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Q81XS5 (AMPA_BACAN) Reviewed, UniProtKB/Swiss-Prot

Last modified November 16, 2011. Version 64. 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:BA_5155, GBAA_5155, BAS4792
OrganismBacillus anthracis
Taxonomic identifier1392 [NCBI]
Taxonomic lineageBacteriaFirmicutesBacillalesBacillaceaeBacillusBacillus cereus group

Protein attributes

Sequence length494 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
Reference 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 – 494494Probable cytosol aminopeptidase HAMAP MF_00181
PRO_0000165718

Sites

Active site2721 Potential
Active site3461 Potential
Metal binding2601Manganese 2 By similarity
Metal binding2651Manganese 1 By similarity
Metal binding2651Manganese 2 By similarity
Metal binding2831Manganese 2 By similarity
Metal binding3421Manganese 1 By similarity
Metal binding3441Manganese 1 By similarity
Metal binding3441Manganese 2 By similarity

Sequences

Sequence LengthMass (Da)Tools
Q81XS5 [UniParc].

Last modified June 1, 2003. Version 1.
Checksum: D400D6CC81FA31DF

FASTA49453,514
        10         20         30         40         50         60 
MFQVQKELAS HEAVVVALFE EEKTSSFVQE LDKAFEGQLQ VLLEEKELST KKKAISKVHS 

        70         80         90        100        110        120 
LGKTDVKRYY FVGLGKKESY TTETLRSALG KTFKTLQAAK VQDAAILLDS FVTEKLDAID 

       130        140        150        160        170        180 
VAHIAAEVQG LGTYELQTYK SDKKDRVELE KFTAITAEDA QEIEAALTVG YVHGRATNSA 

       190        200        210        220        230        240 
RTLVNMPPNV LTATKLAEYA VELAEKYDMD YKVLEKEEME ELGMGALLAV NQGSVEPPKM 

       250        260        270        280        290        300 
IALIYKGKEE WTDVIGFVGK GITYDTGGYS LKPREGMVGM KGDMGGAAAV LGAMEIIGEL 

       310        320        330        340        350        360 
RPEQNVIAVI PSTDNVVSGT AFKPDDVITS MSGKTIEVLN TDAEGRLALA DGITYAKKLG 

       370        380        390        400        410        420 
ANYLIDVATL TGGVIVALGN HTTGAMTNNE ELFEQVLEAS METDESIWQL PIFDRDKERV 

       430        440        450        460        470        480 
RNSKFADLNN SPGREGHAVM AGTFIGEFAE DTPWVHLDIA GTSESSGAHD LGPAGATGAM 

       490 
VRTLATLVER FGEE 

« Hide

References

[1]"The genome sequence of Bacillus anthracis Ames and comparison to closely related bacteria."
Read T.D., Peterson S.N., Tourasse N.J., Baillie L.W., Paulsen I.T., Nelson K.E., Tettelin H., Fouts D.E., Eisen J.A., Gill S.R., Holtzapple E.K., Okstad O.A., Helgason E., Rilstone J., Wu M., Kolonay J.F., Beanan M.J., Dodson R.J. expand/collapse author list , Brinkac L.M., Gwinn M.L., DeBoy R.T., Madpu R., Daugherty S.C., Durkin A.S., Haft D.H., Nelson W.C., Peterson J.D., Pop M., Khouri H.M., Radune D., Benton J.L., Mahamoud Y., Jiang L., Hance I.R., Weidman J.F., Berry K.J., Plaut R.D., Wolf A.M., Watkins K.L., Nierman W.C., Hazen A., Cline R.T., Redmond C., Thwaite J.E., White O., Salzberg S.L., Thomason B., Friedlander A.M., Koehler T.M., Hanna P.C., Kolstoe A.-B., Fraser C.M.
Nature 423:81-86(2003) [PubMed: 12721629] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: Ames / isolate Porton.
[2]"Bacillus anthracis comparative genomics."
Ravel J., Rasko D.A., Shumway M.F., Jiang L., Cer R.Z., Federova N.B., Wilson M., Stanley S., Decker S., Read T.D., Salzberg S.L., Fraser C.M.
Submitted (MAY-2004) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: Ames ancestor.
[3]"Complete genome sequence of Bacillus anthracis Sterne."
Brettin T.S., Bruce D., Challacombe J.F., Gilna P., Han C., Hill K., Hitchcock P., Jackson P., Keim P., Longmire J., Lucas S., Okinaka R., Richardson P., Rubin E., Tice H.
Submitted (JAN-2004) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: Sterne.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AE016879 Genomic DNA. Translation: AAP28827.1.
AE017334 Genomic DNA. Translation: AAT34284.1.
AE017225 Genomic DNA. Translation: AAT57085.1.
RefSeqNP_847341.1. NC_003997.3.
YP_021809.1. NC_007530.2.
YP_031035.1. NC_005945.1.

3D structure databases

ProteinModelPortalQ81XS5.
ModBaseSearch...

Protein family/group databases

MEROPSM17.010.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaEBBACT00000012243; EBBACP00000011999; EBBACG00000012235.
EBBACT00000014816; EBBACP00000014437; EBBACG00000014808.
EBBACT00000022736; EBBACP00000022221; EBBACG00000022727.
GeneID1084531.
2819349.
2849928.
GenomeReviewsGene locus BA_5155 in contig AE016879_GR.
Gene locus BAS4792 in contig AE017225_GR.
Gene locus GBAA_5155 in contig AE017334_GR.
KEGGban:BA_5155.
bar:GBAA_5155.
bat:BAS4792.
TIGRBA_5155.
GBAA_5155.

Phylogenomic databases

GeneTreeEBGT00050000002613.
HOGENOMHBG742580.
OMAFMINLAT.
ProtClustDBPRK00913.

Enzyme and pathway databases

BioCycBANT260799:BAS4792-MONOMER.
BANT261594:GBAA5155-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_BACAN
AccessionPrimary (citable) accession number: Q81XS5
Secondary accession number(s): Q6HRK3, Q6KKW8
Entry history
Integrated into UniProtKB/Swiss-Prot: December 7, 2004
Last sequence update: June 1, 2003
Last modified: November 16, 2011
This is version 64 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