ID A0A2D7NNT5_9DELT Unreviewed; 499 AA. AC A0A2D7NNT5; DT 25-APR-2018, integrated into UniProtKB/TrEMBL. DT 25-APR-2018, sequence version 1. DT 10-APR-2019, entry version 8. DE RecName: Full=Probable cytosol aminopeptidase {ECO:0000256|HAMAP-Rule:MF_00181}; DE EC=3.4.11.1 {ECO:0000256|HAMAP-Rule:MF_00181}; DE AltName: Full=Leucine aminopeptidase {ECO:0000256|HAMAP-Rule:MF_00181}; DE Short=LAP {ECO:0000256|HAMAP-Rule:MF_00181}; DE EC=3.4.11.10 {ECO:0000256|HAMAP-Rule:MF_00181}; DE AltName: Full=Leucyl aminopeptidase {ECO:0000256|HAMAP-Rule:MF_00181}; GN Name=pepA {ECO:0000256|HAMAP-Rule:MF_00181}; GN ORFNames=CL937_02605 {ECO:0000313|EMBL:MAJ48584.1}; OS Deltaproteobacteria bacterium. OC Bacteria; Proteobacteria; Deltaproteobacteria. OX NCBI_TaxID=2026735 {ECO:0000313|EMBL:MAJ48584.1}; RN [1] {ECO:0000313|EMBL:MAJ48584.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=MED631 {ECO:0000313|EMBL:MAJ48584.1}; RX PubMed=29337314; DOI=10.1038/sdata.2017.203; RA Tully B.J., Graham E.D., Heidelberg J.F.; RT "The reconstruction of 2,631 draft metagenome-assembled genomes from RT the global oceans."; RL Sci. Data 5:170203-170203(2018). 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. CC {ECO:0000256|HAMAP-Rule:MF_00181, ECO:0000256|SAAS:SAAS00727879}. CC -!- CATALYTIC ACTIVITY: CC Reaction=Release of an N-terminal amino acid, Xaa-|-Yaa-, in which CC Xaa is preferably Leu, but may be other amino acids including CC Pro although not Arg or Lys, and Yaa may be Pro. Amino acid CC amides and methyl esters are also readily hydrolyzed, but rates CC on arylamides are exceedingly low.; EC=3.4.11.1; CC Evidence={ECO:0000256|HAMAP-Rule:MF_00181, CC ECO:0000256|SAAS:SAAS01118307}; CC -!- CATALYTIC ACTIVITY: CC Reaction=Release of an N-terminal amino acid, preferentially CC leucine, but not glutamic or aspartic acids.; EC=3.4.11.10; CC Evidence={ECO:0000256|HAMAP-Rule:MF_00181}; CC -!- COFACTOR: CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000256|HAMAP- CC Rule:MF_00181}; CC Note=Binds 2 manganese ions per subunit. {ECO:0000256|HAMAP- CC Rule:MF_00181}; CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00181, CC ECO:0000256|SAAS:SAAS00759153}. CC -!- SIMILARITY: Belongs to the peptidase M17 family. CC {ECO:0000256|HAMAP-Rule:MF_00181, ECO:0000256|SAAS:SAAS00754360}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:MAJ48584.1}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; NZHX01000035; MAJ48584.1; -; Genomic_DNA. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0004177; F:aminopeptidase activity; IEA:UniProtKB-UniRule. DR GO; GO:0030145; F:manganese ion binding; IEA:UniProtKB-UniRule. DR GO; GO:0008235; F:metalloexopeptidase activity; IEA:UniProtKB-UniRule. DR CDD; cd00433; Peptidase_M17; 1. DR HAMAP; MF_00181; Cytosol_peptidase_M17; 1. DR InterPro; IPR011356; Leucine_aapep/pepB. DR InterPro; IPR000819; Peptidase_M17_C. DR InterPro; IPR023042; Peptidase_M17_leu_NH2_pept. DR InterPro; IPR008283; Peptidase_M17_N. DR PANTHER; PTHR11963; PTHR11963; 1. DR Pfam; PF00883; Peptidase_M17; 1. DR Pfam; PF02789; Peptidase_M17_N; 1. DR PRINTS; PR00481; LAMNOPPTDASE. DR PROSITE; PS00631; CYTOSOL_AP; 1. PE 3: Inferred from homology; KW Aminopeptidase {ECO:0000256|HAMAP-Rule:MF_00181, KW ECO:0000256|SAAS:SAAS00754331, ECO:0000313|EMBL:MAJ48584.1}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00181, KW ECO:0000256|SAAS:SAAS00759165}; KW Hydrolase {ECO:0000256|HAMAP-Rule:MF_00181, KW ECO:0000256|SAAS:SAAS00754382}; KW Manganese {ECO:0000256|HAMAP-Rule:MF_00181, KW ECO:0000256|SAAS:SAAS00727876}; KW Metal-binding {ECO:0000256|HAMAP-Rule:MF_00181, KW ECO:0000256|SAAS:SAAS00754372}; KW Protease {ECO:0000256|HAMAP-Rule:MF_00181, KW ECO:0000256|SAAS:SAAS00754389}. FT DOMAIN 343 350 CYTOSOL_AP. {ECO:0000259|PROSITE: FT PS00631}. FT ACT_SITE 275 275 {ECO:0000256|HAMAP-Rule:MF_00181}. FT ACT_SITE 349 349 {ECO:0000256|HAMAP-Rule:MF_00181}. FT METAL 263 263 Manganese 2. {ECO:0000256|HAMAP-Rule: FT MF_00181}. FT METAL 268 268 Manganese 1. {ECO:0000256|HAMAP-Rule: FT MF_00181}. FT METAL 268 268 Manganese 2. {ECO:0000256|HAMAP-Rule: FT MF_00181}. FT METAL 286 286 Manganese 2. {ECO:0000256|HAMAP-Rule: FT MF_00181}. FT METAL 345 345 Manganese 1. {ECO:0000256|HAMAP-Rule: FT MF_00181}. FT METAL 347 347 Manganese 1. {ECO:0000256|HAMAP-Rule: FT MF_00181}. FT METAL 347 347 Manganese 2. {ECO:0000256|HAMAP-Rule: FT MF_00181}. SQ SEQUENCE 499 AA; 53110 MW; 57F514155E63F94D CRC64; MDLKISYSSK GIENEDVEGL IVFLPEKSXT RAAGLSXLPE NLXKIIXTAV REEVXNGKTG SSQRLITGSA KPSQLLLIGV GKKEELNPEI IRRAAGGAGK ALACSKLKSI GVMLSNVLST SSSKECGQWX SEGLQLGAYE FKSYKSSENN SPKNLKVRIL DKDALSSAKA VKLGALRAVS ANLARTLGNT PANDMNPXKL AEEAKNLCKT EGLKYKVIEE KEMKKLGMGM LLGVSQGSIT PAKLIFMEYR HPEAKDTLAV VGKGVTFDSG GISLKPGKSM DEMKFDMCGS AAVLGAMNAV AKIKPKLNVI GVVPATENLP GGNAQRPGDI VTAYNGKKVE ILNTDAEGRL ILGDALSYTI EKYNPVAVVD LATLTGACVV ALGHHATGAL SNHSGFMERI RQAGEKSGDR VWELPNFPEY GELLKGKYGD LQNIGGPAGG TITGGKFLQH FVGDTPWVHL DIAGTAWNVK YVDYHPANGA TGVGVRLLID LISEWRPLN //