ID   AMPP2_STRLI             Reviewed;         470 AA.
AC   P0A3Z4; Q60394;
DT   15-MAR-2005, integrated into UniProtKB/Swiss-Prot.
DT   15-MAR-2005, sequence version 1.
DT   03-AUG-2022, entry version 58.
DE   RecName: Full=Xaa-Pro aminopeptidase 2;
DE            EC=3.4.11.9;
DE   AltName: Full=Aminoacylproline aminopeptidase II;
DE   AltName: Full=Aminopeptidase P II;
DE            Short=APP;
DE            Short=PEPP II;
DE   AltName: Full=X-Pro aminopeptidase II;
DE   AltName: Full=Xaa-Pro aminopeptidase II;
GN   Name=pepP2;
OS   Streptomyces lividans.
OC   Bacteria; Actinobacteria; Streptomycetales; Streptomycetaceae;
OC   Streptomyces.
OX   NCBI_TaxID=1916;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=66 / 1326;
RX   PubMed=7765336; DOI=10.1007/bf01569658;
RA   Butler M.J., Aphale J.S., Dizonno M.A., Krygsman P., Walczyk E.,
RA   Malek L.T.;
RT   "Intracellular aminopeptidases in Streptomyces lividans 66.";
RL   J. Ind. Microbiol. 13:24-29(1994).
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. {ECO:0000250}.
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}.
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; L23174; AAB00325.1; -; Genomic_DNA.
DR   AlphaFoldDB; P0A3Z4; -.
DR   SMR; P0A3Z4; -.
DR   MEROPS; M24.033; -.
DR   PRIDE; P0A3Z4; -.
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   3: Inferred from homology;
KW   Aminopeptidase; Hydrolase; Manganese; Metal-binding; Metalloprotease;
KW   Protease.
FT   CHAIN           1..470
FT                   /note="Xaa-Pro aminopeptidase 2"
FT                   /id="PRO_0000185082"
FT   BINDING         287
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         299
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250"
FT   BINDING         382
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250"
FT   BINDING         413
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250"
FT   BINDING         437
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250"
FT   BINDING         437
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   470 AA;  51925 MW;  0D3D33CE256523C2 CRC64;
     MSNRRKNSLY PTLSAELSAL MRTGWADTER HDLAPAEQAP YAALRRAALS ARFPGERLVV
     PSGNLKVRSN DDTYPFRSYS GYVHMTGDQA RDGALVLEPR PDGGHDAYCY QLPRDSRDDD
     EFWTGAHAEL WTGRRRSLAE SERVLGLPCR DVRTAAADLA AVSEVRTRIV RGIDPALEAA
     VTTDEERDAE LEDALSDLRL VKDAWELGEL RKAVDSTVRG FTDVVGELSR AVASSERWLE
     GTFFRRARLE GNAVGYGTIC AAGEHATIMH WTDNDGPVRP GDLLLLDAGV ETRSLYTADV
     TRTLPISGTF TPLQREVYDA VYEAQEAGIA TVKPGAAYRD FHEAAQRHLA ARLVEWGFIE
     GPAERAYELG LQRRFTMAGT GHMLGLDVHD CARARTEEYV EGVLEPGMCL TVEPGLYFQA
     DDLTVPEEWR GIGVRIEDDL VVTEDGHENL SAGLPRSADE VEAWMARFAG