ID AMPA_RICPR Reviewed; 500 AA. AC P27888; DT 01-AUG-1992, integrated into UniProtKB/Swiss-Prot. DT 01-AUG-1992, sequence version 1. DT 27-MAR-2024, entry version 131. DE RecName: Full=Cytosol aminopeptidase; DE EC=3.4.11.1; DE AltName: Full=Leucine aminopeptidase; DE Short=LAP; DE EC=3.4.11.10; DE AltName: Full=Leucyl aminopeptidase; GN Name=pepA; OrderedLocusNames=RP142; OS Rickettsia prowazekii (strain Madrid E). OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rickettsiales; OC Rickettsiaceae; Rickettsieae; Rickettsia; typhus group. OX NCBI_TaxID=272947; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RC STRAIN=Madrid E; RX PubMed=8416891; DOI=10.1128/jb.175.1.159-165.1993; RA Wood D.O., Solomon M.J., Speed R.R.; RT "Characterization of the Rickettsia prowazekii pepA gene encoding leucine RT aminopeptidase."; RL J. Bacteriol. 175:159-165(1993). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Madrid E; RX PubMed=9823893; DOI=10.1038/24094; RA Andersson S.G.E., Zomorodipour A., Andersson J.O., Sicheritz-Ponten T., RA Alsmark U.C.M., Podowski R.M., Naeslund A.K., Eriksson A.-S., Winkler H.H., RA Kurland C.G.; RT "The genome sequence of Rickettsia prowazekii and the origin of RT mitochondria."; RL Nature 396:133-140(1998). 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. 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 -!- 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 -!- COFACTOR: CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000250}; CC Note=Binds 2 manganese ions per subunit. {ECO:0000250}; CC -!- SUBCELLULAR LOCATION: Cytoplasm. CC -!- SIMILARITY: Belongs to the peptidase M17 family. {ECO:0000305}. 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; M68966; AAA26388.1; -; Genomic_DNA. DR EMBL; AJ235270; CAA14610.1; -; Genomic_DNA. DR PIR; A40631; A40631. DR RefSeq; NP_220533.1; NC_000963.1. DR RefSeq; WP_004597194.1; NC_000963.1. DR AlphaFoldDB; P27888; -. DR SMR; P27888; -. DR STRING; 272947.gene:17555225; -. DR EnsemblBacteria; CAA14610; CAA14610; CAA14610. DR GeneID; 57569270; -. DR KEGG; rpr:RP142; -. DR PATRIC; fig|272947.5.peg.145; -. DR eggNOG; COG0260; Bacteria. DR HOGENOM; CLU_013734_2_2_5; -. DR OrthoDB; 9809354at2; -. DR Proteomes; UP000002480; 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; KW Reference proteome. FT CHAIN 1..500 FT /note="Cytosol aminopeptidase" FT /id="PRO_0000165792" FT ACT_SITE 277 FT /evidence="ECO:0000255" FT ACT_SITE 351 FT /evidence="ECO:0000255" FT BINDING 265 FT /ligand="Mn(2+)" FT /ligand_id="ChEBI:CHEBI:29035" FT /ligand_label="2" FT /evidence="ECO:0000250" FT BINDING 270 FT /ligand="Mn(2+)" FT /ligand_id="ChEBI:CHEBI:29035" FT /ligand_label="1" FT /evidence="ECO:0000250" FT BINDING 270 FT /ligand="Mn(2+)" FT /ligand_id="ChEBI:CHEBI:29035" FT /ligand_label="2" FT /evidence="ECO:0000250" FT BINDING 288 FT /ligand="Mn(2+)" FT /ligand_id="ChEBI:CHEBI:29035" FT /ligand_label="2" FT /evidence="ECO:0000250" FT BINDING 347 FT /ligand="Mn(2+)" FT /ligand_id="ChEBI:CHEBI:29035" FT /ligand_label="1" FT /evidence="ECO:0000250" FT BINDING 349 FT /ligand="Mn(2+)" FT /ligand_id="ChEBI:CHEBI:29035" FT /ligand_label="1" FT /evidence="ECO:0000250" FT BINDING 349 FT /ligand="Mn(2+)" FT /ligand_id="ChEBI:CHEBI:29035" FT /ligand_label="2" FT /evidence="ECO:0000250" SQ SEQUENCE 500 AA; 54006 MW; E87FFDEA47EC7C83 CRC64; MLNINFVNEE SSTNQGLIVF IDEQLKLNNN LIALDQQHYE LISKTIQNKL QFSGNYGQIT VVPSVIKSCA VKYLIIVGLG NVEKLTEAKI EELGGKILQH ATCAKIATIG LKIINRINRF TSPTFTSLIA SGAFLASYRF HKYKTTLKEV EKFAVESIEI LTDNNSEAMK LFEVKKLIAE AVFFTRDISN EPSNIKTPQV YAERIVEILE PLGVNIDVIG EHDIKNLGMG ALLGVGQGSQ NESKLVVMEY KGGSRDDSTL ALVGKGVIFD TGGISLKPSS NMHLMRYDMA GSAAVVGTII ALASQKVPVN VVGVVGLVEN MQSGNAQRPG DVVVTMSGQT AEVLNTDAEG RLVLADTVWY VQEKFNPKCV IDVATLTGAI TVALGSTYAG CFSNNDELAD KLIKAGEAVN EKLWRMPLHD DYDAMINSDI ADIANIGNVP GAAGSCTAAH FIKRFIKDGV DWAHLDIAGV ANSNNASALC PKGAVGYGVR LLEKFIKEYN //