ID AMPA_HELAH Reviewed; 496 AA. AC Q17W06; DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot. DT 25-JUL-2006, sequence version 1. DT 27-MAR-2024, entry version 98. 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=Hac_1442; OS Helicobacter acinonychis (strain Sheeba). OC Bacteria; Campylobacterota; Epsilonproteobacteria; Campylobacterales; OC Helicobacteraceae; Helicobacter. OX NCBI_TaxID=382638; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Sheeba; RX PubMed=16789826; DOI=10.1371/journal.pgen.0020120; RA Eppinger M., Baar C., Linz B., Raddatz G., Lanz C., Keller H., Morelli G., RA Gressmann H., Achtman M., Schuster S.C.; RT "Who ate whom? Adaptive Helicobacter genomic changes that accompanied a RT host jump from early humans to large felines."; RL PLoS Genet. 2:1097-1110(2006). 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; AM260522; CAK00170.1; -; Genomic_DNA. DR RefSeq; WP_011578260.1; NC_008229.1. DR AlphaFoldDB; Q17W06; -. DR SMR; Q17W06; -. DR STRING; 382638.Hac_1442; -. DR MEROPS; M17.016; -. DR KEGG; hac:Hac_1442; -. DR eggNOG; COG0260; Bacteria. DR HOGENOM; CLU_013734_2_2_7; -. DR OrthoDB; 9809354at2; -. DR BioCyc; HACI382638:HAC_RS06145-MONOMER; -. DR Proteomes; UP000000775; Chromosome. 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; Cytoplasm; Hydrolase; Manganese; Metal-binding; Protease. FT CHAIN 1..496 FT /note="Probable cytosol aminopeptidase" FT /id="PRO_1000019926" FT ACT_SITE 270 FT /evidence="ECO:0000255|HAMAP-Rule:MF_00181" FT ACT_SITE 344 FT /evidence="ECO:0000255|HAMAP-Rule:MF_00181" FT BINDING 258 FT /ligand="Mn(2+)" FT /ligand_id="ChEBI:CHEBI:29035" FT /ligand_label="2" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00181" FT BINDING 263 FT /ligand="Mn(2+)" FT /ligand_id="ChEBI:CHEBI:29035" FT /ligand_label="1" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00181" FT BINDING 263 FT /ligand="Mn(2+)" FT /ligand_id="ChEBI:CHEBI:29035" FT /ligand_label="2" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00181" FT BINDING 281 FT /ligand="Mn(2+)" FT /ligand_id="ChEBI:CHEBI:29035" FT /ligand_label="2" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00181" FT BINDING 340 FT /ligand="Mn(2+)" FT /ligand_id="ChEBI:CHEBI:29035" FT /ligand_label="1" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00181" FT BINDING 342 FT /ligand="Mn(2+)" FT /ligand_id="ChEBI:CHEBI:29035" FT /ligand_label="1" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00181" FT BINDING 342 FT /ligand="Mn(2+)" FT /ligand_id="ChEBI:CHEBI:29035" FT /ligand_label="2" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00181" SQ SEQUENCE 496 AA; 54522 MW; CDCC18C244A6B076 CRC64; MLKIKLEKSA FENAKAECSL VFIVNKDFNH AWVKNKKLLE TFRYEGEDSF LDQENKILYV GVKEDNVHLL RESACSAIRT LKKLAFKSVK VGVYTCHTHS KDNALLENLK ALFLGLKLGM YEYDTFKSNK KESVLKEAII ALELHKPCEE TCANSLEKSA KEALKYADVM TESLNITKNL VNTPPMIGTP IYMAEVAQKV AKEGNLEIHV YDEKFLEEKK MNAFLAVNKA SLGVNPPRLI HLIYKPKKAK KKIALVGKGL TYDCGGLSLK PADYMVTMKA DKGGGSAVIG LLNALSNLGV EAEVHGIIGA TENMIGPAAY KPDDILISKE GKSIEVRNTD AEGRLVLADC LSYAQDLNPD VIVDFATLTG ACVVGLGEFT SAIMGHNEEL KNLFETSGLE SGELLAKLPF NRHLKKLIES KIADVCNVSA SRYGGAITAG LFLNEFIRDE FKDKWLHIDI AGPAYVEKEW DVNSFGASGA GVRACTAFVE ELLKKA //