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Q9PH08 (AMPA_XYLFA) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 80. 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:XF_0138
OrganismXylella fastidiosa (strain 9a5c) [Complete proteome] [HAMAP]
Taxonomic identifier160492 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaXanthomonadalesXanthomonadaceaeXylella

Protein attributes

Sequence length491 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 – 491491Probable cytosol aminopeptidase HAMAP-Rule MF_00181
PRO_0000165818

Sites

Active site2761 Potential
Active site3501 Potential
Metal binding2641Manganese 2 By similarity
Metal binding2691Manganese 1 By similarity
Metal binding2691Manganese 2 By similarity
Metal binding2871Manganese 2 By similarity
Metal binding3461Manganese 1 By similarity
Metal binding3481Manganese 1 By similarity
Metal binding3481Manganese 2 By similarity

Sequences

Sequence LengthMass (Da)Tools
Q9PH08 [UniParc].

Last modified October 1, 2000. Version 1.
Checksum: 3D0576F8A7CAF3EE

FASTA49151,723
        10         20         30         40         50         60 
MALQFQLNQT TPQTVTTDCV IVGIYADKTL SPTAKTLDAA SGGRITALTA RGDLTGKSGT 

        70         80         90        100        110        120 
SALLHDLNGV TAPRVLVVGL GEADKFGPGQ YIKAVGDAVR ALKDAPVTHA LLTLSELPVK 

       130        140        150        160        170        180 
DRNAAWNIHQ AVIAADHAAY RYTATLGTSR KKAAESGLIT LAIHGQESSG LTLGQAIAEG 

       190        200        210        220        230        240 
VEYARALGNL PPNICTPVYL AETTAHFAAT HPGATCEILD ESKMEALGMG ALLAVARGSA 

       250        260        270        280        290        300 
NRPRLIVLKW NGGGDARPYV LVGKGITFDT GGVNLKTQGG IEEMKYDMCG GAAVIGTFVA 

       310        320        330        340        350        360 
AVKVRLPLNL IVIVPAVENA IDGNAYRPSD VITSMSGKTI EVGNTDAEGR LILCDALTYA 

       370        380        390        400        410        420 
ERFKPEALID VATLTGACMI ALGRAATGLM THHDDLANEL LTAGEHVHDR AWRLPLWDEY 

       430        440        450        460        470        480 
QNLLDSTFAD VYNIGGRWGG AITAGCFLSR FTEGQRWAHL DIAGSASNEG KRGMATGRPV 

       490 
GLLTQWLVDR C 

« Hide

References

[1]"The genome sequence of the plant pathogen Xylella fastidiosa."
Simpson A.J.G., Reinach F.C., Arruda P., Abreu F.A., Acencio M., Alvarenga R., Alves L.M.C., Araya J.E., Baia G.S., Baptista C.S., Barros M.H., Bonaccorsi E.D., Bordin S., Bove J.M., Briones M.R.S., Bueno M.R.P., Camargo A.A., Camargo L.E.A. expand/collapse author list , Carraro D.M., Carrer H., Colauto N.B., Colombo C., Costa F.F., Costa M.C.R., Costa-Neto C.M., Coutinho L.L., Cristofani M., Dias-Neto E., Docena C., El-Dorry H., Facincani A.P., Ferreira A.J.S., Ferreira V.C.A., Ferro J.A., Fraga J.S., Franca S.C., Franco M.C., Frohme M., Furlan L.R., Garnier M., Goldman G.H., Goldman M.H.S., Gomes S.L., Gruber A., Ho P.L., Hoheisel J.D., Junqueira M.L., Kemper E.L., Kitajima J.P., Krieger J.E., Kuramae E.E., Laigret F., Lambais M.R., Leite L.C.C., Lemos E.G.M., Lemos M.V.F., Lopes S.A., Lopes C.R., Machado J.A., Machado M.A., Madeira A.M.B.N., Madeira H.M.F., Marino C.L., Marques M.V., Martins E.A.L., Martins E.M.F., Matsukuma A.Y., Menck C.F.M., Miracca E.C., Miyaki C.Y., Monteiro-Vitorello C.B., Moon D.H., Nagai M.A., Nascimento A.L.T.O., Netto L.E.S., Nhani A. Jr., Nobrega F.G., Nunes L.R., Oliveira M.A., de Oliveira M.C., de Oliveira R.C., Palmieri D.A., Paris A., Peixoto B.R., Pereira G.A.G., Pereira H.A. Jr., Pesquero J.B., Quaggio R.B., Roberto P.G., Rodrigues V., de Rosa A.J.M., de Rosa V.E. Jr., de Sa R.G., Santelli R.V., Sawasaki H.E., da Silva A.C.R., da Silva A.M., da Silva F.R., Silva W.A. Jr., da Silveira J.F., Silvestri M.L.Z., Siqueira W.J., de Souza A.A., de Souza A.P., Terenzi M.F., Truffi D., Tsai S.M., Tsuhako M.H., Vallada H., Van Sluys M.A., Verjovski-Almeida S., Vettore A.L., Zago M.A., Zatz M., Meidanis J., Setubal J.C.
Nature 406:151-159(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: 9a5c.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AE003849 Genomic DNA. Translation: AAF82951.1.
PIRF82843.
RefSeqNP_297431.1. NC_002488.3.

3D structure databases

ProteinModelPortalQ9PH08.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING160492.XF0138.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAF82951; AAF82951; XF_0138.
GeneID1125656.
KEGGxfa:XF0138.
PATRIC24130178. VBIXylFas578_0145.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0260.
KOK01255.
OMAKYDWAHL.
OrthoDBEOG6FV8B3.
ProtClustDBPRK00913.

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_XYLFA
AccessionPrimary (citable) accession number: Q9PH08
Entry history
Integrated into UniProtKB/Swiss-Prot: November 8, 2002
Last sequence update: October 1, 2000
Last modified: February 19, 2014
This is version 80 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