ID   AMPA_MYCPN              Reviewed;         445 AA.
AC   P75206;
DT   01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1997, sequence version 1.
DT   03-AUG-2022, entry version 121.
DE   RecName: Full=Probable 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=MPN_572; ORFNames=MP270;
OS   Mycoplasma pneumoniae (strain ATCC 29342 / M129) (Mycoplasmoides
OS   pneumoniae).
OC   Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mycoplasma.
OX   NCBI_TaxID=272634;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 29342 / M129;
RX   PubMed=8948633; DOI=10.1093/nar/24.22.4420;
RA   Himmelreich R., Hilbert H., Plagens H., Pirkl E., Li B.-C., Herrmann R.;
RT   "Complete sequence analysis of the genome of the bacterium Mycoplasma
RT   pneumoniae.";
RL   Nucleic Acids Res. 24:4420-4449(1996).
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 (By similarity).
CC       {ECO:0000250}.
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 {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the peptidase M17 family. {ECO:0000305}.
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DR   EMBL; U00089; AAB95918.1; -; Genomic_DNA.
DR   PIR; S73596; S73596.
DR   RefSeq; NP_110261.1; NC_000912.1.
DR   RefSeq; WP_010874929.1; NC_000912.1.
DR   AlphaFoldDB; P75206; -.
DR   SMR; P75206; -.
DR   STRING; 272634.MPN_572; -.
DR   PRIDE; P75206; -.
DR   EnsemblBacteria; AAB95918; AAB95918; MPN_572.
DR   GeneID; 66608745; -.
DR   KEGG; mpn:MPN_572; -.
DR   PATRIC; fig|272634.6.peg.634; -.
DR   HOGENOM; CLU_013734_6_3_14; -.
DR   OMA; QWAFAQG; -.
DR   BioCyc; MPNE272634:G1GJ3-937-MON; -.
DR   Proteomes; UP000000808; 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   HAMAP; MF_00181; Cytosol_peptidase_M17; 1.
DR   InterPro; IPR011356; Leucine_aapep/pepB.
DR   InterPro; IPR000819; Peptidase_M17_C.
DR   InterPro; IPR023042; Peptidase_M17_leu_NH2_pept.
DR   PANTHER; PTHR11963; PTHR11963; 1.
DR   Pfam; PF00883; Peptidase_M17; 1.
DR   PRINTS; PR00481; LAMNOPPTDASE.
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..445
FT                   /note="Probable cytosol aminopeptidase"
FT                   /id="PRO_0000165768"
FT   ACT_SITE        229
FT                   /evidence="ECO:0000255"
FT   ACT_SITE        303
FT                   /evidence="ECO:0000255"
FT   BINDING         217
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250"
FT   BINDING         222
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250"
FT   BINDING         222
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250"
FT   BINDING         240
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250"
FT   BINDING         299
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250"
FT   BINDING         301
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250"
FT   BINDING         301
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   445 AA;  48789 MW;  9CE6A05822C4D8E2 CRC64;
     MKLNKLFDSK TVVFKKSDKY GKSDCCKTKC VEGQIEFGVK IPTDFPAFNR ALVTFLKTQK
     NQLNVDLDSF VELYKAENLC YKTALKVVVA SITFCETTPF TMKTEPQKNV EVAVKCDSEH
     TSLIKEYEVV GNYVNMARQL QDTPSDQLYP EEFVKRFEKA ATGLGVKITV LKQADLIKKK
     MGLLLGVNKG SEREARLLVI SYNNNKKSSE TLALVGKGIT YDSGGMNIKT GDYMRGMKYD
     MSGAAIVCST VLALAKNKVK TNVVAVAALT ENLPGPHAQR PDDIQTAYNG KTVEIDNTDA
     EGRLVLADAI SYAAKDLKAT QIIDVATLTG LMSYILSTTY TGIFSTCDMA WDAFKKAACC
     AGEPVWRLPM HPDYLKPLES KLADLQNSTS VKGAGSSRAA CFLAEFREGV PLIHCDIAST
     ASIQDLGQGV LVRTLYERAA QQAKE