P25178 (LSPA_HELPY) 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
Synonyms:	ureD
Ordered Locus Names:	HP_0074

Organism

Helicobacter pylori (strain ATCC 700392 / 26695) (Campylobacter pylori)

Taxonomic identifier

85962 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Epsilonproteobacteria › Campylobacterales › Helicobacteraceae › Helicobacter

Protein attributes

Sequence length	157 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
Subcellular location	Cell membrane; Multi-pass membrane protein By similarity HAMAP MF_00161.
Sequence similarities	Belongs to the peptidase A8 family.
Caution	Was originally (Ref.1) thought to be related to urease function.

Ontologies

Keywords
Cellular component	Cell membrane Membrane
Domain	Transmembrane Transmembrane helix
Molecular function	Aspartyl protease Hydrolase Protease
Technical term	Complete proteome Reference 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 – 157	157	Lipoprotein signal peptidase HAMAP MF_00161		PRO_0000178784
Regions
	Topological domain	1 – 9	9	Cytoplasmic Potential
	Transmembrane	10 – 30	21	Helical; Potential
	Topological domain	31 – 35	5	Extracellular Potential
	Transmembrane	36 – 56	21	Helical; Potential
	Topological domain	57	1	Cytoplasmic Potential
	Transmembrane	58 – 78	21	Helical; Potential
	Topological domain	79 – 121	43	Extracellular Potential
	Transmembrane	122 – 142	21	Helical; Potential
	Topological domain	143 – 157	15	Cytoplasmic Potential
Sites
	Active site	105	1	By similarity
	Active site	131	1	By similarity
Experimental info
	Sequence conflict	13	1	M → I in AAA25019. Ref.1
	Sequence conflict	40	1	M → V in AAA25019. Ref.1
	Sequence conflict	124 – 157	34	FAIFN…NKIKA → LPFLTSLMS in AAA25019. Ref.1

Sequences

	Sequence		Length	Mass (Da)
	P25178 [UniParc]. Last modified November 1, 1997. Version 2. Checksum: 738CF045ED01006C	FASTA	157	17,998
	10 20 30 40 50 60 MLKTTKKSLL VFMGVFFLIF GVDQAIKYAI LEGFRYESLM IDIVLVFNKG VAFSLLSFLE 70 80 90 100 110 120 GGLKYLQILL ILGLFIFLMR QRELFKNHAI EFGMVFGAGV SNVLDRFVHG GVVDYVYYHY 130 140 150 GFDFAIFNFA DVMIDVGVGV LLLKQFFFKQ KQNKIKA

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Shuttle cloning and nucleotide sequences of Helicobacter pylori genes responsible for urease activity." Labigne A., Cussac V., Courcoux P. J. Bacteriol. 173:1920-1931(1991) [PubMed: 2001995] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: 85P.
[2]	"The complete genome sequence of the gastric pathogen Helicobacter pylori." Tomb J.-F., White O., Kerlavage A.R., Clayton R.A., Sutton G.G., Fleischmann R.D., Ketchum K.A., Klenk H.-P., Gill S.R., Dougherty B.A., Nelson K.E., Quackenbush J., Zhou L., Kirkness E.F., Peterson S.N., Loftus B.J., Richardson D.L., Dodson R.J. , Khalak H.G., Glodek A., McKenney K., FitzGerald L.M., Lee N., Adams M.D., Hickey E.K., Berg D.E., Gocayne J.D., Utterback T.R., Peterson J.D., Kelley J.M., Cotton M.D., Weidman J.F., Fujii C., Bowman C., Watthey L., Wallin E., Hayes W.S., Borodovsky M., Karp P.D., Smith H.O., Fraser C.M., Venter J.C. Nature 388:539-547(1997) [PubMed: 9252185] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 700392 / 26695.

Cross-references

Sequence databases
EMBL GenBank DDBJ	M60398 Genomic DNA. Translation: AAA25019.1. AE000511 Genomic DNA. Translation: AAD07145.1.
PIR	B64529.
RefSeq	NP_206874.1. NC_000915.1.
3D structure databases
ProteinModelPortal	P25178.
ModBase	Search...
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
GeneID	899108.
GenomeReviews	Gene locus HP_0074 in contig AE000511_GR.
KEGG	hpy:HP0074.
NMPDR	fig|85962.1.peg.72.
PATRIC	20591353. VBIHelPyl33062_0077.
TIGR	HP_0074.
Phylogenomic databases
HOGENOM	HBG724422.
OMA	MVFGAGV.
ProtClustDB	PRK00376.
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_HELPY

Accession

Primary (citable) accession number: P25178

Entry history

Integrated into UniProtKB/Swiss-Prot:	May 1, 1992
Last sequence update:	November 1, 1997
Last modified:	January 25, 2012
This is version 89 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program