P94449 (PEL2_BACSU) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Pectin lyase
Short name=PNL
EC=4.2.2.10

Alternative name(s):
Endo-pectin transeliminase
Protopectinase-R
Short name=PPase-R

Gene names

Name:	pelB
Synonyms:	ppr

Organism

Bacillus subtilis

Taxonomic identifier

1423 [NCBI]

Taxonomic lineage

Bacteria › Firmicutes › Bacillales › Bacillaceae › Bacillus

Protein attributes

Sequence length	345 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	Catalyzes the depolymerization of pectins of methyl esterification degree from 13 to 75%, with an endo mode of action. Can not degrade polygalacturonate. Also displays protopectinase activity, i.e. releases pectin from protopectin. Ref.2
Catalytic activity	Eliminative cleavage of (1->4)-alpha-D-galacturonan methyl ester to give oligosaccharides with 4-deoxy-6-O-methyl-alpha-D-galact-4-enuronosyl groups at their non-reducing ends. Ref.1 Ref.2
Enzyme regulation	Inhibited by Hg2+ and Mn2+. Not affected by EDTA in vitro. Ref.2
Subcellular location	Secreted Ref.2.
Induction	Up-regulated under high-phosphate conditions. Ref.1 Ref.2
Miscellaneous	Does not require calcium for activity.
Sequence similarities	Belongs to the polysaccharide lyase 1 family.
Biophysicochemical properties	pH dependence: Optimum pH is 8.0. Retains 70% of activity after 16 hours incubation in the pH range 4-11, at 37 degrees Celsius. Temperature dependence: Optimum temperature is 60 degrees Celsius. Retains more than 90% and 70% of activity after 30 min incubation at pH 6 at 50 and 60 degrees Celsius, respectively.

Ontologies

Keywords
Cellular component	Secreted
Domain	Signal
Molecular function	Lyase
Technical term	Direct protein sequencing
Gene Ontology (GO)
Cellular component	extracellular region Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular function	pectin 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 – 24	24	Ref.2
	Chain	25 – 345	321	Pectin lyase		PRO_0000367324
Sites
	Active site	234	1	Potential

Sequences

	Sequence		Length	Mass (Da)
	P94449 [UniParc]. Last modified May 1, 1997. Version 1. Checksum: A18B5C47E438E7E7	FASTA	345	37,996
	10 20 30 40 50 60 MKRFCLWFAV FSLLLVLLPG KAFGAVDFPN TSTNGLLGFA GNAKNEKGIS KASTTGGKNG 70 80 90 100 110 120 QIVYIQSVND LKTHLGGSTP KILVLQNDIS ASSKTTVTIG SNKTLVGSYA KKTLKNIYLT 130 140 150 160 170 180 TSSASGNVIF QNLTFEHSPQ INGNNDIQLY LDSGINYWID HVTFSGHSYS ASGSDLDKLL 190 200 210 220 230 240 YVGKSADYIT ISNSKFANHK YGLILGYPDD SQHQYDGYPH MTIANNYFEN LYVRGPGLMR 250 260 270 280 290 300 YGYFHVKNNY SNNFNQAITI ATKAKIYSEY NYFGKGSEKG GILDDKGTGY FKDTGSYPSL 310 320 330 340 NKQTSPLTSW NPGSNYSYRV QTPQYTKDFV TKYAGSQSTT LVFGY

References

[1]

"Molecular cloning and nucleotide sequence of the gene encoding phosphate-incucible pectin lyase of Bacillus subtilis." Sakamoto T., Kawasaki H., Sakai T. FEBS Lett. 398:269-273(1996) [PubMed: 8977121] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], CATALYTIC ACTIVITY, INDUCTION. Strain: ATCC 6633 / DSM 347 / IFO 3134 / PCI 219 / NRS 231.

[2]

"Purification, characterization, and production of two pectic transeliminases with protopectinase activity from Bacillus subtilis." Sakamoto T., Hours R.A., Sakai T. Biosci. Biotechnol. Biochem. 58:353-358(1994) [PubMed: 7764545] [Abstract] Cited for: PROTEIN SEQUENCE OF 25-49, FUNCTION, CATALYTIC ACTIVITY, SUBSTRATE SPECIFICITY, ENZYME REGULATION, INDUCTION, SUBCELLULAR LOCATION. Strain: ATCC 6633 / DSM 347 / IFO 3134 / PCI 219 / NRS 231.

Cross-references

Sequence databases
EMBL GenBank DDBJ	D83791 Genomic DNA. Translation: BAA12119.1.
3D structure databases
ProteinModelPortal	P94449.
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

PEL2_BACSU

Accession

Primary (citable) accession number: P94449

Entry history

Integrated into UniProtKB/Swiss-Prot:	March 24, 2009
Last sequence update:	May 1, 1997
Last modified:	August 10, 2010
This is version 44 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program