Reviewed, UniProtKB/Swiss-Prot O34310 (PELC_BACSU)

Names and origin

Protein names

Recommended name:
    Pectate lyase C
    EC=4.2.2.2
Alternative name(s):
    Pectin lyase
    EC=4.2.2.10

Gene names

Name:	pelC
Synonyms:	yvpA
Ordered Locus Names:	BSU34950

Organism

Bacillus subtilis [Complete proteome] [HAMAP]

Taxonomic identifier

1423 [NCBI]

Taxonomic lineage

Bacteria › Firmicutes › Bacillales › Bacillaceae › Bacillus

Protein attributes

Sequence length	221 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 both polygalacturonate and pectins of methyl esterification degree from 22 to 89%, with an endo mode of action. In contrast to the majority of pectate lyases, displays high activity on highly methylated pectins. Is also able to cleave trigalacturonate to galacturonic acid and unsaturated digalacturonate. Ref.3
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. 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.
Cofactor	Binds 1 calcium ion per subunit. Ref.3
Pathway	Glycan metabolism; pectin degradation; 2-dehydro-3-deoxy-D-gluconic acid from pectin: step 2/5.
Subcellular location	Secreted By similarity.
Miscellaneous	Hg2+ could replace calcium ion.
Sequence similarities	Belongs to the polysaccharide lyase 3 family.
biophysicochemical properties	Kinetic parameters: Vmax=256.7 µmol/min/mg enzyme with 22% esterified pectin as substrate Vmax=59.6 µmol/min/mg enzyme with polygalacturonic acid as substrate pH dependence: Optimum pH is 10. Temperature dependence: Optimum temperature is 65 degrees Celsius. Thermostable at 50 degrees Celsius in buffers at pH 7.

Ontologies

Keywords
Cellular component	Secreted
Domain	Signal
Ligand	Calcium Metal-binding
Molecular function	Lyase
Technical term	Complete proteome
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 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 – 27	27	Potential
	Chain	28 – 221	194	Pectate lyase C		PRO_0000233104

Sequences

	Sequence		Length	Mass (Da)
	O34310-1 [UniParc]. Last modified January 1, 1998. Version 1. Checksum: AB324700DE573236	FASTA	221	24,281
	10 20 30 40 50 60 MKKIVSILFM FGLVMGFSQF QPSTVFAADK VVHETIIVPK NTTYDGKGQR FVAGKELGDG 70 80 90 100 110 120 SQSENQDPVF RVEDGATLKN VVLGAPAADG VHTYGNVNIQ NVKWEDVGED ALTVKKEGKV 130 140 150 160 170 180 TIDGGSAQKA SDKIFQINKA STFTVKNFTA DNGGKFIRQL GGSTFHVDVI IDKCTITNMK 190 200 210 220 EAIFRTDSKT STVRMTNTRY SNVGQKWIGV QHIYENNNTQ F

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Nucleotide sequence of the 300-304 chromosomal segment of Bacillus subtilis." Lazarevic V., Soldo B., Rivolta C., Reynolds S., Mauel C., Karamata D. Submitted (NOV-1997) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[2]	"The complete genome sequence of the Gram-positive bacterium Bacillus subtilis." Kunst F., Ogasawara N., Moszer I., Albertini A.M., Alloni G., Azevedo V., Bertero M.G., Bessieres P., Bolotin A., Borchert S., Borriss R., Boursier L., Brans A., Braun M., Brignell S.C., Bron S., Brouillet S., Bruschi C.V. , Caldwell B., Capuano V., Carter N.M., Choi S.-K., Codani J.-J., Connerton I.F., Cummings N.J., Daniel R.A., Denizot F., Devine K.M., Duesterhoeft A., Ehrlich S.D., Emmerson P.T., Entian K.-D., Errington J., Fabret C., Ferrari E., Foulger D., Fritz C., Fujita M., Fujita Y., Fuma S., Galizzi A., Galleron N., Ghim S.-Y., Glaser P., Goffeau A., Golightly E.J., Grandi G., Guiseppi G., Guy B.J., Haga K., Haiech J., Harwood C.R., Henaut A., Hilbert H., Holsappel S., Hosono S., Hullo M.-F., Itaya M., Jones L.-M., Joris B., Karamata D., Kasahara Y., Klaerr-Blanchard M., Klein C., Kobayashi Y., Koetter P., Koningstein G., Krogh S., Kumano M., Kurita K., Lapidus A., Lardinois S., Lauber J., Lazarevic V., Lee S.-M., Levine A., Liu H., Masuda S., Mauel C., Medigue C., Medina N., Mellado R.P., Mizuno M., Moestl D., Nakai S., Noback M., Noone D., O'Reilly M., Ogawa K., Ogiwara A., Oudega B., Park S.-H., Parro V., Pohl T.M., Portetelle D., Porwollik S., Prescott A.M., Presecan E., Pujic P., Purnelle B., Rapoport G., Rey M., Reynolds S., Rieger M., Rivolta C., Rocha E., Roche B., Rose M., Sadaie Y., Sato T., Scanlan E., Schleich S., Schroeter R., Scoffone F., Sekiguchi J., Sekowska A., Seror S.J., Serror P., Shin B.-S., Soldo B., Sorokin A., Tacconi E., Takagi T., Takahashi H., Takemaru K., Takeuchi M., Tamakoshi A., Tanaka T., Terpstra P., Tognoni A., Tosato V., Uchiyama S., Vandenbol M., Vannier F., Vassarotti A., Viari A., Wambutt R., Wedler E., Wedler H., Weitzenegger T., Winters P., Wipat A., Yamamoto H., Yamane K., Yasumoto K., Yata K., Yoshida K., Yoshikawa H.-F., Zumstein E., Yoshikawa H., Danchin A. Nature 390:249-256(1997) [PubMed: 9384377] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: 168.
[3]	"Pectate lyase C from Bacillus subtilis: a novel endo-cleaving enzyme with activity on highly methylated pectin." Soriano M., Diaz P., Pastor F.I.J. Microbiology 152:617-625(2006) [PubMed: 16514142] [Abstract] Cited for: GENE NAME, FUNCTION, SUBSTRATE SPECIFICITY, COFACTOR, BIOPHYSICOCHEMICAL PROPERTIES. Strain: 168.

Cross-references

Sequence databases
EMBLGenBankDDBJ	AF017113 Genomic DNA. Translation: AAC67291.1. AL009126 Genomic DNA. Translation: CAB15500.1.
PIR	A70045.
RefSeq	NP_391375.1.
3D structure databases
HSSP	HSSP built from PDB template 1EE6 based on UniProtKB Q9RHW0.
ModBase	Search...
Protein family/group databases
CAZy	PL3. Polysaccharide Lyase Family 3.
Genome annotation databases
GeneID	936594.
GenomeReviews	Gene locus BSU34950 in contig AL009126_GR.
KEGG	bsu:BSU34950.
NMPDR	fig|224308.1.peg.3501.
Organism-specific databases
SubtiList	BG14129. yvpA. [Micado]
CMR	Search...
Phylogenomic databases
HOGENOM	O34310.
OMA	O34310. EAIFRTD.
Enzyme and pathway databases
BioCyc	BSUB224308:BSU3492-MON.
BRENDA	4.2.2.2. 150.
Family and domain databases
InterPro	IPR004898. Pectate_lyase_cat. IPR012334. Pectin_lyas_fold. [Graphical view]
Gene3D	G3DSA:2.160.20.10. Pectin_lyas_fold. 1 hit.
Pfam	PF03211. Pectate_lyase. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

PELC_BACSU

Accession

Primary (citable) accession number: O34310
Secondary accession number(s): Q795F2

Entry history

Integrated into UniProtKB/Swiss-Prot:	May 2, 2006
Last sequence update:	January 1, 1998
Last modified:	June 16, 2009
This is version 45 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)