Reviewed, UniProtKB/Swiss-Prot Q89AV0 (LSPA_BUCBP)

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:	bbp_138

Organism

Buchnera aphidicola subsp. Baizongia pistaciae [Complete proteome] [HAMAP]

Taxonomic identifier

135842 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Gammaproteobacteria › Enterobacteriales › Enterobacteriaceae › Buchnera

Protein attributes

Sequence length	163 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. HAMAP MF_00161
Pathway	Protein modification; lipoprotein biosynthesis (signal peptide cleavage). HAMAP MF_00161
Subcellular location	Cell membrane; Multi-pass membrane protein By similarity.
Sequence similarities	Belongs to the peptidase A8 family.

Ontologies

Keywords
Cellular component	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-SubCell 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 – 163	163	Lipoprotein signal peptidase HAMAP MF_00161		PRO_0000178773
Regions
	Transmembrane	5 – 27	23	Potential
	Transmembrane	71 – 90	20	Potential
	Transmembrane	97 – 119	23	Potential
	Transmembrane	134 – 156	23	Potential
Sites
	Active site	116	1	By similarity
	Active site	143	1	By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q89AV0-1 [UniParc]. Last modified May 23, 2003. Version 1. Checksum: D585E91DD7C5AFC4	FASTA	163	19,147
	10 20 30 40 50 60 MKIPLIYNRI LILFFFIANI IILDQVSKKW IINNLLLHEK KPLISIMNIF YVRNYGTAFN 70 80 90 100 110 120 FFSNNPGEKN YILCLISSIA ILIILKTMYN NTTIENFFYN IPSAFIISGA IGNFIDRCYL 130 140 150 160 GYVIDFIDFH INNWHFATFN IADVSIFIGS VLFIYHNKYF LKN

References

[1]

"Reductive genome evolution in Buchnera aphidicola." van Ham R.C.H.J., Kamerbeek J., Palacios C., Rausell C., Abascal F., Bastolla U., Fernandez J.M., Jimenez L., Postigo M., Silva F.J., Tamames J., Viguera E., Latorre A., Valencia A., Moran F., Moya A. Proc. Natl. Acad. Sci. U.S.A. 100:581-586(2003) [PubMed: 12522265] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].

Cross-references

Sequence databases
EMBLGenBankDDBJ	AE016826 Genomic DNA. Translation: AAO26872.1.
RefSeq	NP_777767.1.
3D structure databases
ModBase	Search...
Protein family/group databases
MEROPS	A08.001.
Genome annotation databases
GeneID	1058168.
GenomeReviews	Gene locus bbp_138 in contig AE016826_GR.
KEGG	bab:bbp138.
Organism-specific databases
CMR	Search...
Phylogenomic databases
HOGENOM	Q89AV0.
OMA	SIGNIID.
Enzyme and pathway databases
BioCyc	BAPH224915:BBP_138-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_BUCBP

Accession

Primary (citable) accession number: Q89AV0

Entry history

Integrated into UniProtKB/Swiss-Prot:	May 23, 2003
Last sequence update:	May 23, 2003
Last modified:	November 3, 2009
This is version 47 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)