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B5EKZ2 (AMPA_ACIF5) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 22. 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:Lferr_1857
OrganismAcidithiobacillus ferrooxidans (strain ATCC 53993) (Leptospirillum ferrooxidans (ATCC 53993)) [Complete proteome] [HAMAP]
Taxonomic identifier380394 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaAcidithiobacillalesAcidithiobacillaceaeAcidithiobacillus

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_1000098300

Sites

Active site2811 Potential
Active site3551 Potential
Metal binding2691Manganese 2 By similarity
Metal binding2741Manganese 1 By similarity
Metal binding2741Manganese 2 By similarity
Metal binding2921Manganese 2 By similarity
Metal binding3511Manganese 1 By similarity
Metal binding3531Manganese 1 By similarity
Metal binding3531Manganese 2 By similarity

Sequences

Sequence LengthMass (Da)Tools
B5EKZ2 [UniParc].

Last modified October 14, 2008. Version 1.
Checksum: 7E950A380AC66BF1

FASTA50052,844
        10         20         30         40         50         60 
MEIAVQCQNP TTDNSDCVVV GIYEGGILSP AATLVDLASG GALRALLDTG DFTGDCGDTQ 

        70         80         90        100        110        120 
LLYQVPGMAA ARVLVLGLGS HGKVKDSQFR KAALAAARAL QGARVGRASL HLLDTPVIRR 

       130        140        150        160        170        180 
SAPACAKILV QAVADAEYHF DRHKKPADAP QRPISELQLS ISENDTAALA ELQGAVAEAQ 

       190        200        210        220        230        240 
ATARAVAWTR DMANEPGNIC TPTWLAEQAE AMAGRLGIKS TILGPDAMEA LGMHLLLGVA 

       250        260        270        280        290        300 
HGSRQPPRLI ILEYRGGAEN QAPIVLVGKG ITFDAGGISL KPADKMDEMK YDMCGGASAL 

       310        320        330        340        350        360 
AAIQAAAELQ LPLNIVTVVP ASENLPDGQA TKPGDIHRSM NGLSVEVVNT DAEGRLILAD 

       370        380        390        400        410        420 
TLTYVERFEP DVVIDMATLT GACIIALGHQ TAAVMGNHEG LVHDLIAAGK ESMDRVWELP 

       430        440        450        460        470        480 
LFEEYQEQLK SPVADLSNVG GRPAGTITAA CFLSRFTENY RWAHLDIAGV AWKSGEHKGA 

       490        500 
TGRPVPLLVE YLLRRARQVA 

« Hide

References

[1]"Complete sequence of Acidithiobacillus ferrooxidans ATCC 53993."
Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E., Tice H., Bruce D., Goodwin L., Pitluck S., Sims D., Brettin T., Detter J.C., Han C., Kuske C.R., Larimer F., Land M., Hauser L., Kyrpides N., Lykidis A., Borole A.P.
Submitted (AUG-2008) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 53993.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP001132 Genomic DNA. Translation: ACH84078.1.
RefSeqYP_002220285.1. NC_011206.1.

3D structure databases

ProteinModelPortalB5EKZ2.
ModBaseSearch...

Protein-protein interaction databases

STRINGB5EKZ2.

Protein family/group databases

MEROPSM17.003.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID6877841.
GenomeReviewsGene locus Lferr_1857 in contig CP001132_GR.
KEGGafe:Lferr_1857.
PATRIC20661314. VBIAciFer6930_1853.

Organism-specific databases

CMRSearch...

Phylogenomic databases

HOGENOMHBG742580.
OMAKYDWAHL.
ProtClustDBCLSK2408208.

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_ACIF5
AccessionPrimary (citable) accession number: B5EKZ2
Entry history
Integrated into UniProtKB/Swiss-Prot: March 24, 2009
Last sequence update: October 14, 2008
Last modified: January 25, 2012
This is version 22 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