Pectate lyase 2 precursor - Erwinia carotovora subsp. atroseptica

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Reviewed, UniProtKB/Swiss-Prot Q6CZT3 (PEL2_ERWCT)

Last modified January 19, 2010. Version 38. History...

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Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

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Names and origin

Protein names

Recommended name:
    Pectate lyase 2
    EC=4.2.2.2
Alternative name(s):
    Pectate lyase II
      Short name=PEL II
    Pectate lyase B
      Short name=PLB

Gene names

Name:	pel2
Synonyms:	pelB
Ordered Locus Names:	ECA4068

Organism

Erwinia carotovora subsp. atroseptica (Pectobacterium atrosepticum) [Complete proteome] [HAMAP]

Taxonomic identifier

29471 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Gammaproteobacteria › Enterobacteriales › Enterobacteriaceae › Pectobacterium

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Protein attributes

Sequence length	374 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level.

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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 By similarity.
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.

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Ontologies

Keywords
Cellular component	Secreted
Domain	Signal
Ligand	Calcium Metal-binding
Molecular function	Lyase
PTM	Disulfide bond
Technical term	Complete proteome Direct protein sequencing
Gene Ontology (GO)
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...

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Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Signal peptide

1 – 22

Chain

23 – 374

352

Pectate lyase 2

PRO_0000234449

Sites

Active site

239

Potential

Metal binding

150

Calcium By similarity

Metal binding

152

Calcium By similarity

Metal binding

187

Calcium By similarity

Metal binding

191

Calcium By similarity

Amino acid modifications

Disulfide bond

93 ↔ 176

By similarity

Disulfide bond

350 ↔ 373

By similarity

Experimental info

Sequence conflict

T → A in AAA24848. Ref.1

Sequence conflict

T → A in CAA57440. Ref.2

Sequence conflict

V → M in AAA24848. Ref.1

Sequence conflict

V → M in CAA57440. Ref.2

Sequence conflict

E → D in AAA24848. Ref.1

Sequence conflict

T → V in AAA24848. Ref.1

Sequence conflict

T → V in CAA57440. Ref.2

Sequence conflict

47 – 48

LQ → MK in CAA57440. Ref.2

Sequence conflict

K → Q in CAA57440. Ref.2

Sequence conflict

N → S in CAA57440. Ref.2

Sequence conflict

115

L → Q in AAA24848. Ref.1

Sequence conflict

115

L → Q in CAA57440. Ref.2

Sequence conflict

133

D → N in AAA24848. Ref.1

Sequence conflict

133

D → N in CAA57440. Ref.2

Sequence conflict

136

V → L in CAA57440. Ref.2

Sequence conflict

139

M → I in CAA57440. Ref.2

Sequence conflict

144

M → I in CAA57440. Ref.2

Sequence conflict

150

D → H in CAA57440. Ref.2

Sequence conflict

156

V → I in CAA57440. Ref.2

Sequence conflict

168

E → K in AAA24848. Ref.1

Sequence conflict

172 – 173

KN → QS in AAA24848. Ref.1

Sequence conflict

234

R → S in CAA57440. Ref.2

Sequence conflict

252

N → T in AAA24848. Ref.1

Sequence conflict

280

N → I in AAA24848. Ref.1

Sequence conflict

304

V → I in AAA24848. Ref.1

Sequence conflict

304

V → I in CAA57440. Ref.2

Sequence conflict

314

N → K in CAA57440. Ref.2

Sequence conflict

319

R → K in CAA57440. Ref.2

Sequence conflict

322

T → S in CAA57440. Ref.2

Sequence conflict

325

V → I in CAA57440. Ref.2

Sequence conflict

332

N → S in AAA24848. Ref.1

Sequence conflict

332

N → S in CAA57440. Ref.2

Sequence conflict

338 – 339

SI → AV in CAA57440. Ref.2

Sequence conflict

344

S → T Ref.1

Sequence conflict

344

S → T Ref.2

Sequence conflict

362

S → G Ref.1

Sequence conflict

362

S → G Ref.2

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Sequences

Sequence

Length

Mass (Da)

Tools

Q6CZT3-1 [UniParc].

Last modified August 16, 2004. Version 1.
Checksum: 2F8C41B4C30DA91B
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FASTA

374

40,446

        10         20         30         40         50         60 
MKYLLPTAAT GLLLLAAQPA VAANTGGYAT TDGGETSGAV KKTARSLQEI VDIIEAAKVD 

        70         80         90        100        110        120 
SKGKKVKGGA YPLIITYNGN EDSLIKAAEK NICGQWSKDA RGVQIKEFTK GITILGTNGS 

       130        140        150        160        170        180 
SANFGVWIVN SSDVVVRNMR FGYMPGGAQD GDAIRVDNSP NVWIDHNEIF AKNFECKGTP 

       190        200        210        220        230        240 
DNDTTFESAV DIKKGSTNVT VSYNYIHGIK KVGLSGASNT DTGRNLTYHH NIYRDVNSRL 

       250        260        270        280        290        300 
PLQRGGLVHA YNNLYDGITG SGFNVRQKGI ALIESNWFEN ALNPVTARND SSNFGTWELR 

       310        320        330        340        350        360 
NNNVTKPADF SKYNITWGRP STPHVNADDW KNTGKFPSIS YKYSPVSAQC VKDKLANYAG 

       370 
VSKNLAVLTA ANCK

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References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Characterization of the Erwinia carotovora pelB gene and its product pectate lyase." Lei S.-P., Lin H.-C., Wang S.-S., Callaway J., Wilcox G. J. Bacteriol. 169:4379-4383(1987) [PubMed: 3040692] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], PARTIAL PROTEIN SEQUENCE. Strain: EC.
[2]	"Synergism between Erwinia pectate lyase isoenzymes that depolymerize both pectate and pectin." Bartling S., Wegener C., Olsen O. Microbiology 141:873-881(1995) [PubMed: 7773390] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: C18.
[3]	"Genome sequence of the enterobacterial phytopathogen Erwinia carotovora subsp. atroseptica and characterization of virulence factors." Bell K.S., Sebaihia M., Pritchard L., Holden M.T.G., Hyman L.J., Holeva M.C., Thomson N.R., Bentley S.D., Churcher L.J.C., Mungall K., Atkin R., Bason N., Brooks K., Chillingworth T., Clark K., Doggett J., Fraser A., Hance Z. Toth I.K. Proc. Natl. Acad. Sci. U.S.A. 101:11105-11110(2004) [PubMed: 15263089] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: SCRI 1043 / ATCC BAA-672.

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Cross-references

Sequence databases
EMBL GenBank DDBJ	M17364 Genomic DNA. Translation: AAA24848.1. X81847 Genomic DNA. Translation: CAA57440.1. BX950851 Genomic DNA. Translation: CAG76965.1.
RefSeq	YP_052155.1.
3D structure databases
ModBase	Search...
Genome annotation databases
GeneID	2885351.
GenomeReviews	Gene locus ECA4068 in contig BX950851_GR.
KEGG	eca:ECA4068.
NMPDR	fig\|218491.3.peg.2899.
Organism-specific databases
CMR	Search...
Phylogenomic databases
HOGENOM	HBG401253.
Enzyme and pathway databases
BioCyc	ECAR218491:ECA4068-MONOMER.
BRENDA	4.2.2.2. 281579.
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]
ProtoNet	Search...

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Entry information

Entry name

PEL2_ERWCT

Accession

Primary (citable) accession number: Q6CZT3
Secondary accession number(s): P11431, Q06112, Q47469

Entry history

Integrated into UniProtKB/Swiss-Prot:	May 16, 2006
Last sequence update:	August 16, 2004
Last modified:	January 19, 2010
This is version 38 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)

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Relevant documents

PATHWAY comments

Index of metabolic and biosynthesis pathways

SIMILARITY comments

Index of protein domains and families

Names and origin

Protein attributes

General annotation (Comments)

Ontologies

Sequence annotation (Features)

Molecule processing

Sites

Amino acid modifications

Experimental info

Sequences

References

Cross-references

Sequence databases

3D structure databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Enzyme and pathway databases

Family and domain databases

Entry information

Relevant documents