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A3M1A8 (AMPA_ACIBT) Reviewed, UniProtKB/Swiss-Prot

Last modified December 14, 2011. Version 40. 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:A1S_0227
OrganismAcinetobacter baumannii (strain ATCC 17978 / NCDC KC 755) [Complete proteome] [HAMAP]
Taxonomic identifier400667 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaPseudomonadalesMoraxellaceaeAcinetobacterAcinetobacter calcoaceticus/baumannii complex

Protein attributes

Sequence length482 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 – 482482Probable cytosol aminopeptidase HAMAP MF_00181
PRO_1000098298

Sites

Active site2631 Potential
Active site3371 Potential
Metal binding2511Manganese 2 By similarity
Metal binding2561Manganese 1 By similarity
Metal binding2561Manganese 2 By similarity
Metal binding2741Manganese 2 By similarity
Metal binding3331Manganese 1 By similarity
Metal binding3351Manganese 1 By similarity
Metal binding3351Manganese 2 By similarity

Sequences

Sequence LengthMass (Da)Tools
A3M1A8 [UniParc].

Last modified September 2, 2008. Version 2.
Checksum: E11507C7B3B71401

FASTA48252,177
        10         20         30         40         50         60 
MKFTTYTTFP EQTSNESLWI LVDSEQLQSN LNTYQINNLE SILTATQFKA NFNETLPLFG 

        70         80         90        100        110        120 
QLSTQPHSQL LGLGKAAELQ AAKLAKLAQT IIKSAQNKFK HIAIDIAALP VEYHYLFALS 

       130        140        150        160        170        180 
LTQAAYGYDE FKSKKNEFVL QQVDLISSQT SLDENQLALV HAVQSGQSYA RDLGNRPGNI 

       190        200        210        220        230        240 
CFPEYLAEQA LALAAEFPDL LKVTVLNEQQ MADLGMYAFL AVSKGSERPG RIVTLEYQAQ 

       250        260        270        280        290        300 
LEQAPVVLVG KGVTFDTGGI SLKPGLGMDE MKFDMCGAAS VLGTIRALCE ARLPIHVVGA 

       310        320        330        340        350        360 
IAAAENMPSG KATRPGDIVT TMSGQTVEIL NTDAEGRLVL CDTLTYIKRF NPAVVIDIAT 

       370        380        390        400        410        420 
LTGACVVALG KVLSGLFSPD DTLAAELQQA GEQSFDRVWR MPVIDDYQEL LDSPFADIAN 

       430        440        450        460        470        480 
IGGPHGGAIT AACFLERFTR DYRWAHLDVA GTAWLSGSAK GATGRPVPLL MQFLANRVST 


NG 

« Hide

References

[1]"New insights into Acinetobacter baumannii pathogenesis revealed by high-density pyrosequencing and transposon mutagenesis."
Smith M.G., Gianoulis T.A., Pukatzki S., Mekalanos J.J., Ornston L.N., Gerstein M., Snyder M.
Genes Dev. 21:601-614(2007) [PubMed: 17344419] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 17978 / NCDC KC 755.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000521 Genomic DNA. Translation: ABO10702.2.
RefSeqYP_001083304.1. NC_009085.1.

3D structure databases

ProteinModelPortalA3M1A8.
ModBaseSearch...

Protein-protein interaction databases

STRINGA3M1A8.

Protein family/group databases

MEROPSM17.003.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID4918337.
GenomeReviewsGene locus A1S_0227 in contig CP000521_GR.
KEGGacb:A1S_0227.
NMPDRfig|400667.4.peg.241.
PATRIC20716581. VBIAciBau103176_0235.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0260.
HOGENOMHBG742580.
ProtClustDBPRK00913.

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_ACIBT
AccessionPrimary (citable) accession number: A3M1A8
Entry history
Integrated into UniProtKB/Swiss-Prot: March 24, 2009
Last sequence update: September 2, 2008
Last modified: December 14, 2011
This is version 40 of the entry and version 2 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