Q9PJY8 (LSPA_CHLMU) 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:	TC_0688

Organism

Chlamydia muridarum [Complete proteome] [HAMAP]

Taxonomic identifier

83560 [NCBI]

Taxonomic lineage

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

Protein attributes

Sequence length	167 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 – 167	167	Lipoprotein signal peptidase HAMAP MF_00161		PRO_0000178775
Regions
	Transmembrane	8 – 28	21	Helical; Potential
	Transmembrane	68 – 88	21	Helical; Potential
	Transmembrane	101 – 121	21	Helical; Potential
	Transmembrane	139 – 159	21	Helical; Potential
Sites
	Active site	116	1	By similarity
	Active site	143	1	By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q9PJY8 [UniParc]. Last modified October 1, 2000. Version 1. Checksum: 8FA90E16E849CC43	FASTA	167	18,917
	10 20 30 40 50 60 MTTRSLSTFL TSFLLVSLDW VSKLVVLLKS CQLSPHSPAL LYSYVWGHFS FLIVPSFNEG 70 80 90 100 110 120 AAFGLFAQYK IPLLIFRVFV ILCLFLFLGI KFRSLHIRTR IALTLILAGA LGNVGDILFH 130 140 150 160 GKVVDFLSIN YYSWSFPSFN LADAFISLGT LLLVGHLYFS KEDKKYF

References

[1]

"Genome sequences of Chlamydia trachomatis MoPn and Chlamydia pneumoniae AR39." Read T.D., Brunham R.C., Shen C., Gill S.R., Heidelberg J.F., White O., Hickey E.K., Peterson J.D., Utterback T.R., Berry K.J., Bass S., Linher K.D., Weidman J.F., Khouri H.M., Craven B., Bowman C., Dodson R.J., Gwinn M.L. , Nelson W.C., DeBoy R.T., Kolonay J.F., McClarty G., Salzberg S.L., Eisen J.A., Fraser C.M. Nucleic Acids Res. 28:1397-1406(2000) [PubMed: 10684935] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: MoPn / Nigg.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AE002160 Genomic DNA. Translation: AAF39505.1.
PIR	B81676.
RefSeq	NP_297062.1. NC_002620.2.
3D structure databases
ModBase	Search...
Protein family/group databases
MEROPS	A08.001.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
GeneID	1246049.
GenomeReviews	Gene locus TC_0688 in contig AE002160_GR.
KEGG	cmu:TC0688.
PATRIC	20372832. VBIChlMur19118_0728.
TIGR	TC_0688.
Phylogenomic databases
HOGENOM	HBG724422.
OMA	MVFGAGV.
ProtClustDB	PRK00376.
Enzyme and pathway databases
BioCyc	CMUR243161:TC_0688-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_CHLMU

Accession

Primary (citable) accession number: Q9PJY8

Entry history

Integrated into UniProtKB/Swiss-Prot:	June 1, 2001
Last sequence update:	October 1, 2000
Last modified:	January 25, 2012
This is version 71 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program