ID A0A2D7NNT5_UNCDE Unreviewed; 499 AA. AC A0A2D7NNT5; DT 25-APR-2018, integrated into UniProtKB/TrEMBL. DT 25-APR-2018, sequence version 1. DT 27-MAR-2024, entry version 19. 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; Myxococcota; Myxococcia. OX NCBI_TaxID=2026735 {ECO:0000313|EMBL:MAJ48584.1, ECO:0000313|Proteomes:UP000226880}; RN [1] {ECO:0000313|Proteomes:UP000226880} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RA Tully B.J., Graham E.D., Heidelberg J.F.; RT "The Reconstruction of 2,631 Draft Metagenome-Assembled Genomes from the RT Global Oceans."; RL Submitted (SEP-2017) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Presumably involved in the processing and regular turnover of CC intracellular proteins. Catalyzes the removal of unsubstituted N- CC terminal amino acids from various peptides. {ECO:0000256|HAMAP- CC Rule:MF_00181}. CC -!- CATALYTIC ACTIVITY: CC Reaction=Release of an N-terminal amino acid, Xaa-|-Yaa-, in which Xaa CC is preferably Leu, but may be other amino acids including Pro CC although not Arg or Lys, and Yaa may be Pro. Amino acid amides and CC methyl esters are also readily hydrolyzed, but rates on arylamides CC are exceedingly low.; EC=3.4.11.1; CC Evidence={ECO:0000256|ARBA:ARBA00000135, ECO:0000256|HAMAP- CC Rule:MF_00181}; CC -!- CATALYTIC ACTIVITY: CC Reaction=Release of an N-terminal amino acid, preferentially leucine, CC but not glutamic or aspartic acids.; EC=3.4.11.10; CC Evidence={ECO:0000256|ARBA:ARBA00000967, ECO:0000256|HAMAP- CC Rule:MF_00181}; CC -!- COFACTOR: CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035; CC Evidence={ECO:0000256|HAMAP-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 -!- SIMILARITY: Belongs to the peptidase M17 family. CC {ECO:0000256|ARBA:ARBA00009528, ECO:0000256|HAMAP-Rule:MF_00181}. CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ CC whole genome shotgun (WGS) entry which is preliminary data. CC {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 Proteomes; UP000226880; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0030145; F:manganese ion binding; IEA:UniProtKB-UniRule. DR GO; GO:0070006; F:metalloaminopeptidase activity; IEA:InterPro. DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW. DR CDD; cd00433; Peptidase_M17; 1. DR Gene3D; 3.40.220.10; Leucine Aminopeptidase, subunit E, domain 1; 1. DR Gene3D; 3.40.630.10; Zn peptidases; 1. DR HAMAP; MF_00181; Cytosol_peptidase_M17; 1. DR InterPro; IPR011356; Leucine_aapep/pepB. DR InterPro; IPR043472; Macro_dom-like. DR InterPro; IPR000819; Peptidase_M17_C. DR InterPro; IPR023042; Peptidase_M17_leu_NH2_pept. DR InterPro; IPR008283; Peptidase_M17_N. DR PANTHER; PTHR11963; LEUCINE AMINOPEPTIDASE-RELATED; 1. DR PANTHER; PTHR11963:SF23; ZGC:152830; 1. DR Pfam; PF00883; Peptidase_M17; 1. DR Pfam; PF02789; Peptidase_M17_N; 1. DR PRINTS; PR00481; LAMNOPPTDASE. DR SUPFAM; SSF52949; Macro domain-like; 1. DR SUPFAM; SSF53187; Zn-dependent exopeptidases; 1. DR PROSITE; PS00631; CYTOSOL_AP; 1. PE 3: Inferred from homology; KW Aminopeptidase {ECO:0000256|ARBA:ARBA00022438, ECO:0000256|HAMAP- KW Rule:MF_00181}; Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00181}; KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|HAMAP-Rule:MF_00181}; KW Manganese {ECO:0000256|HAMAP-Rule:MF_00181}; KW Metal-binding {ECO:0000256|HAMAP-Rule:MF_00181}; KW Protease {ECO:0000256|ARBA:ARBA00022670, ECO:0000256|HAMAP-Rule:MF_00181}. FT DOMAIN 343..350 FT /note="Cytosol aminopeptidase" FT /evidence="ECO:0000259|PROSITE:PS00631" FT ACT_SITE 275 FT /evidence="ECO:0000256|HAMAP-Rule:MF_00181" FT ACT_SITE 349 FT /evidence="ECO:0000256|HAMAP-Rule:MF_00181" FT BINDING 263 FT /ligand="Mn(2+)" FT /ligand_id="ChEBI:CHEBI:29035" FT /ligand_label="2" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00181" FT BINDING 268 FT /ligand="Mn(2+)" FT /ligand_id="ChEBI:CHEBI:29035" FT /ligand_label="2" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00181" FT BINDING 268 FT /ligand="Mn(2+)" FT /ligand_id="ChEBI:CHEBI:29035" FT /ligand_label="1" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00181" FT BINDING 286 FT /ligand="Mn(2+)" FT /ligand_id="ChEBI:CHEBI:29035" FT /ligand_label="2" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00181" FT BINDING 345 FT /ligand="Mn(2+)" FT /ligand_id="ChEBI:CHEBI:29035" FT /ligand_label="1" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00181" FT BINDING 347 FT /ligand="Mn(2+)" FT /ligand_id="ChEBI:CHEBI:29035" FT /ligand_label="1" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00181" FT BINDING 347 FT /ligand="Mn(2+)" FT /ligand_id="ChEBI:CHEBI:29035" FT /ligand_label="2" FT /evidence="ECO:0000256|HAMAP-Rule: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 //