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Q3MA96 (LSPA_ANAVT) Reviewed, UniProtKB/Swiss-Prot

Last modified May 14, 2014. Version 57. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended 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:Ava_2475
OrganismAnabaena variabilis (strain ATCC 29413 / PCC 7937) [Complete proteome] [HAMAP]
Taxonomic identifier240292 [NCBI]
Taxonomic lineageBacteriaCyanobacteriaNostocalesNostocaceaeAnabaena

Protein attributes

Sequence length158 AA.
Sequence statusComplete.
Protein existenceInferred 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 componentCell inner membrane
Cell membrane
Membrane
   DomainTransmembrane
Transmembrane helix
   Molecular functionAspartyl protease
Hydrolase
Protease
   Technical termComplete proteome
Gene Ontology (GO)
   Cellular_componentintegral component of membrane

Inferred from electronic annotation. Source: UniProtKB-KW

plasma membrane

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular_functionaspartic-type endopeptidase activity

Inferred from electronic annotation. Source: UniProtKB-HAMAP

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 158158Lipoprotein signal peptidase HAMAP-Rule MF_00161
PRO_1000038778

Regions

Transmembrane7 – 2721Helical; Potential
Transmembrane38 – 5821Helical; Potential
Transmembrane67 – 8721Helical; Potential
Transmembrane95 – 11521Helical; Potential
Transmembrane125 – 14521Helical; Potential

Sites

Active site1071 By similarity
Active site1321 By similarity

Sequences

Sequence LengthMass (Da)Tools
Q3MA96 [UniParc].

Last modified October 25, 2005. Version 1.
Checksum: D42151194AB70B57

FASTA15817,771
        10         20         30         40         50         60 
MRFKNRLFWI AAFIAFFVDQ LTKYWVVQTF SLGETLPILP GIFHFTYVTN TGAAFSLFSG 

        70         80         90        100        110        120 
KVEWLRWLSL GVSLLLIGLA LLGPVLERWD QLGYGLILGG AMGNGIDRFA LGYVVDFLDF 

       130        140        150 
RLINFAVFNM ADSFISIGIV CLLLASLQKS PDSHHRSR 

« Hide

References

[1]"Complete sequence of Anabaena variabilis ATCC 29413."
Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina T., Hammon N., Israni S., Pitluck S., Saunders E.H., Schmutz J., Larimer F., Land M., Kyrpides N., Mavrommatis K., Richardson P.
Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 29413 / PCC 7937.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000117 Genomic DNA. Translation: ABA22090.1.
RefSeqYP_322985.1. NC_007413.1.

3D structure databases

ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING240292.Ava_2475.

Protein family/group databases

MEROPSA08.001.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaABA22090; ABA22090; Ava_2475.
GeneID3682826.
KEGGava:Ava_2475.
PATRIC35425799. VBIAnaVar43351_3449.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0597.
HOGENOMHOG000096992.
KOK03101.
OMAKADNANP.
OrthoDBEOG6PGKBM.

Enzyme and pathway databases

BioCycAVAR240292:GCY3-2503-MONOMER.
UniPathwayUPA00665.

Family and domain databases

HAMAPMF_00161. LspA.
InterProIPR001872. Peptidase_A8.
[Graphical view]
PfamPF01252. Peptidase_A8. 1 hit.
[Graphical view]
PRINTSPR00781. LIPOSIGPTASE.
TIGRFAMsTIGR00077. lspA. 1 hit.
PROSITEPS00855. SPASE_II. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameLSPA_ANAVT
AccessionPrimary (citable) accession number: Q3MA96
Entry history
Integrated into UniProtKB/Swiss-Prot: January 15, 2008
Last sequence update: October 25, 2005
Last modified: May 14, 2014
This is version 57 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

Peptidase families

Classification of peptidase families and list of entries

PATHWAY comments

Index of metabolic and biosynthesis pathways