Q8GCB2 (PTLY_BACLI) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Pectate trisaccharide-lyase
EC=4.2.2.22

Alternative name(s):
Exopolygalacturonate lyase
Pectate lyase A
Short name=PelA

Gene names

Name:	pelA
Synonyms:	pel

Organism

Bacillus licheniformis

Taxonomic identifier

1402 [NCBI]

Taxonomic lineage

Bacteria › Firmicutes › Bacillales › Bacillaceae › Bacillus

Protein attributes

Sequence length	341 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	Cleaves unsaturated oligo-galacturonides from pectin. The major product is trigalacturonate; digalacturonate and tetragalacturonate are also produced. Activity on methylated pectins decreases with an increasing degree of methylation. Ref.1 Ref.2 UniProtKB B1B6T1
Catalytic activity	Eliminative cleavage of unsaturated trigalacturonate as the major product from the reducing end of polygalacturonic acid/pectate. Ref.1 Ref.2
Cofactor	Calcium. Ref.2
Enzyme regulation	Inhibited by excess substrate. Inhibited by EDTA. Ref.1 Ref.2
Subcellular location	Secreted Probable.
Sequence similarities	Belongs to the polysaccharide lyase 1 family. Contains 4 PbH1 repeats.
Biophysicochemical properties	pH dependence: Optimum pH is 11.0. Stable from pH 7.0 to 11.0. Ref.2 Temperature dependence: Optimum temperature is 69 degrees Celsius. Thermostable, retains 100% of activity after 2 hours incubation at 65 degrees Celsius.

Ontologies

Keywords
Biological process	Carbohydrate metabolism Cell wall biogenesis/degradation Polysaccharide degradation
Cellular component	Secreted
Domain	Repeat Signal
Ligand	Calcium Metal-binding
Molecular function	Lyase
Technical term	Direct protein sequencing
Gene Ontology (GO)
Biological process	cellular cell wall organization Inferred from electronic annotation. Source: UniProtKB-KW polysaccharide catabolic process Inferred from electronic annotation. Source: UniProtKB-KW
Cellular component	extracellular region Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular function	lyase activity Inferred from electronic annotation. Source: UniProtKB-KW metal ion binding Inferred from electronic annotation. Source: UniProtKB-KW
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Signal peptide	1 – 27	27	Potential
	Propeptide	28 – 39	12	Ref.2		PRO_0000405012
	Chain	40 – 341	302	Pectate trisaccharide-lyase Ref.2		PRO_0000405013
Regions
	Repeat	131 – 156	26	PbH1 1
	Repeat	158 – 186	29	PbH1 2
	Repeat	262 – 283	22	PbH1 3
	Repeat	287 – 322	36	PbH1 4
Sites
	Active site	233	1	By similarity UniProtKB P39116
	Metal binding	150	1	Calcium By similarity UniProtKB P39116
	Metal binding	180	1	Calcium By similarity UniProtKB P39116
	Metal binding	184	1	Calcium By similarity UniProtKB P39116

Sequences

	Sequence		Length	Mass (Da)
	Q8GCB2 [UniParc]. Last modified March 1, 2003. Version 1. Checksum: 4662DFCBF915E9C6	FASTA	341	37,365
	10 20 30 40 50 60 MKKLISIIFI FVLGVVGSLT AAVSAEAASA LNSGKVNPLA DFSLKGFAAL NGGTTGGEGG 70 80 90 100 110 120 QTVTVTTGDQ LIAALKNKNA NTPLKIYVNG TITTSNTSAS KIDVKDVSNV SIVGSGTKGE 130 140 150 160 170 180 LKGIGIKIWR ANNIIIRNLK IHEVASGDKD AIGIEGPSKN IWVDHNELYH SLNVDKDYYD 190 200 210 220 230 240 GLFDVKRDAE YITFSWNYVH DGWKSMLMGS SDSDNYNRTI TFHHNWFENL NSRVPSFRFG 250 260 270 280 290 300 EGHIYNNYFN KIIDSGINSR MGARIRIENN LFENAKDPIV SWYSSSPGYW HVSNNKFVNS 310 320 330 340 RGSMPTTSTT TYNPPYSYSL DNVDNVKSIV KQNAGVGKIN P

References

[1]	"Cloning of the pelA gene from Bacillus licheniformis 14A and biochemical characterization of recombinant, thermostable, high-alkaline pectate lyase." Berensmeier S., Singh S.A., Meens J., Buchholz K. Appl. Microbiol. Biotechnol. 64:560-567(2004) [PubMed: 14673544] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, CATALYTIC ACTIVITY, ENZYME REGULATION. Strain: 14A.
[2]	"Exopolygalacturonate lyase from a thermophilic Bacillus sp." Singh S.A., Plattner H., Diekmann H. Enzyme Microb. Technol. 25:420-425(1999) Cited for: PROTEIN SEQUENCE OF 40-57; 205-218 AND 243-249, FUNCTION, CATALYTIC ACTIVITY, COFACTOR, ENZYME REGULATION, BIOPHYSICOCHEMICAL PROPERTIES. Strain: 14A.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AJ517194 Genomic DNA. Translation: CAD56882.1.
3D structure databases
HSSP	HSSP built from PDB template 1BN8 based on UniProtKB P39116.
ProteinModelPortal	Q8GCB2.
ModBase	Search...
Protein family/group databases
CAZy	PL1. Polysaccharide Lyase Family 1.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Enzyme and pathway databases
BRENDA	4.2.2.22. 669.
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. 4 hits. [Graphical view]
SUPFAM	SSF51126. Pectin_lyas_like. 1 hit.
ProtoNet	Search...

Entry information

Entry name

PTLY_BACLI

Accession

Primary (citable) accession number: Q8GCB2

Entry history

Integrated into UniProtKB/Swiss-Prot:	February 8, 2011
Last sequence update:	March 1, 2003
Last modified:	May 31, 2011
This is version 32 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program