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O67868 (AMPA_AQUAE) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 79. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | 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:
Probable cytosol aminopeptidase

EC=3.4.11.1
Alternative name(s):
Leucine aminopeptidase
Short name=LAP
EC=3.4.11.10
Leucyl aminopeptidase
Gene names
Name:pepA
Ordered Locus Names:aq_2099
OrganismAquifex aeolicus (strain VF5)
Taxonomic identifier224324 [NCBI]
Taxonomic lineageBacteriaAquificaeAquificalesAquificaceaeAquifex

Protein attributes

Sequence length493 AA.
Sequence statusComplete.
Protein existenceInferred from homology

General annotation (Comments)

Function

Presumably involved in the processing and regular turnover of intracellular proteins. Catalyzes the removal of unsubstituted N-terminal amino acids from various peptides By similarity. HAMAP MF_00181

Catalytic activity

Release of an N-terminal amino acid, Xaa-|-Yaa-, in which Xaa is preferably Leu, but may be other amino acids including Pro although not Arg or Lys, and Yaa may be Pro. Amino acid amides and methyl esters are also readily hydrolyzed, but rates on arylamides are exceedingly low. HAMAP MF_00181

Release of an N-terminal amino acid, preferentially leucine, but not glutamic or aspartic acids.

Cofactor

Binds 2 manganese ions per subunit By similarity. HAMAP MF_00181

Subcellular location

Cytoplasm By similarity HAMAP MF_00181.

Sequence similarities

Belongs to the peptidase M17 family.

Ontologies

Keywords
   Cellular componentCytoplasm
   LigandManganese
Metal-binding
   Molecular functionAminopeptidase
Hydrolase
Protease
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological processproteolysis

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular componentcytoplasm

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular functionaminopeptidase activity

Inferred from electronic annotation. Source: UniProtKB-KW

manganese ion binding

Inferred from electronic annotation. Source: InterPro

metalloexopeptidase activity

Inferred from electronic annotation. Source: InterPro

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 493493Probable cytosol aminopeptidase HAMAP MF_00181
PRO_0000165717

Sites

Active site2691 Potential
Active site3431 Potential
Metal binding2571Manganese 2 By similarity
Metal binding2621Manganese 1 By similarity
Metal binding2621Manganese 2 By similarity
Metal binding2801Manganese 2 By similarity
Metal binding3391Manganese 1 By similarity
Metal binding3411Manganese 1 By similarity
Metal binding3411Manganese 2 By similarity

Sequences

Sequence LengthMass (Da)Tools
O67868 [UniParc].

Last modified August 1, 1998. Version 1.
Checksum: A32B499C7A52065B

FASTA49354,543
        10         20         30         40         50         60 
MKEMEVRAFK DDIKKYKGKS VAVFVYEGDL KPLARLSKGT SNKAKRVAEL ENFKGKEGEI 

        70         80         90        100        110        120 
LKVPTLGTSV DFVYIVGLGK KEKVGEDTYR RASANLVKRM RRDKVESTVV VIPRRGDVSK 

       130        140        150        160        170        180 
EITKAITEGA ILGNYRFDKY KSKKEDEKFE IKEVLINRGD EEGIRLGKIF AEAQNYARNL 

       190        200        210        220        230        240 
VNEPGNVINP ITLAEEAKKL AEEFGLECKV YDEKQIQEMG MMALYSVGKG SATPPRFIHL 

       250        260        270        280        290        300 
IYKPSGKPKE KIALVGKGLT FDSGGLNIKP GDYMRTMKMD KSGACAVLGI MRAIAQLKPD 

       310        320        330        340        350        360 
VEVHGLIGAA ENMPDGNAYR PDDVIKAKNG KYIEIDNTDA EGRVTLADVL SYASELKPDK 

       370        380        390        400        410        420 
IIDMATLTGA CMVALGEYTA GLFTNAPDFA EEIKKTAKRT GERVWELPMD DERLRKKIKN 

       430        440        450        460        470        480 
TVADVLNTGG RYGGAITAAM FLEEFVGEGI KWVHLDIAGP AWSKEEYGYY TKGGTGFGVR 

       490 
TCLEYIMKVS SNV 

« Hide

References

[1]"The complete genome of the hyperthermophilic bacterium Aquifex aeolicus."
Deckert G., Warren P.V., Gaasterland T., Young W.G., Lenox A.L., Graham D.E., Overbeek R., Snead M.A., Keller M., Aujay M., Huber R., Feldman R.A., Short J.M., Olsen G.J., Swanson R.V.
Nature 392:353-358(1998) [PubMed: 9537320] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: VF5.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AE000657 Genomic DNA. Translation: AAC07829.1.
PIRH70479.
RefSeqNP_214437.1. NC_000918.1.

3D structure databases

ProteinModelPortalO67868.
ModBaseSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID1193857.
GenomeReviewsGene locus aq_2099 in contig AE000657_GR.
KEGGaae:aq_2099.
NMPDRfig|224324.1.peg.1452.
PATRIC20961052. VBIAquAeo85532_1619.

Phylogenomic databases

HOGENOMHBG742580.
OMANMHLMRY.
PhylomeDBO67868.
ProtClustDBPRK00913.

Enzyme and pathway databases

BioCycAAEO224324:AQ_2099-MONOMER.

Family and domain databases

HAMAPMF_00181. Cytosol_peptidase_M17.
[Tree]
InterProIPR011356. Peptidase_M17.
IPR000819. Peptidase_M17_C.
IPR023042. Peptidase_M17_cytosol_amino.
IPR008283. Peptidase_M17_N.
[Graphical view]
KOK01255.
PfamPF00883. Peptidase_M17. 1 hit.
PF02789. Peptidase_M17_N. 1 hit.
[Graphical view]
PRINTSPR00481. LAMNOPPTDASE.
PROSITEPS00631. CYTOSOL_AP. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameAMPA_AQUAE
AccessionPrimary (citable) accession number: O67868
Entry history
Integrated into UniProtKB/Swiss-Prot: December 1, 2000
Last sequence update: August 1, 1998
Last modified: January 25, 2012
This is version 79 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

Peptidase families

Classification of peptidase families and list of entries

SIMILARITY comments

Index of protein domains and families