ID AMPA_ALISL Reviewed; 502 AA. AC B6EMT2; DT 24-MAR-2009, integrated into UniProtKB/Swiss-Prot. DT 25-NOV-2008, sequence version 1. DT 04-NOV-2026, entry version 76. 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=VSAL_I0526; OS Aliivibrio salmonicida (strain LFI1238) (Vibrio salmonicida (strain OS LFI1238)). OC Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria; Vibrionales; OC Vibrionaceae; Aliivibrio. OX NCBI_TaxID=316275; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=LFI1238; RX PubMed=19099551; DOI=10.1186/1471-2164-9-616; RA Hjerde E., Lorentzen M.S., Holden M.T., Seeger K., Paulsen S., Bason N., RA Churcher C., Harris D., Norbertczak H., Quail M.A., Sanders S., RA Thurston S., Parkhill J., Willassen N.P., Thomson N.R.; RT "The genome sequence of the fish pathogen Aliivibrio salmonicida strain RT LFI1238 shows extensive evidence of gene decay."; RL BMC Genomics 9:616-616(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; FM178379; CAQ78211.1; -; Genomic_DNA. DR RefSeq; WP_012549335.1; NC_011312.1. DR AlphaFoldDB; B6EMT2; -. DR SMR; B6EMT2; -. DR MEROPS; M17.003; -. DR KEGG; vsa:VSAL_I0526; -. DR eggNOG; COG0260; Bacteria. DR HOGENOM; CLU_013734_0_1_6; -. DR OMA; AADHACY; -. DR Proteomes; UP000001730; Chromosome 1. 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; IPR064115; LAP_cs. 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; pepA; 1. DR NCBIfam; NF002074; PRK00913.1-4; 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; KW Reference proteome. FT CHAIN 1..502 FT /note="Probable cytosol aminopeptidase" FT /id="PRO_1000098303" FT ACT_SITE 281 FT /evidence="ECO:0000255|HAMAP-Rule:MF_00181" FT ACT_SITE 355 FT /evidence="ECO:0000255|HAMAP-Rule:MF_00181" FT BINDING 269 FT /ligand="Mn(2+)" FT /ligand_id="ChEBI:CHEBI:29035" FT /ligand_label="2" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00181" FT BINDING 274 FT /ligand="Mn(2+)" FT /ligand_id="ChEBI:CHEBI:29035" FT /ligand_label="1" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00181" FT BINDING 274 FT /ligand="Mn(2+)" FT /ligand_id="ChEBI:CHEBI:29035" FT /ligand_label="2" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00181" FT BINDING 292 FT /ligand="Mn(2+)" FT /ligand_id="ChEBI:CHEBI:29035" FT /ligand_label="2" 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 353 FT /ligand="Mn(2+)" FT /ligand_id="ChEBI:CHEBI:29035" FT /ligand_label="1" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00181" FT BINDING 353 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; 54605 MW; 0C7FAB9734B7BEC1 CRC64; MEFSVKSGSP EKQRSACIVV GVFEPRRLSP IAEQLDKISD GYISSLLRRG DLEGKPGQML LLHQVPNILS ERVLLVGCGK ERELGERQYK DIIKKTISTL NETGSMEAVC FLTELHVKGR DTYWKVRQAV ESTKDSLYTF NQFKSNKPET RRPLRKLVFN VPTRRELSLG EKAINHGLSI SSGVKASKDL GNMPPNVANP AYLASQARRL ADDFETVTTK VIGEEEMKKL GMTSYLAVGQ GSHNESMMSV MEYKGHPNPD AKPIVLIGKG LTFDSGGISL KPSDSMDEMK YDMCGAASVF GAMKALAKLN LPLNVVGILA GCENMPSSNS YRPGDILTTM SGQTVEVLNT DAEGRLVLCD ALTYVERYEP DCVVDVATLT GACVVALGHH INGLLSNHNP LAHELINASE QSGDRAWRLP MSEEYNEQLN SPFADMANIG GKAGGTITAG CFLARFAKKY NWAHIDSAGT AWVSGANKGS TGRPVSLLVQ FLLNRSGPES VE //