ID   AMPA_METSV              Reviewed;         520 AA.
AC   P47707;
DT   01-FEB-1996, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1996, sequence version 1.
DT   03-AUG-2022, entry version 96.
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;
OS   Metamycoplasma salivarium (Mycoplasma salivarium).
OC   Bacteria; Tenericutes; Mycoplasmoidales; Metamycoplasmataceae;
OC   Metamycoplasma.
OX   NCBI_TaxID=2124;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=ATCC 23064 / NBRC 14478 / NCTC 10113 / H110;
RX   PubMed=7557291; DOI=10.1016/0378-1097(95)00178-8;
RA   Shibata K.I., Tsuchida N., Watanabe T.;
RT   "Cloning and sequence analysis of the aminopeptidase My gene from
RT   Mycoplasma salivarium.";
RL   FEMS Microbiol. Lett. 130:19-24(1995).
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; D17450; BAA04266.1; -; Genomic_DNA.
DR   AlphaFoldDB; P47707; -.
DR   SMR; P47707; -.
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; -; 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   PANTHER; PTHR11963; PTHR11963; 1.
DR   Pfam; PF00883; Peptidase_M17; 1.
DR   PRINTS; PR00481; LAMNOPPTDASE.
DR   SUPFAM; SSF52949; SSF52949; 1.
DR   PROSITE; PS00631; CYTOSOL_AP; 1.
PE   3: Inferred from homology;
KW   Aminopeptidase; Cytoplasm; Hydrolase; Manganese; Metal-binding; Protease.
FT   CHAIN           1..520
FT                   /note="Probable cytosol aminopeptidase"
FT                   /id="PRO_0000165769"
FT   REGION          488..520
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        489..520
FT                   /note="Basic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        244
FT                   /evidence="ECO:0000255"
FT   ACT_SITE        318
FT                   /evidence="ECO:0000255"
FT   BINDING         232
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250"
FT   BINDING         237
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250"
FT   BINDING         237
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250"
FT   BINDING         255
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250"
FT   BINDING         314
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250"
FT   BINDING         316
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250"
FT   BINDING         316
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   520 AA;  58080 MW;  85A010B93A27A170 CRC64;
     MELIKEIETS RNSSVLLKAI FEGDDAPTLL VKKQSQITEY LKENVAYVYL GKKSEFGYKD
     AYEFARDLAE NCARSYQLDL TTFVTEKLCI KGVVDAFTKG INFSAFQYYN LKTFTKRVNE
     NSLSFYLENI SQDVLNVFKK ALILVDAQNF ARNLGVTPPN ELNSEQLAEI IRKDFKKYHN
     LKVKVLERKQ IELLGMDLLL SVNKGSVYEP RVVIIEYKGN PSSQEKTVLV GKGITFDSGG
     YSLKPPKFML GMKYDMSGSA IVAAVMKAIA QLKPNKNVSA IMCITDNRIN GDASLPDSVY
     TSMSGKTVEV NNTDAEGRLV LADRLYYGAT KLNATRLIDT ATLTGTMLTA LGQTYSGIYA
     TSCKIWHQFE DAAKIAHEKV WRMPLHEDFN KTNKESLVAD LNNYSNNEKS DCNTAAMFLK
     EFTNNVPYIH CDVAGTADKK GMGLGILVST FVEFGKSQQR NCESCECDEQ KCETKNCNIE
     ESTTKIVKAK KSTAKKATTK KTTTRKTASK TKSTKSKARK