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A5IAU5 (AMPA_LEGPC) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 48. 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:LPC_0510
OrganismLegionella pneumophila (strain Corby) [Complete proteome] [HAMAP]
Taxonomic identifier400673 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaLegionellalesLegionellaceaeLegionella

Protein attributes

Sequence length483 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-Rule 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-Rule 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-Rule MF_00181

Subcellular location

Cytoplasm By similarity HAMAP-Rule MF_00181.

Sequence similarities

Belongs to the peptidase M17 family.

Ontologies

Keywords
   Cellular componentCytoplasm
   LigandManganese
Metal-binding
   Molecular functionAminopeptidase
Hydrolase
Protease
   Technical termComplete 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-HAMAP

manganese ion binding

Inferred from electronic annotation. Source: UniProtKB-HAMAP

metalloexopeptidase activity

Inferred from electronic annotation. Source: UniProtKB-HAMAP

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 483483Probable cytosol aminopeptidase HAMAP-Rule MF_00181
PRO_1000203833

Sites

Active site2641 Potential
Active site3381 Potential
Metal binding2521Manganese 2 By similarity
Metal binding2571Manganese 1 By similarity
Metal binding2571Manganese 2 By similarity
Metal binding2751Manganese 2 By similarity
Metal binding3341Manganese 1 By similarity
Metal binding3361Manganese 1 By similarity
Metal binding3361Manganese 2 By similarity

Sequences

Sequence LengthMass (Da)Tools
A5IAU5 [UniParc].

Last modified June 26, 2007. Version 1.
Checksum: 695CC2F46D38ACE6

FASTA48352,613
        10         20         30         40         50         60 
MNYGLTHTPS LTMSECLVLG VFSDLALPDF ATAIDNEQKG LIKKLCQRVP EPGNTVWQTD 

        70         80         90        100        110        120 
VEGHSLLIIQ CGKKEEFSAN SLQKRVGEIT EALIKQRFSS ATVCLPRLNQ ESAEWQLEQM 

       130        140        150        160        170        180 
IVQIDNLRYQ LLDFKTKHAK SHKLESVIFH LPGATEKSLE MAKAIVTGVE FCRDLANMPA 

       190        200        210        220        230        240 
NICTPTYLGE QAISLSKQFD QISCQVMGPE EIKEMGMGAL LAVAQGSDQP PRLIDIHYHG 

       250        260        270        280        290        300 
NKNSTPVILV GKGITFDSGG LSIKPANAMD EMKYDMSGAA SVLGVIKACA LLKLPINLIG 

       310        320        330        340        350        360 
IIASAENLIS GSAVKSGDIV TTMSGQTVEI INTDAEGRLV LADALTYAER YNPDFVIDIA 

       370        380        390        400        410        420 
TLTGAIIVAL GNIATGYMTR DEQLAKSIER AANESQDKVW RMPLDEAYQD ALESPLADMI 

       430        440        450        460        470        480 
NAGFDRSAGS ITAACFLSRF TEKYRWAHLD IAGTAWISGK KRNATGRPVP LLIQLLRHVA 


NSR 

« Hide

References

[1]"Identification and characterization of a new conjugation/ type IVA secretion system (trb/tra) of L. pneumophila Corby localized on a mobile genomic island."
Gloeckner G., Albert-Weissenberger C., Weinmann E., Jacobi S., Schunder E., Steinert M., Buchrieser C., Hacker J., Heuner K.
Submitted (NOV-2006) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: Corby.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000675 Genomic DNA. Translation: ABQ54495.1.
RefSeqYP_001249841.1. NC_009494.2.

3D structure databases

ProteinModelPortalA5IAU5.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING400673.LPC_0510.

Protein family/group databases

MEROPSM17.003.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaABQ54495; ABQ54495; LPC_0510.
GeneID5182305.
KEGGlpc:LPC_0510.
PATRIC22307385. VBILegPne45588_0530.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0260.
HOGENOMHOG000243132.
KOK01255.
OMAMPANICT.
OrthoDBEOG6FV8B3.
ProtClustDBCLSK833523.

Enzyme and pathway databases

BioCycLPNE400673:GCIT-2852-MONOMER.

Family and domain databases

HAMAPMF_00181. Cytosol_peptidase_M17.
InterProIPR011356. Leucine_aapep/pepB.
IPR000819. Peptidase_M17_C.
IPR023042. Peptidase_M17_leu_NH2_pept.
IPR008283. Peptidase_M17_N.
[Graphical view]
PANTHERPTHR11963:SF3. PTHR11963:SF3. 1 hit.
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_LEGPC
AccessionPrimary (citable) accession number: A5IAU5
Entry history
Integrated into UniProtKB/Swiss-Prot: September 22, 2009
Last sequence update: June 26, 2007
Last modified: February 19, 2014
This is version 48 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