Q8PN18 (LSPA_XANAC) 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:	XAC1255

Organism

Xanthomonas axonopodis pv. citri (strain 306) [Complete proteome] [HAMAP]

Taxonomic identifier

190486 [NCBI]

Taxonomic lineage

cellular organisms › Bacteria › Proteobacteria › Gammaproteobacteria › Xanthomonadales › Xanthomonadaceae › Xanthomonas › Xanthomonas citri group › Xanthomonas campestris pv. citri › Xanthomonas citri pv. citri

Protein attributes

Sequence length	172 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
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 – 172	172	Lipoprotein signal peptidase HAMAP-Rule MF_00161		PRO_0000289458
Regions
	Transmembrane	10 – 30	21	Helical; Potential
	Transmembrane	68 – 88	21	Helical; Potential
	Transmembrane	98 – 118	21	Helical; Potential
	Transmembrane	138 – 158	21	Helical; Potential
Sites
	Active site	115	1	By similarity
	Active site	142	1	By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q8PN18 [UniParc]. Last modified October 1, 2002. Version 1. Checksum: D8CE34A8637ABD22	FASTA	172	18,918
	10 20 30 40 50 60 MSQRPNPSAL IWLLLSALVV GLDQWSKAWV LSSLPEYTPV PVIDGFWNWY RTYNTGAAFS 70 80 90 100 110 120 FLSDAGGWQL WFFTALAVGI SGLLAFWLSR TARGQWRSAL PYALVIGGAI GNVIDRLMHG 130 140 150 160 170 HVVDFIQWYI GSHTWPSFNI ADSAIVGGAI GIAVFGLFDK SDKQQPGTGN LR

References

[1]

"Comparison of the genomes of two Xanthomonas pathogens with differing host specificities." da Silva A.C.R., Ferro J.A., Reinach F.C., Farah C.S., Furlan L.R., Quaggio R.B., Monteiro-Vitorello C.B., Van Sluys M.A., Almeida N.F. Jr., Alves L.M.C., do Amaral A.M., Bertolini M.C., Camargo L.E.A., Camarotte G., Cannavan F., Cardozo J., Chambergo F., Ciapina L.P. , Cicarelli R.M.B., Coutinho L.L., Cursino-Santos J.R., El-Dorry H., Faria J.B., Ferreira A.J.S., Ferreira R.C.C., Ferro M.I.T., Formighieri E.F., Franco M.C., Greggio C.C., Gruber A., Katsuyama A.M., Kishi L.T., Leite R.P., Lemos E.G.M., Lemos M.V.F., Locali E.C., Machado M.A., Madeira A.M.B.N., Martinez-Rossi N.M., Martins E.C., Meidanis J., Menck C.F.M., Miyaki C.Y., Moon D.H., Moreira L.M., Novo M.T.M., Okura V.K., Oliveira M.C., Oliveira V.R., Pereira H.A., Rossi A., Sena J.A.D., Silva C., de Souza R.F., Spinola L.A.F., Takita M.A., Tamura R.E., Teixeira E.C., Tezza R.I.D., Trindade dos Santos M., Truffi D., Tsai S.M., White F.F., Setubal J.C., Kitajima J.P. Nature 417:459-463(2002) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: 306.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AE008923 Genomic DNA. Translation: AAM36127.1.
RefSeq	NP_641591.1. NC_003919.1.
3D structure databases
ModBase	Search...
Protein-protein interaction databases
STRING	190486.XAC1255.
Protein family/group databases
MEROPS	A08.001.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblBacteria	AAM36127; AAM36127; XAC1255.
GeneID	1155326.
KEGG	xac:XAC1255.
PATRIC	24054483. VBIXanAxo33670_1323.
Organism-specific databases
CMR	Search...
Phylogenomic databases
eggNOG	COG0597.
HOGENOM	HOG000096993.
KO	K03101.
OMA	DMSQRPN.
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_XANAC

Accession

Primary (citable) accession number: Q8PN18

Entry history

Integrated into UniProtKB/Swiss-Prot:	May 29, 2007
Last sequence update:	October 1, 2002
Last modified:	May 1, 2013
This is version 67 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program