AMPP_MYCPN
ID AMPP_MYCPN Reviewed; 354 AA.
AC P75313;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1997, sequence version 1.
DT 03-AUG-2022, entry version 116.
DE RecName: Full=Putative Xaa-Pro aminopeptidase;
DE Short=X-Pro aminopeptidase;
DE EC=3.4.11.9;
DE AltName: Full=Aminoacylproline aminopeptidase;
DE AltName: Full=Aminopeptidase P;
DE Short=APP;
GN Name=pepP; OrderedLocusNames=MPN_470; ORFNames=MP371;
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 -!- 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}.
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DR EMBL; U00089; AAB96019.1; -; Genomic_DNA.
DR PIR; S73697; S73697.
DR RefSeq; NP_110158.1; NC_000912.1.
DR RefSeq; WP_010874826.1; NC_000912.1.
DR AlphaFoldDB; P75313; -.
DR SMR; P75313; -.
DR STRING; 272634.MPN_470; -.
DR EnsemblBacteria; AAB96019; AAB96019; MPN_470.
DR KEGG; mpn:MPN_470; -.
DR PATRIC; fig|272634.6.peg.508; -.
DR HOGENOM; CLU_017266_4_0_14; -.
DR OMA; YCSDRTR; -.
DR BioCyc; MPNE272634:G1GJ3-773-MON; -.
DR Proteomes; UP000000808; Chromosome.
DR GO; GO:0004177; F:aminopeptidase activity; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0008237; F:metallopeptidase activity; IEA:UniProtKB-KW.
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; IPR029149; Creatin/AminoP/Spt16_NTD.
DR InterPro; IPR036005; Creatinase/aminopeptidase-like.
DR InterPro; IPR000587; Creatinase_N.
DR InterPro; IPR000994; Pept_M24.
DR InterPro; IPR001131; Peptidase_M24B_aminopep-P_CS.
DR Pfam; PF01321; Creatinase_N; 1.
DR Pfam; PF00557; Peptidase_M24; 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; Reference proteome.
FT CHAIN 1..354
FT /note="Putative Xaa-Pro aminopeptidase"
FT /id="PRO_0000185078"
FT BINDING 213
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 224
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 224
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 290
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 319
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 333
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 333
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
SQ SEQUENCE 354 AA; 39624 MW; A5286BD9F414A132 CRC64;
MHNELQQKLA VLHKLLQDNK ADAILIGSDQ NRFWLTGFPS SAGWLVVHKQ RVNLFIDGRY
FEAAKTAIDP LVKVELFTTY KQVKALCEQV GVKHLLIEGD YLTFNYQNFI KELCAQYTVI
NAQEIRRQKL PSEILAIEKV VEITRKVAVK LKRFIQPGMT ELFIAQWITD QLVKAGGAKN
SFDPIVATGK NGANPHHKPS KLKVKSGDFV TCDFGTIYNG YCSDITRTFL VGKKPNNEVL
LKAYKKVDEA NMAGINAANT QLTGAEVDKV CRDIIEASEF KDYFVHSTGH GVGLDIHEMP
NVSTSYNKLL CENAVITIEP GIYIPSVGGI RIEDMVLVKD HKSVWLSAKI PRAF
