(data stored in SCRATCH zone)

HOGENOM: BUPSE2_1_PE1004

ID   BUPSE2_1_PE1004                      STANDARD;      PRT;   503 AA.
AC   BUPSE2_1_PE1004; C4KSK1;
DT   00-JAN-0000 (Rel. 1, Created)
DT   00-JAN-0000 (Rel. 2, Last sequence update)
DT   00-JAN-0000 (Rel. 3, Last annotation update)
DE   RecName: Full=Probable cytosol aminopeptidase; EC=3.4.11 1;AltName:
DE   Full=Leucine aminopeptidase;AltName: Full=Leucyl aminopeptidase;
DE   (BUPSE2_1.PE1004).
GN   Name=pepA; ORFNames=GBP346_A1009;
OS   BURKHOLDERIA PSEUDOMALLEI MSHR346.
OC   Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC   Burkholderiaceae; Burkholderia; pseudomallei group.
OX   NCBI_TaxID=536230;
RN   [0]
RP   -.;
RG   -.;
RL   -.;
CC   -!- SEQ. DATA ORIGIN: Translated from the HOGENOM CDS BUPSE2_1.PE1004.
CC       Burkholderia pseudomallei MSHR346 chromosome I, complete genome.
CC       sequence.
CC   -!- ANNOTATIONS ORIGIN:C4KSK1_BURPS
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   -!- CATALYTIC ACTIVITY: Release of an N-terminal amino acid,
CC       preferentially leucine, but not glutamic or aspartic acids.
CC   -!- COFACTOR: Binds 2 manganese ions per subunit (By similarity).
CC   -!- SUBCELLULAR LOCATION: Cytoplasm (By similarity).
CC   -!- SIMILARITY: Belongs to the peptidase M17 family.
CC   -!- GENE_FAMILY: HOG000243132 [ FAMILY / ALN / TREE ]
DR   UniProtKB/Swiss-Prot; C4KSK1; -.
DR   EMBL; CP001408; ACQ98661.1; -; Genomic_DNA.
DR   RefSeq; YP_002895733.1; NC_012695.1.
DR   ProteinModelPortal; C4KSK1; -.
DR   STRING; C4KSK1; -.
DR   GeneID; 7889339; -.
DR   ProtClustDB; PRK00913; -.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0004177; F:aminopeptidase activity; IEA:HAMAP.
DR   GO; GO:0030145; F:manganese ion binding; IEA:HAMAP.
DR   GO; GO:0008235; F:metalloexopeptidase activity; IEA:HAMAP.
DR   GO; GO:0006508; P:proteolysis; IEA:InterPro.
DR   HAMAP; MF_00181; Cytosol_peptidase_M17; 1; -.
DR   InterPro; IPR011356; Peptidase_M17.
DR   InterPro; IPR000819; Peptidase_M17_C.
DR   InterPro; IPR023042; Peptidase_M17_cytosol_amino.
DR   InterPro; IPR008283; Peptidase_M17_N.
DR   PANTHER; PTHR11963:SF3; Peptidase_M17; 1.
DR   Pfam; PF00883; Peptidase_M17; 1.
DR   Pfam; PF02789; Peptidase_M17_N; 1.
DR   PRINTS; PR00481; LAMNOPPTDASE.
DR   PROSITE; PS00631; CYTOSOL_AP; 1.
DR   HOGENOMDNA; BUPSE2_1.PE1004; -.
KW   leucyl aminopeptidase;
KW   Aminopeptidase; Cytoplasm; Hydrolase; Manganese; Metal-binding;
KW   Protease.
SQ   SEQUENCE   503 AA;  UNKNOWN MW;  UNKNOWN CRC64;
     MDFSIKGCDW SKGTANGFLT GKSDCIVLGV FEAQTLSGAA LDIDEATKGL VSRVIKAGDI
     DGKLGKTLFL HEVSGIGASR VLLVGLGRQD AFSQKAYGDA AKAAWRALLG TKVVQVTFTL
     AQLPVPERAS DWGVRAAILA LRNETYKFTQ MKSKPDAGAP ALKRVVFSVD PADDKAAKVA
     AKQAVALANG MDLTRDLGNL PGNVCTPTYL ANTAKKIAKD WDLKVDVLGL 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
//

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