ID   AMPP2_BOTFB             Reviewed;         555 AA.
AC   A6SL16; A0A384JUX0;
DT   27-JUL-2011, integrated into UniProtKB/Swiss-Prot.
DT   29-MAY-2024, sequence version 2.
DT   02-SEP-2026, entry version 93.
DE   RecName: Full=Probable Xaa-Pro aminopeptidase BC1G_13431;
DE            EC=3.4.11.9;
DE   AltName: Full=Aminoacylproline aminopeptidase;
DE   AltName: Full=Prolidase;
GN   ORFNames=BC1G_13431, BCIN_10g03210;
OS   Botrytis cinerea (strain B05.10) (Noble rot fungus) (Botryotinia
OS   fuckeliana).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Leotiomycetes;
OC   Helotiales; Sclerotiniaceae; Botrytis.
OX   NCBI_TaxID=332648;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=B05.10;
RX   PubMed=21876677; DOI=10.1371/journal.pgen.1002230;
RA   Amselem J., Cuomo C.A., van Kan J.A.L., Viaud M., Benito E.P., Couloux A.,
RA   Coutinho P.M., de Vries R.P., Dyer P.S., Fillinger S., Fournier E.,
RA   Gout L., Hahn M., Kohn L., Lapalu N., Plummer K.M., Pradier J.-M.,
RA   Quevillon E., Sharon A., Simon A., ten Have A., Tudzynski B., Tudzynski P.,
RA   Wincker P., Andrew M., Anthouard V., Beever R.E., Beffa R., Benoit I.,
RA   Bouzid O., Brault B., Chen Z., Choquer M., Collemare J., Cotton P.,
RA   Danchin E.G., Da Silva C., Gautier A., Giraud C., Giraud T., Gonzalez C.,
RA   Grossetete S., Gueldener U., Henrissat B., Howlett B.J., Kodira C.,
RA   Kretschmer M., Lappartient A., Leroch M., Levis C., Mauceli E.,
RA   Neuveglise C., Oeser B., Pearson M., Poulain J., Poussereau N.,
RA   Quesneville H., Rascle C., Schumacher J., Segurens B., Sexton A., Silva E.,
RA   Sirven C., Soanes D.M., Talbot N.J., Templeton M., Yandava C., Yarden O.,
RA   Zeng Q., Rollins J.A., Lebrun M.-H., Dickman M.;
RT   "Genomic analysis of the necrotrophic fungal pathogens Sclerotinia
RT   sclerotiorum and Botrytis cinerea.";
RL   PLoS Genet. 7:E1002230-E1002230(2011).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND GENOME REANNOTATION.
RC   STRAIN=B05.10;
RX   PubMed=23104368; DOI=10.1128/ec.00164-12;
RA   Staats M., van Kan J.A.L.;
RT   "Genome update of Botrytis cinerea strains B05.10 and T4.";
RL   Eukaryot. Cell 11:1413-1414(2012).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND GENOME REANNOTATION.
RC   STRAIN=B05.10;
RX   PubMed=26913498; DOI=10.1111/mpp.12384;
RA   van Kan J.A.L., Stassen J.H.M., Mosbach A., van der Lee T.A.J., Faino L.,
RA   Farmer A.D., Papasotiriou D.G., Zhou S., Seidl M.F., Cottam E., Edel D.,
RA   Hahn M., Schwartz D.C., Dietrich R.A., Widdison S., Scalliet G.;
RT   "A gapless genome sequence of the fungus Botrytis cinerea.";
RL   Mol. Plant Pathol. 18:75-89(2017).
CC   -!- FUNCTION: Catalyzes the removal of a penultimate prolyl residue from
CC       the N-termini of peptides. {ECO:0000250}.
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   -!- 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; CP009814; ATZ54311.1; -; Genomic_DNA.
DR   RefSeq; XP_001548054.2; XM_001548004.2.
DR   AlphaFoldDB; A6SL16; -.
DR   SMR; A6SL16; -.
DR   EnsemblFungi; Bcin10g03210.1; Bcin10p03210.1; Bcin10g03210.
DR   GeneID; 5428547; -.
DR   KEGG; bfu:BCIN_10g03210; -.
DR   VEuPathDB; FungiDB:Bcin10g03210; -.
DR   OrthoDB; 10261878at2759; -.
DR   Proteomes; UP000001798; Chromosome 10.
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:TreeGrafter.
DR   CDD; cd01087; Prolidase; 1.
DR   Gene3D; 3.90.230.10; Creatinase/methionine aminopeptidase superfamily; 1.
DR   Gene3D; 3.40.350.10; Creatinase/prolidase N-terminal domain; 1.
DR   InterPro; IPR007865; Aminopep_P_N.
DR   InterPro; IPR029149; Creatin/AminoP/Spt16_N.
DR   InterPro; IPR036005; Creatinase/aminopeptidase-like.
DR   InterPro; IPR000994; Pept_M24.
DR   InterPro; IPR001131; Peptidase_M24B_aminopep-P_CS.
DR   InterPro; IPR052433; X-Pro_dipept-like.
DR   PANTHER; PTHR43226; XAA-PRO AMINOPEPTIDASE 3; 1.
DR   PANTHER; PTHR43226:SF3; XAA-PRO AMINOPEPTIDASE AN0832-RELATED; 1.
DR   Pfam; PF05195; AMP_N; 1.
DR   Pfam; PF00557; Peptidase_M24; 1.
DR   SMART; SM01011; AMP_N; 1.
DR   SUPFAM; SSF55920; Creatinase/aminopeptidase; 1.
DR   SUPFAM; SSF53092; Creatinase/prolidase N-terminal domain; 1.
DR   PROSITE; PS00491; PROLINE_PEPTIDASE; 1.
PE   3: Inferred from homology;
KW   Aminopeptidase; Hydrolase; Manganese; Metal-binding; Metalloprotease;
KW   Protease; Reference proteome.
FT   CHAIN           1..555
FT                   /note="Probable Xaa-Pro aminopeptidase BC1G_13431"
FT                   /id="PRO_0000411830"
FT   REGION          527..555
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        538..547
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         303
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         314
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /ligand_label="2"
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         499
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250"
FT   BINDING         499
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   555 AA;  62799 MW;  068B1C5FC41EEA83 CRC64;
     MNIQTIMSSF TAQDKDQEVR PSSSGSWACK EVDEFDALSI EYKPKPTEKY PAKLHARNVR
     KYLDVGEGLI YLPGLPSFNY EDSDMPPAFR QRRYFYYITG VNLSDCIVTY NIHRDQLWLW
     IPPPNSGRSV IYNGARPTIK EIMSKYDFDH VETLTHLDSY LTWYAHTEPG KIHVLHDYQA
     PKNIELQITR KNGCHSIISE SPFDSSKLEE AMNTARAIKS PYELRMIRKA SAITAQGHLN
     VLRGLRHLSN EAEIEAIFTA TCIAKQAKTQ AYGVIAGSGE NASTLHYMAN NEPLKGRQLL
     CLDAGCEWDC YASDVTRTVP ISGEYTEEAE AIYDIVAKMQ DECIELLKPG ANYRDIHIHA
     HKVALKGLMD LGLVEGGTFD ELFMAGVSVA FFPHGLGHYV GLEVHDVGPG GSRITNRLYG
     FDKKPADWTD AYFQILSNTG VTSDGGSILE KDMVVTVEPG IYFSRYALEE VYLKSPNYAK
     YINKDLLQKY YPVGGVRIED DLLITEDGYE NLTTVLKGKE ALKIINEGKE QEEEEEREAN
     RKATESRKQK KTWFW
//