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A1K9L5 (AMPA_AZOSB) Reviewed, UniProtKB/Swiss-Prot

Last modified December 14, 2011. Version 34. 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:azo2904
OrganismAzoarcus sp. (strain BH72) [Complete proteome] [HAMAP]
Taxonomic identifier62928 [NCBI]
Taxonomic lineageBacteriaProteobacteriaBetaproteobacteriaRhodocyclalesRhodocyclaceaeAzoarcus

Protein attributes

Sequence length500 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
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 – 500500Probable cytosol aminopeptidase HAMAP MF_00181
PRO_1000019879

Sites

Active site2801 Potential
Active site3541 Potential
Metal binding2681Manganese 2 By similarity
Metal binding2731Manganese 1 By similarity
Metal binding2731Manganese 2 By similarity
Metal binding2911Manganese 2 By similarity
Metal binding3501Manganese 1 By similarity
Metal binding3521Manganese 1 By similarity
Metal binding3521Manganese 2 By similarity

Sequences

Sequence LengthMass (Da)Tools
A1K9L5 [UniParc].

Last modified February 6, 2007. Version 1.
Checksum: A3418B04A52A721E

FASTA50052,409
        10         20         30         40         50         60 
MEFTIKTATP EKVRTGVLVV GLFADGILPP AAHAVDKASK GKLAQLVKRG DLDEKAGAAV 

        70         80         90        100        110        120 
MLHDLAGIAA ERVLVVSLGK SAEFSDKAYR DALNSVAKAL ASGVAKVAAV AIADAELDGR 

       130        140        150        160        170        180 
TLAWRLQQAT RQIADGAYRF DAPKAGAKDA KKERGARKIT LLIGDKVSDE LEAAVRRGQA 

       190        200        210        220        230        240 
VAEGMALAKD LGNLPGNVCT PAYLADTAEA LGKQFKFDVE VLERADMEKL GMGSLLSVAK 

       250        260        270        280        290        300 
GSHIPPKFIV MHYKGGKSKA KPVVLVGKGI TFDTGGISLK PGAEMDEMKY DMCGAASVLG 

       310        320        330        340        350        360 
TFKAIARMAL PLNVVGIVPA TENMPGGNAT RPGDVVTSMS GQTIEILNTD AEGRLILCDA 

       370        380        390        400        410        420 
LTYAERFKPA CVIDIATLTG ACVVALGKIP SGLLANDDDL AAELLKRGTE SGDRAWQLPL 

       430        440        450        460        470        480 
WDEYQDLLKS NFADMANIGG RYGGTITAAC FLARFTKAYK WAHLDIAGTA WVSGDAKGAT 

       490        500 
GRPVPLLAEF LVGRAAAKAD 

« Hide

References

[1]"Complete genome of the mutualistic, N2-fixing grass endophyte Azoarcus sp. strain BH72."
Krause A., Ramakumar A., Bartels D., Battistoni F., Bekel T., Boch J., Boehm M., Friedrich F., Hurek T., Krause L., Linke B., McHardy A.C., Sarkar A., Schneiker S., Syed A.A., Thauer R., Vorhoelter F.-J., Weidner S. expand/collapse author list , Puehler A., Reinhold-Hurek B., Kaiser O., Goesmann A.
Nat. Biotechnol. 24:1385-1391(2006) [PubMed: 17057704] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: BH72.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AM406670 Genomic DNA. Translation: CAL95520.1.
RefSeqYP_934407.1. NC_008702.1.

3D structure databases

ProteinModelPortalA1K9L5.
ModBaseSearch...

Protein-protein interaction databases

STRINGA1K9L5.

Protein family/group databases

MEROPSM17.003.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID4607676.
GenomeReviewsGene locus azo2904 in contig AM406670_GR.
KEGGazo:azo2904.
PATRIC21014230. VBIAzoSp26047_2944.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0260.
HOGENOMHBG742580.
OMAKYDWAHL.
PhylomeDBA1K9L5.
ProtClustDBPRK00913.

Enzyme and pathway databases

BioCycASP62928:AZO2904-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.
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_AZOSB
AccessionPrimary (citable) accession number: A1K9L5
Entry history
Integrated into UniProtKB/Swiss-Prot: January 15, 2008
Last sequence update: February 6, 2007
Last modified: December 14, 2011
This is version 34 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