ID AMPA_BURPS STANDARD; PRT; 503 AA. AC Q63WC3; DT 01-FEB-2005 (Rel. 46, Created) DT 01-FEB-2005 (Rel. 46, Last sequence update) DT 01-FEB-2005 (Rel. 46, Last annotation update) DE Probable cytosol aminopeptidase (EC 3.4.11.1) (Leucine aminopeptidase) DE (LAP) (Leucyl aminopeptidase). GN Name=pepA; OrderedLocusNames=BPSL0965; OS Burkholderia pseudomallei (Pseudomonas pseudomallei). OC Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales; OC Burkholderiaceae; Burkholderia. OX NCBI_TaxID=28450; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=K96243; RX PubMed=15377794; DOI=10.1073/pnas.0403302101; RA Holden M.T.G., Titball R.W., Peacock S.J., Cerdeno-Tarraga A.-M., RA Atkins T., Crossman L.C., Pitt T., Churcher C., Mungall K.L., RA Bentley S.D., Sebaihia M., Thomson N.R., Bason N., Beacham I.R., RA Brooks K., Brown K.A., Brown N.F., Challis G.L., Cherevach I., RA Chillingworth T., Cronin A., Crossett B., Davis P., DeShazer D., RA Feltwell T., Fraser A., Hance Z., Hauser H., Holroyd S., Jagels K., RA Keith K.E., Maddison M., Moule S., Price C., Quail M.A., RA Rabbinowitsch E., Rutherford K., Sanders M., Simmonds M., RA Songsivilai S., Stevens K., Tumapa S., Vesaratchavest M., RA Whitehead S., Yeats C., Barrell B.G., Oyston P.C.F., Parkhill J.; RT "Genomic plasticity of the causative agent of melioidosis, RT Burkholderia pseudomallei."; RL Proc. Natl. Acad. Sci. U.S.A. 101:14240-14245(2004). CC -!- FUNCTION: Presumably involved in the processing and regular CC turnover of intracellular proteins. Catalyzes the removal of CC unsubstituted N-terminal amino acids from various peptides (By CC similarity). CC -!- CATALYTIC ACTIVITY: Release of an N-terminal amino acid, Xaa-|- CC Yaa-, in which Xaa is preferably Leu, but may be other amino acids CC including Pro although not Arg or Lys, and Yaa may be Pro. Amino CC acid amides and methyl esters are also readily hydrolyzed, but CC rates on arylamides are exceedingly low. CC -!- COFACTOR: Binds 2 manganese ions per subunit (By similarity). CC -!- SUBCELLULAR LOCATION: Cytoplasmic (By similarity). CC -!- SIMILARITY: Belongs to the peptidase M17 family. CC -------------------------------------------------------------------------- CC This Swiss-Prot entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use as long as its content is in no way modified and this statement is not CC removed. CC -------------------------------------------------------------------------- DR EMBL; BX571965; CAH34961.1; -. DR HAMAP; MF_00181; -; 1. DR InterPro; IPR011356; Peptidase_M17. DR InterPro; IPR000819; Peptidase_M17_C. DR InterPro; IPR008283; Peptidase_M17_N. DR Pfam; PF00883; Peptidase_M17; 1. DR Pfam; PF02789; Peptidase_M17_N; 1. DR PIRSF; PIRSF001116; Ctsl_amnpptdse; 1. DR PRINTS; PR00481; LAMNOPPTDASE. DR PROSITE; PS00631; CYTOSOL_AP; 1. KW Aminopeptidase; Complete proteome; Hydrolase; Manganese; Protease. FT ACT_SITE 286 286 Potential. FT ACT_SITE 360 360 Potential. FT METAL 274 274 Manganese 2 (By similarity). FT METAL 279 279 Manganese 1 and 2 (By similarity). FT METAL 297 297 Manganese 2 (By similarity). FT METAL 356 356 Manganese 1 (By similarity). FT METAL 358 358 Manganese 1 and 2 (By similarity). SQ SEQUENCE 503 AA; 52653 MW; A641EACDE75CEC4F CRC64; MDFSIKGCDW SKGTANGFLT GKSDCIVLGV FEAQTLSGAA LDIDEATKGL VSRVIKAGDI DGKLGKTLFL HEVSGIGASR VLLVGLGRQD AFSQKAYGDA AKAAWRALLG TKVVQVTFTL AQLPVPERAS DWGVRAAILA LRNETYKFTQ MKSKPDAGAP ALKRVVFSVD PADDKAAKVA AKQAVALANG MDLTRDLGNL PGNVCTPTYL ANTAKKIAKD WGLKVDVLGL KQIQALKMGS FLSVAKGSVE PPQFIVLQYR GAAAKAAPVV LVGKGITFDS GGISLKPGEG MDEMKYDMCG AGSVLGTMRA VAEMGLKVNV VAIVPTCENM PAGNANKPGD IVTSMKGLTI EVLNTDAEGR LILCDALTYA ERFKPAAVID VATLTGACII ALGHHNTGLF SKDDALAGEL LDASREAGDP AWRLPLDDEY QDQLKSNFAD LANIGGRPAG SVTAACFLSR FAENYPWAHL DIAGTAWKSG AAKGATGRPV PLLAQFLIDR AGA //