Q5L6Q8 (LSPA_CHLAB) Reviewed, UniProtKB/Swiss-Prot

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:	CAB205

Organism

Chlamydophila abortus [Complete proteome] [HAMAP]

Taxonomic identifier

83555 [NCBI]

Taxonomic lineage

Bacteria › Chlamydiae › Chlamydiales › Chlamydiaceae › Chlamydia/Chlamydophila group › Chlamydophila

Protein attributes

Sequence length	165 AA.
Sequence status	Complete.
Protein existence	Inferred from homology

General annotation (Comments)

Function	This protein specifically catalyzes the removal of signal peptides from prolipoproteins By similarity. HAMAP MF_00161
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 inner membrane; Multi-pass membrane protein By similarity HAMAP MF_00161.
Sequence similarities	Belongs to the peptidase A8 family.

Ontologies

Keywords
Cellular component	Cell inner membrane Cell membrane Membrane
Domain	Transmembrane Transmembrane helix
Molecular function	Aspartyl protease Hydrolase Protease
Technical term	Complete proteome
Gene Ontology (GO)
Biological process	proteolysis Inferred from electronic annotation. Source: UniProtKB-KW
Cellular component	integral to membrane Inferred from electronic annotation. Source: UniProtKB-KW plasma membrane Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular function	aspartic-type endopeptidase activity 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
	Chain	1 – 165	165	Lipoprotein signal peptidase HAMAP MF_00161		PRO_0000289363
Regions
	Transmembrane	9 – 29	21	Helical; Potential
	Transmembrane	69 – 89	21	Helical; Potential
	Transmembrane	98 – 118	21	Helical; Potential
	Transmembrane	133 – 153	21	Helical; Potential
Sites
	Active site	115	1	By similarity
	Active site	142	1	By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q5L6Q8 [UniParc]. Last modified June 21, 2005. Version 1. Checksum: 7BFE771C235F7A74	FASTA	165	19,000
	10 20 30 40 50 60 MSSRSRSTFL AIACFVLIDW VTKLAVLLYL GNLPDANPIL YQYSWGKLLF CICPTFNEGA 70 80 90 100 110 120 AFGLFAKYKY FLFFIRITII LGILAFLFLR KKTSSPAIRF SLILLCSGAI GNVGDIVFYR 130 140 150 160 HVVDFISIGY KRWFFPTFNF ADIFISLGTL IFIYKLYFPT KQKIK

References

[1]

"The Chlamydophila abortus genome sequence reveals an array of variable proteins that contribute to interspecies variation." Thomson N.R., Yeats C., Bell K., Holden M.T.G., Bentley S.D., Livingstone M., Cerdeno-Tarraga A.-M., Harris B., Doggett J., Ormond D., Mungall K., Clarke K., Feltwell T., Hance Z., Sanders M., Quail M.A., Price C., Barrell B.G., Parkhill J., Longbottom D. Genome Res. 15:629-640(2005) [PubMed: 15837807] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: S26/3.

Cross-references

Sequence databases
EMBL GenBank DDBJ	CR848038 Genomic DNA. Translation: CAH63663.1.
RefSeq	YP_219634.1. NC_004552.2.
3D structure databases
ModBase	Search...
Protein family/group databases
MEROPS	A08.001.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
GeneID	3337619.
GenomeReviews	Gene locus CAB205 in contig CR848038_GR.
KEGG	cab:CAB205.
PATRIC	20201820. VBIChlAbo21869_0229.
Organism-specific databases
CMR	Search...
Phylogenomic databases
HOGENOM	HBG724422.
OMA	RHVVDFI.
ProtClustDB	PRK00376.
Enzyme and pathway databases
BioCyc	CABO218497:CAB205-MONOMER.
Family and domain databases
HAMAP	MF_00161. LspA. [Tree]
InterPro	IPR001872. Peptidase_A8. [Graphical view]
KO	K03101.
Pfam	PF01252. Peptidase_A8. 1 hit. [Graphical view]
PRINTS	PR00781. LIPOSIGPTASE.
TIGRFAMs	TIGR00077. LspA. 1 hit.
PROSITE	PS00855. SPASE_II. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

LSPA_CHLAB

Accession

Primary (citable) accession number: Q5L6Q8

Entry history

Integrated into UniProtKB/Swiss-Prot:	May 29, 2007
Last sequence update:	June 21, 2005
Last modified:	January 25, 2012
This is version 40 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program