Reviewed, UniProtKB/Swiss-Prot P85142 (PRLA_LYSSX)

Names and origin

Protein names	Recommended name:     Alpha-lytic protease L1     EC=3.4.21.12 Alternative name(s):     Alpha-lytic endopeptidase L1
Organism	Lysobacter sp. (strain XL1)
Taxonomic identifier	186334 [NCBI]
Taxonomic lineage	Bacteria › Proteobacteria › Gammaproteobacteria › Xanthomonadales › Xanthomonadaceae › Lysobacter

Protein attributes

Sequence length	62 AA.
Sequence status	Fragments.
Sequence processing	The displayed sequence is not processed.
Protein existence	Evidence at protein level.

General annotation (Comments)

Function	Has bacteriolytic activity. Ref.2
Catalytic activity	Preferential cleavage: Ala-|-Xaa, Val-|-Xaa in bacterial cell walls, elastin and other proteins. Ref.2 UniProtKB P00778
Enzyme regulation	Inhibited by phenylmethanesulfonyl fluoride (PMSF) and p-chloromercuribenzoate (PCMB). Ref.2
Subunit structure	Monomer. Ref.2
Subcellular location	Secreted. Ref.2
Sequence similarities	Belongs to the peptidase S1 family.
biophysicochemical properties	pH dependence: Optimum pH is 8.0. Active from pH 7.0 to 11.0. Ref.2 Temperature dependence: Optimum temperature is 70 degrees Celsius. Ref.2

Ontologies

Keywords
Cellular component	Secreted
Molecular function	Antibiotic Antimicrobial Hydrolase Protease Serine protease
PTM	Disulfide bond
Technical term	Direct protein sequencing
Gene Ontology (GO)
Biological process	defense response to bacterium Inferred from electronic annotation. Source: UniProtKB-KW proteolysis Inferred from electronic annotation. Source: InterPro
Cellular component	extracellular region Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular function	serine-type endopeptidase activity Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – ›62	›62	Alpha-lytic protease L1		PRO_0000287680
Sites
	Active site	48	1	By similarity UniProtKB P00778
Amino acid modifications
	Disulfide bond	17 ↔ ?		By similarity UniProtKB P00778
	Disulfide bond	42 ↔ ?		By similarity UniProtKB P00778
Experimental info
	Non-adjacent residues	23 – 24	2
	Non-adjacent residues	26 – 27	2
	Non-adjacent residues	54 – 55	2
	Non-adjacent residues	58 – 59	2
	Non-terminal residue	62	1

Sequences

	Sequence		Length	Mass (Da)
	P85142-1 [UniParc]. Last modified May 15, 2007. Version 1. Checksum: 2C602878C9E3BFDE	FASTA	62	6,611
	10 20 30 40 50 60 VNVLGGIEYS INNATLCSVG FSVRVFNYAE GAVRGLTQGN ACMGRGDSGG SWFTLFERQY GL

References

[1]	"Structural investigations and identification of the extracellular bacteriolytic endopeptidase L1 from Lysobacter sp. XL1." Muranova T.A., Krasovskaya L.A., Tsfasman I.M., Stepnaya O.A., Kulaev I.S. Biokhimiia 69:501-505(2004) [PubMed: 15193123] [Abstract] Cited for: PROTEIN SEQUENCE.
[2]	"Identification of extracellular bacteriolytic enzymes from Lysobacter sp. XL1." Muranova T.A., Stepnaya O.A., Tsfasman I.M., Kulaev I.S. Submitted (APR-2007) to UniProtKB Cited for: FUNCTION, CATALYTIC ACTIVITY, ENZYME REGULATION, BIOPHYSICOCHEMICAL PROPERTIES, SUBUNIT, SUBCELLULAR LOCATION.

Cross-references

3D structure databases
ModBase	Search...
Family and domain databases
InterPro	IPR018114. Peptidase_S1/S6_AS. [Graphical view]
PROSITE	PS50240. TRYPSIN_DOM. Partial match. PS00134. TRYPSIN_HIS. Partial match. PS00135. TRYPSIN_SER. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

PRLA_LYSSX

Accession

Primary (citable) accession number: P85142

Entry history

Integrated into UniProtKB/Swiss-Prot:	May 15, 2007
Last sequence update:	May 15, 2007
Last modified:	June 16, 2009
This is version 11 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)