P44975 (LSPA_HAEIN) 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:	HI_1006

Organism

Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd) [Reference proteome] [HAMAP]

Taxonomic identifier

71421 [NCBI]

Taxonomic lineage

cellular organisms › Bacteria › Proteobacteria › Gammaproteobacteria › Pasteurellales › Pasteurellaceae › Haemophilus › Haemophilus influenzae

Protein attributes

Sequence length	171 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-Rule 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-Rule MF_00161
Pathway	Protein modification; lipoprotein biosynthesis (signal peptide cleavage). HAMAP-Rule MF_00161
Subcellular location	Cell inner membrane; Multi-pass membrane protein By similarity HAMAP-Rule 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 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: HAMAP
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 171	171	Lipoprotein signal peptidase HAMAP-Rule MF_00161		PRO_0000178783
Regions
	Topological domain	1 – 7	7	Cytoplasmic Potential
	Transmembrane	8 – 28	21	Helical; Potential
	Topological domain	29 – 63	35	Periplasmic Potential
	Transmembrane	64 – 84	21	Helical; Potential
	Topological domain	85 – 98	14	Cytoplasmic Potential
	Transmembrane	99 – 119	21	Helical; Potential
	Topological domain	120 – 132	13	Periplasmic Potential
	Transmembrane	133 – 153	21	Helical; Potential
	Topological domain	154 – 171	18	Cytoplasmic Potential
Sites
	Active site	111	1	By similarity
	Active site	138	1	By similarity

Sequences

	Sequence		Length	Mass (Da)
	P44975 [UniParc]. Last modified November 1, 1995. Version 1. Checksum: D3DE4D74A173B3ED	FASTA	171	19,363
	10 20 30 40 50 60 MSKKSGLSFL WLSAVAFVID LLTKYIVVQK FDLYESVNVL PVFNLTYVRN YGAAFSFLAD 70 80 90 100 110 120 HSGWQQYFFI LLALAISGML VYFLAKNNAE QKIQNSAYAL IIGGALANMV DRAYNGFVVD 130 140 150 160 170 FFDFYWDIYH YPVFNIADIA ICIGAGLLVL DAFKSEKKKV QDKQVEKCGQ K

References

[1]

"Whole-genome random sequencing and assembly of Haemophilus influenzae Rd." Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., Scott J.D., Shirley R., Liu L.-I. , Glodek A., Kelley J.M., Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., Venter J.C. Science 269:496-512(1995) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 51907 / DSM 11121 / KW20 / Rd.

Cross-references

Sequence databases
EMBL GenBank DDBJ	L42023 Genomic DNA. Translation: AAC22667.1.
PIR	H64107.
RefSeq	NP_439167.1. NC_000907.1.
3D structure databases
ModBase	Search...
Protein-protein interaction databases
STRING	71421.HI1006.
Protein family/group databases
MEROPS	A08.001.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblBacteria	AAC22667; AAC22667; HI_1006.
GeneID	949998.
KEGG	hin:HI1006.
PATRIC	20190673. VBIHaeInf48452_1049.
Phylogenomic databases
eggNOG	COG0597.
KO	K03101.
OMA	WLWLAIL.
ProtClustDB	PRK00376.
Enzyme and pathway databases
UniPathway	UPA00665.
Family and domain databases
HAMAP	MF_00161. LspA.
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. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

LSPA_HAEIN

Accession

Primary (citable) accession number: P44975

Entry history

Integrated into UniProtKB/Swiss-Prot:	November 1, 1995
Last sequence update:	November 1, 1995
Last modified:	May 1, 2013
This is version 94 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program