Reviewed, UniProtKB/Swiss-Prot P11073 (PELC_ERWCH)

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

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-gluconic acid 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
Cellular component	extracellular region Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular function	calcium 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

1

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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

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)
	P11073-1 [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: 3042750] [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: 8502994] [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: 12226275] [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: 12540845] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS).
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBLGenBankDDBJ

M19411 Genomic DNA. Translation: AAA24849.1.

PIR

WZWC6C. A31091.

3D structure databases

PDBPDBe

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	[»]

ModBase

Search...

Protein family/group databases

CAZy

PL1. Polysaccharide Lyase Family 1.

Enzyme and pathway databases

BRENDA

4.2.2.2. 1459.

Family and domain databases

InterPro

IPR002022. Amb_allergen.
IPR012334. Pectin_lyas_fold.
[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]

ProtoNet

Search...

Entry information

Entry name

PELC_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:	June 16, 2009
This is version 78 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HAMAP (High-quality Automated and Manual Annotation of microbial Proteomes)