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Reviewed, UniProtKB/Swiss-Prot Q1IPU7 (AMPA_ACIBL)

Last modified January 19, 2010. Version 31. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

Names and origin

Protein namesRecommended name:
    Probable cytosol aminopeptidase
    EC=3.4.11.1
Alternative name(s):
    Leucine aminopeptidase
      Short name=LAP
    Leucyl aminopeptidase
Gene names
Name: pepA
Ordered Locus Names: Acid345_2102
OrganismAcidobacteria bacterium (strain Ellin345) [Complete proteome] [HAMAP]
Taxonomic identifier204669 [NCBI]
Taxonomic lineageBacteriaAcidobacteriaCandidatus Koribacter

Protein attributes

Sequence length512 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

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
Gene Ontology (GO)
   Biological processproteolysis

Inferred from electronic annotation. Source: InterPro

   Cellular componentcytoplasm

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular functionaminopeptidase activity

Inferred from electronic annotation. Source: HAMAP

manganese ion binding

Inferred from electronic annotation. Source: HAMAP

metalloexopeptidase activity

Inferred from electronic annotation. Source: HAMAP

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 512512Probable cytosol aminopeptidase HAMAP MF_00181
PRO_1000019873

Sites

Active site2931 Potential
Active site3671 Potential
Metal binding2811Manganese 2 By similarity
Metal binding2861Manganese 1 By similarity
Metal binding2861Manganese 2 By similarity
Metal binding3041Manganese 2 By similarity
Metal binding3631Manganese 1 By similarity
Metal binding3651Manganese 1 By similarity
Metal binding3651Manganese 2 By similarity

Sequences

Sequence LengthMass (Da)Tools
Q1IPU7-1 [UniParc].

Last modified June 13, 2006. Version 1.
Checksum: 13B78F4597A895D4

FASTA51254,376
        10         20         30         40         50         60 
MKIHLSTLDP AQLETDALIV LAIDGGDKDN NKPQLQAKSD AFAKAAADLI ASKEITGKLL 

        70         80         90        100        110        120 
EIATLHKPEG VKAKRLIVVG VGKAKSFTSY ELRKAAGAAV RALKKSVKSA AIVAPENWGG 

       130        140        150        160        170        180 
AADPSTTSTL MFERGGLPEA VKAIAEGAVV ANPDYNYYHS DRKTYELDEL TILVPANGHA 

       190        200        210        220        230        240 
NDLEAAMKEG HVIGESQNFT RDLVNEPGNR MTPTILGQRA KKMAEEVGIQ CDVYSTDFLH 

       250        260        270        280        290        300 
EKKMGAFWSV SQGSEEPPAL IVMKYEPAGA PQSPVLGLVG KGITFDTGGI SIKPADGMEK 

       310        320        330        340        350        360 
MKYDMAGGAA MIGAMRAIAL LKPNVRVIGV VCAAENMPSG KAQKPGDVQI AMSGKSIEII 

       370        380        390        400        410        420 
NTDAEGRLVL ADGLHYAKQL GATHLIDAAT LTGACMVALG GINAGVFAND EDYFNRFAEA 

       430        440        450        460        470        480 
LKKSGEKMWR LPIDDDYKEL IKSPIADIKN TGGRYGGAIT AAMFLKEFVG ETPWIHLDIA 

       490        500        510 
GVAWQEEAVP FLAKGPSGIA VRSIIELVQS FG 

« Hide

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000360 Genomic DNA. Translation: ABF41103.1.
RefSeqYP_591177.1.

3D structure databases

SMRQ1IPU7. Positions 15-511.
ModBaseSearch...

Protein-protein interaction databases

STRINGQ1IPU7.

Protein family/group databases

MEROPSM17.010.

Genome annotation databases

GeneID4069701.
GenomeReviewsGene locus Acid345_2102 in contig CP000360_GR.
KEGGaba:Acid345_2102.
NMPDRfig|204669.6.peg.2087.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0260.
HOGENOMHBG742580.
OMAEGHAIMA.
PhylomeDBQ1IPU7.

Enzyme and pathway databases

BioCycABAC204669:ACID345_2102-MONOMER.

Family and domain databases

HAMAPMF_00181. Cytosol_peptidase_M17.
[Tree]
InterProIPR011356. Peptidase_M17.
IPR000819. Peptidase_M17_C.
IPR008283. Peptidase_M17_N.
[Graphical view]
PANTHERPTHR11963:SF3. Peptidase_M17. 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_ACIBL
AccessionPrimary (citable) accession number: Q1IPU7
Entry history
Integrated into UniProtKB/Swiss-Prot: January 15, 2008
Last sequence update: June 13, 2006
Last modified: January 19, 2010
This is version 31 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHAMAP (High-quality Automated and Manual Annotation of microbial Proteomes)

Relevant documents

Peptidase families

Classification of peptidase families and list of entries

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents