Reviewed, UniProtKB/Swiss-Prot Q5P9U0 (LSPA_ANAMM)

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:	AM1081

Organism

Anaplasma marginale (strain St. Maries) [Complete proteome] [HAMAP]

Taxonomic identifier

234826 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Alphaproteobacteria › Rickettsiales › Anaplasmataceae › Anaplasma

Protein attributes

Sequence length	170 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
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 – 170	170	Lipoprotein signal peptidase HAMAP MF_00161		PRO_1000076914
Regions
	Transmembrane	5 – 25	21	Potential
	Transmembrane	62 – 82	21	Potential
	Transmembrane	89 – 111	23	Potential
	Transmembrane	126 – 146	21	Potential
Sites
	Active site	106	1	By similarity
	Active site	133	1	By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q5P9U0-1 [UniParc]. Last modified January 4, 2005. Version 1. Checksum: A7DA88C94C9D0743	FASTA	170	18,587
	10 20 30 40 50 60 MKSKIVGVIA IVLVFALDQV SKAYAIDWYS QSGATEIFKF CSLVEVWNRG ISFGMFGALE 70 80 90 100 110 120 SSNLIFTYVS LGVILMLFVL FVQSKCNKST ICMGVVIGGA LGNLADRLRF GAVYDFVSLH 130 140 150 160 170 AGEFHWPAFN FADVCVTCGV ICFLCLEIMY HAKACVDTSG DPDALSVKKY

References

[1]

"Complete genome sequencing of Anaplasma marginale reveals that the surface is skewed to two superfamilies of outer membrane proteins." Brayton K.A., Kappmeyer L.S., Herndon D.R., Dark M.J., Tibbals D.L., Palmer G.H., McGuire T.C., Knowles D.P. Jr. Proc. Natl. Acad. Sci. U.S.A. 102:844-849(2005) [PubMed: 15618402] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].

Cross-references

Sequence databases
EMBL GenBank DDBJ	CP000030 Genomic DNA. Translation: AAV86940.1.
RefSeq	YP_154195.1.
3D structure databases
ModBase	Search...
Protein-protein interaction databases
STRING	Q5P9U0.
Protein family/group databases
MEROPS	A08.001.
Genome annotation databases
GeneID	3170986.
GenomeReviews	Gene locus AM1081 in contig CP000030_GR.
KEGG	ama:AM1081.
Organism-specific databases
CMR	Search...
Phylogenomic databases
eggNOG	COG0597.
HOGENOM	HBG724422.
OMA	RYFFIAI.
Enzyme and pathway databases
BioCyc	AMAR234826:AM1081-MONOMER.
Family and domain databases
HAMAP	MF_00161. LspA. [Tree]
InterPro	IPR001872. Peptidase_A8. [Graphical view]
Pfam	PF01252. Peptidase_A8. 1 hit. [Graphical view]
PRINTS	PR00781. LIPOSIGPTASE.
TIGRFAMs	TIGR00077. lspA. 1 hit.
PROSITE	PS00855. SPASE_II. False negative. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

LSPA_ANAMM

Accession

Primary (citable) accession number: Q5P9U0

Entry history

Integrated into UniProtKB/Swiss-Prot:	May 20, 2008
Last sequence update:	January 4, 2005
Last modified:	February 9, 2010
This is version 36 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)