ID   AMPP1_STRLI             Reviewed;         491 AA.
AC   P0A3Z2; Q05813;
DT   15-MAR-2005, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 2.
DT   03-AUG-2022, entry version 61.
DE   RecName: Full=Xaa-Pro aminopeptidase 1;
DE            EC=3.4.11.9;
DE   AltName: Full=Aminoacylproline aminopeptidase I;
DE   AltName: Full=Aminopeptidase P I;
DE            Short=APP;
DE            Short=PEPP I;
DE   AltName: Full=X-Pro aminopeptidase I;
DE   AltName: Full=Xaa-Pro aminopeptidase I;
GN   Name=pepPI; Synonyms=pepP;
OS   Streptomyces lividans.
OC   Bacteria; Actinobacteria; Streptomycetales; Streptomycetaceae;
OC   Streptomyces.
OX   NCBI_TaxID=1916;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND PROTEIN SEQUENCE OF 2-16.
RC   STRAIN=66 / 1326;
RX   PubMed=8422994; DOI=10.1016/0378-1119(93)90549-i;
RA   Butler M.J., Bergeron A., Soostmeyer G., Zimny T., Malek L.T.;
RT   "Cloning and characterisation of an aminopeptidase P-encoding gene from
RT   Streptomyces lividans.";
RL   Gene 123:115-119(1993).
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=Release of any N-terminal amino acid, including proline, that
CC         is linked to proline, even from a dipeptide or tripeptide.;
CC         EC=3.4.11.9;
CC   -!- COFACTOR:
CC       Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000250};
CC       Note=Binds 2 manganese ions per subunit. {ECO:0000250};
CC   -!- SUBUNIT: Homodimer.
CC   -!- MISCELLANEOUS: S.lividans has two genes (pepP1 and pepP2) which encode
CC       aminopeptidase P.
CC   -!- SIMILARITY: Belongs to the peptidase M24B family. {ECO:0000305}.
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DR   EMBL; M91546; AAA26703.1; -; Genomic_DNA.
DR   PIR; JN0491; JN0491.
DR   AlphaFoldDB; P0A3Z2; -.
DR   SMR; P0A3Z2; -.
DR   MEROPS; M24.033; -.
DR   GO; GO:0030145; F:manganese ion binding; IEA:InterPro.
DR   GO; GO:0070006; F:metalloaminopeptidase activity; IEA:InterPro.
DR   GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR   Gene3D; 3.40.350.10; -; 1.
DR   Gene3D; 3.90.230.10; -; 1.
DR   InterPro; IPR007865; Aminopep_P_N.
DR   InterPro; IPR029149; Creatin/AminoP/Spt16_NTD.
DR   InterPro; IPR036005; Creatinase/aminopeptidase-like.
DR   InterPro; IPR000994; Pept_M24.
DR   InterPro; IPR001131; Peptidase_M24B_aminopep-P_CS.
DR   Pfam; PF05195; AMP_N; 1.
DR   Pfam; PF00557; Peptidase_M24; 1.
DR   SMART; SM01011; AMP_N; 1.
DR   SUPFAM; SSF53092; SSF53092; 1.
DR   SUPFAM; SSF55920; SSF55920; 1.
DR   PROSITE; PS00491; PROLINE_PEPTIDASE; 1.
PE   1: Evidence at protein level;
KW   Aminopeptidase; Direct protein sequencing; Hydrolase; Manganese;
KW   Metal-binding; Metalloprotease; Protease.
FT   INIT_MET        1
FT                   /note="Removed"
FT                   /evidence="ECO:0000269|PubMed:8422994"
FT   CHAIN           2..491
FT                   /note="Xaa-Pro aminopeptidase 1"
FT                   /id="PRO_0000185081"
FT   REGION          1..32
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         308
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250"
FT   BINDING         320
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250"
FT   BINDING         320
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250"
FT   BINDING         403
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250"
FT   BINDING         434
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250"
FT   BINDING         458
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250"
FT   BINDING         458
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   491 AA;  54048 MW;  1FE2C5E8C26C70DF CRC64;
     MAEELTPENP AIPETPEETE EPIKQRKNGL YPGVSDELAE NMQSGWADTE LHDLEPIAQA
     AETAARRAAL SARFPGERLV IPAGNLKTRS NDTEYSFRAS VEYAYLTGNQ TEDGVLVMEP
     EGDGHAATIY LLPRSDRENG EFWLDGQGEL WVGRRHSLAE AGELYGIPAS DVRELAGSLR
     EATGPVRVVR GFDAGIEAAL TDKVTAERDE ELRVFLSEAR LVKDEFEIGE LQKAVDSTVR
     GFEDVVKVLD RAEATSERYI EGTFFLRARV EGNDVGYGSI CAAGPHACTL HWVRNDGPVR
     SGDLLLLDAG VETHTYYTAD VTRTLPISGT YSELQKKIYD AVYDAQEAGI AAVRPGAKYR
     DFHDASQRVL AERLVEWGLV EGPVERVLEL GLQRRWTLHG TGHMLGMDVH DCAAARVESY
     VDGTLEPGMV LTVEPGLYFQ ADDLTVPEEY RGIGVRIEDD ILVTADGNRN LSAGLPRRSD
     EVEEWMAALK G