Detail Information for IndEnz0002014078
IED ID IndEnz0002014078
Enzyme Type ID protease014078
Protein Name Probable cytosol aminopeptidase
EC 3.4.11.1
Leucine aminopeptidase
LAP
EC 3.4.11.10
Leucyl aminopeptidase
Gene Name pepA Cj0929
Organism Campylobacter jejuni subsp. jejuni serotype O:2 (strain ATCC 700819 / NCTC 11168)
Taxonomic Lineage cellular organisms Bacteria Proteobacteria delta/epsilon subdivisions Epsilonproteobacteria Campylobacterales Campylobacteraceae Campylobacter Campylobacter jejuni Campylobacter jejuni subsp. jejuni Campylobacter jejuni subsp. jejuni serotype O:2 (strain ATCC 700819 / NCTC 11168)
Enzyme Sequence MKFELNDKKLDAIKADFELVFIQDKNLKIFNKEKDFFKLNNYKGEGALLDLNNKKLYLELKSLAYEDIRLSLCTAYKTLEKLNIKSVKLPSIIGDCVVRSFASLVEGVLFGAYKFDKYKSEKKTSTLEKFIISNEELNGKKFNKDEAKIGLERGEILANATNFTKNIVNEIPEIYTPLKMAEDAQNLAKENKNIICKIYDEKFLAKEKMNAFLAVNHASVHPPRLIHLSYKAKNAKKRVVFVGKGLTYDSGGLSLKPADFMLTMKADKSGAAAAMGIIKAVAELALDLEVHCILGATENMIGGNAYKPDDVLISREGVSIEVRNTDAEGRLVLADCLSFAQDLKPDLLIDMATLTGACVVGLGEFTSAIMGNNEELQNDFYLSSKKSGEYTTILHFNPHLRELIKSNIADVSNTASSRYGGAITAGLFLDKFIRKEYKDKWLHLDIAGPAYTEKSWGYSSFGAGGAGVRMCVNYLIQILRKAK
Enzyme Length 483
Uniprot Accession Number Q9PP04
Absorption
Active Site ACT_SITE 256; /evidence=ECO:0000255|HAMAP-Rule:MF_00181; ACT_SITE 330; /evidence=ECO:0000255|HAMAP-Rule:MF_00181
Activity Regulation
Binding Site
Calcium Binding
catalytic Activity CATALYTIC ACTIVITY: Reaction=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.; EC=3.4.11.1; Evidence={ECO:0000255|HAMAP-Rule:MF_00181}; CATALYTIC ACTIVITY: Reaction=Release of an N-terminal amino acid, preferentially leucine, but not glutamic or aspartic acids.; EC=3.4.11.10; Evidence={ECO:0000255|HAMAP-Rule:MF_00181};
DNA Binding
EC Number 3.4.11.1; 3.4.11.10
Enzyme Function FUNCTION: Presumably involved in the processing and regular turnover of intracellular proteins. Catalyzes the removal of unsubstituted N-terminal amino acids from various peptides. {ECO:0000255|HAMAP-Rule:MF_00181}.
Temperature Dependency
PH Dependency
Pathway
nucleotide Binding
Features Active site (2); Chain (1); Metal binding (7)
Keywords Aminopeptidase;Cytoplasm;Hydrolase;Manganese;Metal-binding;Protease;Reference proteome
Interact With
Induction
Subcellular Location SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00181}.
Modified Residue
Post Translational Modification
Signal Peptide
Structure 3D
Cross Reference PDB -
Mapped Pubmed ID 17615063; 17667950;
Motif
Gene Encoded By
Mass 53,694
Kinetics
Metal Binding METAL 244; /note=Manganese 2; /evidence=ECO:0000255|HAMAP-Rule:MF_00181; METAL 249; /note=Manganese 1; /evidence=ECO:0000255|HAMAP-Rule:MF_00181; METAL 249; /note=Manganese 2; /evidence=ECO:0000255|HAMAP-Rule:MF_00181; METAL 267; /note=Manganese 2; /evidence=ECO:0000255|HAMAP-Rule:MF_00181; METAL 326; /note=Manganese 1; /evidence=ECO:0000255|HAMAP-Rule:MF_00181; METAL 328; /note=Manganese 1; /evidence=ECO:0000255|HAMAP-Rule:MF_00181; METAL 328; /note=Manganese 2; /evidence=ECO:0000255|HAMAP-Rule:MF_00181
Rhea ID
Cross Reference Brenda