ID AMPA_AERS4 Reviewed; 502 AA. AC A4SSA7; DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot. DT 15-MAY-2007, sequence version 1. DT 02-SEP-2026, entry version 92. DE RecName: Full=Probable cytosol aminopeptidase {ECO:0000255|HAMAP-Rule:MF_00181}; DE EC=3.4.11.1 {ECO:0000255|HAMAP-Rule:MF_00181}; DE AltName: Full=Leucine aminopeptidase {ECO:0000255|HAMAP-Rule:MF_00181}; DE Short=LAP {ECO:0000255|HAMAP-Rule:MF_00181}; DE EC=3.4.11.10 {ECO:0000255|HAMAP-Rule:MF_00181}; DE AltName: Full=Leucyl aminopeptidase {ECO:0000255|HAMAP-Rule:MF_00181}; GN Name=pepA {ECO:0000255|HAMAP-Rule:MF_00181}; GN OrderedLocusNames=ASA_3823; OS Aeromonas salmonicida (strain A449). OC Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria; OC Aeromonadales; Aeromonadaceae; Aeromonas. OX NCBI_TaxID=382245; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=A449; RX PubMed=18801193; DOI=10.1186/1471-2164-9-427; RA Reith M.E., Singh R.K., Curtis B., Boyd J.M., Bouevitch A., Kimball J., RA Munholland J., Murphy C., Sarty D., Williams J., Nash J.H., Johnson S.C., RA Brown L.L.; RT "The genome of Aeromonas salmonicida subsp. salmonicida A449: insights into RT the evolution of a fish pathogen."; RL BMC Genomics 9:427-427(2008). 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:0000255|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; Evidence={ECO:0000255|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:0000255|HAMAP-Rule:MF_00181}; CC -!- COFACTOR: CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000255|HAMAP- CC Rule:MF_00181}; CC Note=Binds 2 manganese ions per subunit. {ECO:0000255|HAMAP- CC Rule:MF_00181}; CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00181}. CC -!- SIMILARITY: Belongs to the peptidase M17 family. {ECO:0000255|HAMAP- CC Rule:MF_00181}. 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; CP000644; ABO91779.1; -; Genomic_DNA. DR RefSeq; WP_005315741.1; NC_009348.1. DR AlphaFoldDB; A4SSA7; -. DR SMR; A4SSA7; -. DR STRING; 29491.GCA_000820065_04182; -. DR MEROPS; M17.003; -. DR KEGG; asa:ASA_3823; -. DR eggNOG; COG0260; Bacteria. DR HOGENOM; CLU_013734_2_2_6; -. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-ARBA. DR GO; GO:0030145; F:manganese ion binding; IEA:UniProtKB-UniRule. DR GO; GO:0070006; F:metalloaminopeptidase activity; IEA:InterPro. DR GO; GO:0006310; P:DNA recombination; IEA:UniProtKB-ARBA. DR GO; GO:0006508; P:proteolysis; IEA:InterPro. DR GO; GO:0006355; P:regulation of DNA-templated transcription; IEA:UniProtKB-ARBA. DR CDD; cd00433; Peptidase_M17; 1. DR FunFam; 3.40.220.10:FF:000001; Probable cytosol aminopeptidase; 1. DR FunFam; 3.40.630.10:FF:000004; Probable cytosol aminopeptidase; 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 NCBIfam; NF002072; PRK00913.1-1; 1. DR NCBIfam; NF002073; PRK00913.1-2; 1. DR NCBIfam; NF002074; PRK00913.1-4; 1. DR NCBIfam; NF002077; PRK00913.2-4; 1. DR PANTHER; PTHR11963:SF23; CYTOSOL AMINOPEPTIDASE; 1. DR PANTHER; PTHR11963; LEUCINE AMINOPEPTIDASE-RELATED; 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; Cytoplasm; Hydrolase; Manganese; Metal-binding; Protease. FT CHAIN 1..502 FT /note="Probable cytosol aminopeptidase" FT /id="PRO_1000019876" FT ACT_SITE 279 FT /evidence="ECO:0000255|HAMAP-Rule:MF_00181" FT ACT_SITE 353 FT /evidence="ECO:0000255|HAMAP-Rule:MF_00181" FT BINDING 267 FT /ligand="Mn(2+)" FT /ligand_id="ChEBI:CHEBI:29035" FT /ligand_label="2" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00181" FT BINDING 272 FT /ligand="Mn(2+)" FT /ligand_id="ChEBI:CHEBI:29035" FT /ligand_label="1" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00181" FT BINDING 272 FT /ligand="Mn(2+)" FT /ligand_id="ChEBI:CHEBI:29035" FT /ligand_label="2" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00181" FT BINDING 290 FT /ligand="Mn(2+)" FT /ligand_id="ChEBI:CHEBI:29035" FT /ligand_label="2" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00181" FT BINDING 349 FT /ligand="Mn(2+)" FT /ligand_id="ChEBI:CHEBI:29035" FT /ligand_label="1" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00181" FT BINDING 351 FT /ligand="Mn(2+)" FT /ligand_id="ChEBI:CHEBI:29035" FT /ligand_label="1" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00181" FT BINDING 351 FT /ligand="Mn(2+)" FT /ligand_id="ChEBI:CHEBI:29035" FT /ligand_label="2" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00181" SQ SEQUENCE 502 AA; 54676 MW; 307109404ED4D70C CRC64; MEFSVKSGSP EKQRSACVVV GVFEPRRLSP VAEQLDKISD GYISSLLRRG DLEGKPGQML LLHQVPGVLS ERVLLVGCGK ERELDERQYK QIINKTITTL NETGSMEAVC FLTELHVKGR DTYWKVRQAV ETTKAGLYNF DQFKTNKAEP RRPLRKLVFN VPTRRELTIG EKAIAHGLAV AKGVRVCRDV ANMPPNVCNP AYLASQARRL ADSFDNITTK VIGEQEMAEL GMNSYLAVAR GSENEAMMAI IEYKGNADAK PIVLVGKGLT FDSGGISIKP AEGMDEMKYD MGGAASVLGT MHALAQLQLP INVIGVLAGC ENMPGGNAYR PGDILTSMSG QTIEVLNTDA EGRLVLCDAL TYVDRYDPET VIDVATLTGA CIIALGHHTT GLLANHNPLA HELLNASEQA GDRAWRLPLF DEYQEQLESP FADMANIGGR PAGTITAAAF LSRFTKKYNW AHLDIAGTAW KSGKDKGSTG RPVPLLTQFL LNRAGVDIEE KE //