Reviewed, UniProtKB/Swiss-Prot P0C1C3 (PEL3_PECCC)

Names and origin

Protein names

Recommended name:
    Pectate lyase 3
    EC=4.2.2.2
Alternative name(s):
    Pectate lyase III
      Short name=PEL III
    Pectate lyase C
      Short name=PLC

Gene names

Name:	pel3
Synonyms:	pelC, pelCI

Organism

Pectobacterium carotovorum subsp. carotovorum (Erwinia carotovora subsp. carotovora)

Taxonomic identifier

555 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Gammaproteobacteria › Enterobacteriales › Enterobacteriaceae › Pectobacterium

Protein attributes

Sequence length	374 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Inferred from homology.

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.

Ontologies

Keywords
Cellular component	Secreted
Domain	Signal
Ligand	Calcium Metal-binding
Molecular function	Lyase
PTM	Disulfide bond
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...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Signal peptide	1 – 22	22	By similarity
	Chain	23 – 374	352	Pectate lyase 3		PRO_0000234451
Sites
	Active site	239	1	Potential
	Metal binding	150	1	Calcium By similarity
	Metal binding	152	1	Calcium By similarity
	Metal binding	187	1	Calcium By similarity
	Metal binding	191	1	Calcium By similarity
Amino acid modifications
	Disulfide bond	93 ↔ 176		By similarity
	Disulfide bond	350 ↔ 373		By similarity
Experimental info
	Sequence conflict	90 – 91	2	ND → AN in AAB82289. Ref.2
	Sequence conflict	97	1	K → S in AAB82289. Ref.2
	Sequence conflict	129	1	T → V in AAB82289. Ref.2
	Sequence conflict	132	1	S → P in AAB82289. Ref.2
	Sequence conflict	144	1	M → Y in AAB82289. Ref.2
	Sequence conflict	237	1	N → D in AAB82289. Ref.2
	Sequence conflict	321	1	T → S in AAB82289. Ref.2

Sequences

	Sequence		Length	Mass (Da)
	P0C1C3-1 [UniParc]. Last modified May 16, 2006. Version 1. Checksum: 34CE8929170CC21C	FASTA	374	40,565
	10 20 30 40 50 60 MKYLLPSAAA GLLLLAAQPT MAANTGGYAT TDGGDVAGAV KKTARSMQDI IDIIEAAKLD 70 80 90 100 110 120 SNGKKVKGGA YPLVITYNGN EDALIKAAEN DICGQWKKDA RGVEIKEFTK GITIIGTNGS 130 140 150 160 170 180 SANFGIWLTK SSDIVIRNMR FGYMPGGAQD GDAIRIDNTP NVWIDHNEIF AKNFECAGTK 190 200 210 220 230 240 DGDTTFESAI DIKKASTNVT VSYNYIHGIK KVGLSGFSSS DTGRDLTYHH NIYDDVNARL 250 260 270 280 290 300 PLQRGGQVHA YNNLYTGITS SGLNVRQKGI ALIERNWFEN AKNPVTSRYD GSNFGTWELR 310 320 330 340 350 360 NNNVMSPADF AKYNITWDKD TKPYVNAEDW KSTGTFASVP YSYSPVSAQC VKDKLANYAG 370 VNKNLAVLTA ANCN

References

[1]	"Extracellular and periplasmic isoenzymes of pectate lyase from Erwinia carotovora subspecies carotovora belong to different gene families." Hinton J.C.D., Sidebotham J.M., Gill D.R., Salmond G.P.C. Mol. Microbiol. 3:1785-1795(1989) [PubMed: 2695748] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: SCRI 193.
[2]	Lim S.T., Park Y.W., Yun H.D. Submitted (SEP-1997) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: LY34.

Cross-references

Sequence databases
EMBL GenBank DDBJ	X16398 Genomic DNA. Translation: CAA34433.1. AF026033 Genomic DNA. Translation: AAB82289.1.
PIR	WZWCPC. S07652.
3D structure databases
SMR	P0C1C3. Positions 22-373.
ModBase	Search...
Protein family/group databases
CAZy	PL1. Polysaccharide Lyase Family 1.
Enzyme and pathway databases
BRENDA	4.2.2.2. 290410.
Family and domain databases
InterPro	IPR002022. Amb_allergen. IPR006626. PbH1. 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. SM00710. PbH1. 5 hits. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

PEL3_PECCC

Accession

Primary (citable) accession number: P0C1C3
Secondary accession number(s): O31035 , P14006, P29171, Q47470

Entry history

Integrated into UniProtKB/Swiss-Prot:	May 16, 2006
Last sequence update:	May 16, 2006
Last modified:	January 19, 2010
This is version 23 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)