Reviewed, UniProtKB/Swiss-Prot Q57FM7 (LSPA_BRUAB)

Names and origin

Protein names

Recommended name:
    Lipoprotein signal peptidase
    EC=3.4.23.36
Alternative name(s):
    Prolipoprotein signal peptidase
    Signal peptidase II
      Short name=SPase II

Gene names

Name:	lspA
Ordered Locus Names:	BruAb1_0145

Organism

Brucella abortus [Complete proteome] [HAMAP]

Taxonomic identifier

235 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Alphaproteobacteria › Rhizobiales › Brucellaceae › Brucella

Protein attributes

Sequence length	160 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Inferred from homology.

General annotation (Comments)

Function	This protein specifically catalyzes the removal of signal peptides from prolipoproteins By similarity.
Catalytic activity	Release of signal peptides from bacterial membrane prolipoproteins. Hydrolyzes -Xaa-Yaa-Zaa-|-(S,diacylglyceryl)Cys-, in which Xaa is hydrophobic (preferably Leu), and Yaa (Ala or Ser) and Zaa (Gly or Ala) have small, neutral side chains.
Pathway	Protein modification; lipoprotein biosynthesis (signal peptide cleavage).
Subcellular location	Cell inner membrane; Multi-pass membrane proteinBy similarity.
Sequence similarities	Belongs to the peptidase A8 family.

Ontologies

Keywords
Cellular component	Cell inner membrane Cell membrane Membrane
Domain	Transmembrane
Molecular function	Aspartyl protease Hydrolase Protease
Technical term	Complete proteome
Gene Ontology (GO)
Biological process	proteolysis Inferred from electronic annotation. Source: InterPro
Cellular component	integral to membrane Inferred from electronic annotation. Source: UniProtKB-KW plasma membrane Inferred from electronic annotation. Source: HAMAP
Molecular function	aspartic-type endopeptidase activity Inferred from electronic annotation. Source: HAMAP
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 160	160	Lipoprotein signal peptidase		PRO_0000289357
Regions
	Transmembrane	6 – 26	21	Potential
	Transmembrane	58 – 78	21	Potential
	Transmembrane	95 – 115	21	Potential
	Transmembrane	127 – 147	21	Potential
Sites
	Active site	108	1	By similarity
	Active site	135	1	By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q57FM7-1 [UniParc]. Last modified May 10, 2005. Version 1. Checksum: D88410930B2A0B74	FASTA	160	18,230
	10 20 30 40 50 60 MKRHAVWSSL FVVILAVLID QGIKYLVESR MFYGQQIDLL PFLALFRTHN EGIAFSMLAW 70 80 90 100 110 120 LHDGGLIAIT LAVIAFVLYL WWTNAPERVF ARYGFALVIG GAIGNLIDRV MHGYVVDYVL 130 140 150 160 FHLPTWSFAV FNLADAFITI GAGLIILEEF LGWRRERISH

References

[1]

"Completion of the genome sequence of Brucella abortus and comparison to the highly similar genomes of Brucella melitensis and Brucella suis." Halling S.M., Peterson-Burch B.D., Bricker B.J., Zuerner R.L., Qing Z., Li L.-L., Kapur V., Alt D.P., Olsen S.C. J. Bacteriol. 187:2715-2726(2005) [PubMed: 15805518] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: 9-941 / Biovar 1.

Cross-references

Sequence databases
EMBLGenBankDDBJ	AE017223 Genomic DNA. Translation: AAX73557.1.
RefSeq	YP_220918.1.
3D structure databases
ModBase	Search...
Protein family/group databases
MEROPS	A08.001.
Genome annotation databases
GeneID	3339208.
GenomeReviews	Gene locus BruAb1_0145 in contig AE017223_GR.
KEGG	bmb:BruAb1_0145.
Organism-specific databases
CMR	Search...
Phylogenomic databases
HOGENOM	Q57FM7.
Enzyme and pathway databases
BioCyc	BABO262698:BRUAB1_0145-MON.
Family and domain databases
HAMAP	MF_00161. [Tree]
InterPro	IPR001872. Peptidase_A8. [Graphical view]
Pfam	PF01252. Peptidase_A8. 1 hit. [Graphical view]
PRINTS	PR00781. LIPOSIGPTASE.
ProDom	PD004304. Peptidase_A8. 1 hit. [Graphical view] [Entries sharing at least one domain]
TIGRFAMs	TIGR00077. lspA. 1 hit.
PROSITE	PS00855. SPASE_II. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

LSPA_BRUAB

Accession

Primary (citable) accession number: Q57FM7

Entry history

Integrated into UniProtKB/Swiss-Prot:	May 29, 2007
Last sequence update:	May 10, 2005
Last modified:	November 25, 2008
This is version 29 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)