-KW pectin catabolic process Inferred from electronic annotation. Source: UniProtKB-UniPathway
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 – 22

22

Chain

23 – 375

353

Pectate lyase C

PRO_0000024854

Sites

Active site

240

1

Potential

Metal binding

151

1

Calcium

Metal binding

153

1

Calcium

Metal binding

188

1

Calcium

Metal binding

192

1

Calcium

Amino acid modifications

Disulfide bond

94 ↔ 177

Disulfide bond

351 ↔ 374

Secondary structure

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375

Helix Strand Turn

Details...

Beta strand

27 – 29

3

Beta strand

41 – 47

7

Helix

48 – 57

10

Beta strand

74 – 78

5

Helix

83 – 90

8

Helix

93 – 95

3

Turn

96 – 98

3

Beta strand

103 – 109

7

Beta strand

113 – 117

5

Beta strand

123 – 131

9

Beta strand

134 – 139

6

Beta strand

141 – 144

4

Helix

148 – 150

3

Beta strand

154 – 159

6

Beta strand

162 – 167

6

Beta strand

169 – 171

3

Helix

181 – 183

3

Beta strand

190 – 196

7

Beta strand

199 – 204

6

Beta strand

206 – 212

7

Beta strand

215 – 219

5

Beta strand

226 – 231

6

Beta strand

233 – 239

7

Beta strand

243 – 253

11

Beta strand

255 – 261

7

Beta strand

263 – 267

5

Beta strand

271 – 276

6

Beta strand

278 – 288

11

Beta strand

290 – 294

5

Beta strand

297 – 302

6

Helix

310 – 314

5

Helix

349 – 355

7

Helix

356 – 358

3

Beta strand

360 – 364

5

Helix

371 – 373

3

Sequences

	Sequence		Length	Mass (Da)
	P11073 [UniParc]. Last modified July 1, 1989. Version 1. Checksum: F76DD8195A35B886	FASTA	375	39,944
	10 20 30 40 50 60 MKSLITPITA GLLLALSQPL LAATDTGGYA ATAGGNVTGA VSKTATSMQD IVNIIDAARL 70 80 90 100 110 120 DANGKKVKGG AYPLVITYTG NEDSLINAAA ANICGQWSKD PRGVEIKEFT KGITIIGANG 130 140 150 160 170 180 SSANFGIWIK KSSDVVVQNM RIGYLPGGAK DGDMIRVDDS PNVWVDHNEL FAANHECDGT 190 200 210 220 230 240 PDNDTTFESA VDIKGASNTV TVSYNYIHGV KKVGLDGSSS SDTGRNITYH HNYYNDVNAR 250 260 270 280 290 300 LPLQRGGLVH AYNNLYTNIT GSGLNVRQNG QALIENNWFE KAINPVTSRY DGKNFGTWVL 310 320 330 340 350 360 KGNNITKPAD FSTYSITWTA DTKPYVNADS WTSTGTFPTV AYNYSPVSAQ CVKDKLPGYA 370 GVGKNLATLT STACK

References

[1]	"Structure and organization of the pel genes from Erwinia chrysanthemi EC16." Tamaki S.J., Gold S., Robeson M., Manulis S., Keen N.T. J. Bacteriol. 170:3468-3478(1988) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: EC16.
[2]	"New domain motif: the structure of pectate lyase C, a secreted plant virulence factor." Yoder M.D., Keen N.T., Jurnak F. Science 260:1503-1507(1993) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS).
[3]	"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] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS).
[4]	"Characterization and implications of Ca2+ binding to pectate lyase C." Herron S.R., Scavetta R.D., Garrett M., Legner M., Jurnak F. J. Biol. Chem. 278:12271-12277(2003) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS).
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

M19411 Genomic DNA. Translation: AAA24849.1.

PIR

WZWC6C. A31091.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1AIR	X-ray	2.20	A	23-375	[»]
1O88	X-ray	2.20	A	23-375	[»]
1O8D	X-ray	2.20	A	23-375	[»]
1O8E	X-ray	2.20	A	23-375	[»]
1O8F	X-ray	2.20	A	23-375	[»]
1O8G	X-ray	2.20	A	23-375	[»]
1O8H	X-ray	2.20	A	23-375	[»]
1O8I	X-ray	2.20	A	23-375	[»]
1O8J	X-ray	2.20	A	23-375	[»]
1O8K	X-ray	2.20	A	23-375	[»]
1O8L	X-ray	2.20	A	23-375	[»]
1O8M	X-ray	2.20	A	23-375	[»]
1PLU	X-ray	2.20	A	23-375	[»]
2EWE	X-ray	2.20	A	23-375	[»]
2PEC	X-ray	2.20	A	23-375	[»]

ProteinModelPortal

P11073.

SMR

P11073. Positions 23-374.

ModBase

Search...

Protein family/group databases

CAZy

PL1. Polysaccharide Lyase Family 1.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Enzyme and pathway databases

UniPathway

UPA00545; UER00824.

Family and domain databases

Gene3D

2.160.20.10. 1 hit.

InterPro

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

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...

Other

EvolutionaryTrace

P11073.

Entry information

Entry name

PLYC_ERWCH

Accession

Primary (citable) accession number: P11073

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 1, 1989
Last sequence update:	July 1, 1989
Last modified:	April 3, 2013
This is version 94 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program