ID   AMPP_ECOLI              Reviewed;         441 AA.
AC   P15034; Q2M9T3;
DT   01-APR-1990, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 2.
DT   27-MAR-2024, entry version 203.
DE   RecName: Full=Xaa-Pro aminopeptidase;
DE            EC=3.4.11.9;
DE   AltName: Full=Aminoacylproline aminopeptidase;
DE   AltName: Full=Aminopeptidase P II;
DE            Short=APP-II;
DE   AltName: Full=X-Pro aminopeptidase;
GN   Name=pepP; OrderedLocusNames=b2908, JW2876;
OS   Escherichia coli (strain K12).
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=83333;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 2-21, AND
RP   CHARACTERIZATION.
RC   STRAIN=ATCC 33694 / HB101;
RX   PubMed=2659585; DOI=10.1093/oxfordjournals.jbchem.a122678;
RA   Yoshimoto T., Tone H., Honda T., Osatomi K., Kobayashi R., Tsuru D.;
RT   "Sequencing and high expression of aminopeptidase P gene from Escherichia
RT   coli HB101.";
RL   J. Biochem. 105:412-416(1989).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=ATCC 33694 / HB101;
RX   PubMed=1339425; DOI=10.1128/jb.174.22.7352-7359.1992;
RA   Nakahigashi K., Miyamoto K., Nishimura K., Inokuchi H.;
RT   "Isolation and characterization of a light-sensitive mutant of Escherichia
RT   coli K-12 with a mutation in a gene that is required for the biosynthesis
RT   of ubiquinone.";
RL   J. Bacteriol. 174:7352-7359(1992).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=K12 / MG1655 / ATCC 47076;
RX   PubMed=9278503; DOI=10.1126/science.277.5331.1453;
RA   Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V.,
RA   Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F.,
RA   Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B.,
RA   Shao Y.;
RT   "The complete genome sequence of Escherichia coli K-12.";
RL   Science 277:1453-1462(1997).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX   PubMed=16738553; DOI=10.1038/msb4100049;
RA   Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S.,
RA   Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.;
RT   "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655
RT   and W3110.";
RL   Mol. Syst. Biol. 2:E1-E5(2006).
RN   [5]
RP   X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS).
RX   PubMed=9520390; DOI=10.1073/pnas.95.7.3472;
RA   Wilce M.C.J., Bond C.S., Dixon N.E., Freeman H.C., Guss J.M., Lilley P.E.,
RA   Wilce J.A.;
RT   "Structure and mechanism of a proline-specific aminopeptidase from
RT   Escherichia coli.";
RL   Proc. Natl. Acad. Sci. U.S.A. 95:3472-3477(1998).
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;
CC       Note=Binds 2 manganese ions per subunit.;
CC   -!- SUBUNIT: Homotetramer.
CC   -!- INTERACTION:
CC       P15034; P60560: guaC; NbExp=3; IntAct=EBI-554801, EBI-544491;
CC       P15034; P15288: pepD; NbExp=4; IntAct=EBI-554801, EBI-542419;
CC   -!- SUBCELLULAR LOCATION: Cytoplasm.
CC   -!- SIMILARITY: Belongs to the peptidase M24B family. {ECO:0000305}.
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DR   EMBL; D00398; BAA00299.1; -; Genomic_DNA.
DR   EMBL; D90281; BAA14325.1; -; Genomic_DNA.
DR   EMBL; U28377; AAA69076.1; -; Genomic_DNA.
DR   EMBL; U00096; AAC75946.1; -; Genomic_DNA.
DR   EMBL; AP009048; BAE76973.1; -; Genomic_DNA.
DR   PIR; JX0067; DPECP.
DR   RefSeq; NP_417384.1; NC_000913.3.
DR   RefSeq; WP_001290136.1; NZ_LN832404.1.
DR   PDB; 1A16; X-ray; 2.30 A; A=2-441.
DR   PDB; 1JAW; X-ray; 2.70 A; A=2-441.
DR   PDB; 1M35; X-ray; 2.40 A; A/B/C/D/E/F=2-441.
DR   PDB; 1N51; X-ray; 2.30 A; A=2-441.
DR   PDB; 1W2M; X-ray; 2.40 A; A/B/C/D/E/F=2-441.
DR   PDB; 1W7V; X-ray; 2.00 A; A/B/C/D=2-441.
DR   PDB; 1WBQ; X-ray; 2.30 A; A/B/C/D=2-441.
DR   PDB; 1WL6; X-ray; 2.00 A; A=2-441.
DR   PDB; 1WL9; X-ray; 1.90 A; A=2-441.
DR   PDB; 1WLR; X-ray; 2.10 A; A=2-441.
DR   PDB; 2BH3; X-ray; 2.40 A; A=2-441.
DR   PDB; 2BHA; X-ray; 2.40 A; A=2-441.
DR   PDB; 2BHB; X-ray; 2.41 A; A=2-441.
DR   PDB; 2BHC; X-ray; 2.40 A; A=2-441.
DR   PDB; 2BHD; X-ray; 2.50 A; A=2-441.
DR   PDB; 2BN7; X-ray; 2.40 A; A=2-441.
DR   PDB; 2BWS; X-ray; 1.75 A; A=2-441.
DR   PDB; 2BWT; X-ray; 2.90 A; A=2-441.
DR   PDB; 2BWU; X-ray; 2.20 A; A=2-441.
DR   PDB; 2BWV; X-ray; 1.70 A; A=2-441.
DR   PDB; 2BWW; X-ray; 2.61 A; A=2-441.
DR   PDB; 2BWX; X-ray; 1.70 A; A=2-441.
DR   PDB; 2BWY; X-ray; 2.40 A; A=2-441.
DR   PDB; 2V3X; X-ray; 1.70 A; A=2-441.
DR   PDB; 2V3Y; X-ray; 1.60 A; A=2-441.
DR   PDB; 2V3Z; X-ray; 1.56 A; A=2-441.
DR   PDBsum; 1A16; -.
DR   PDBsum; 1JAW; -.
DR   PDBsum; 1M35; -.
DR   PDBsum; 1N51; -.
DR   PDBsum; 1W2M; -.
DR   PDBsum; 1W7V; -.
DR   PDBsum; 1WBQ; -.
DR   PDBsum; 1WL6; -.
DR   PDBsum; 1WL9; -.
DR   PDBsum; 1WLR; -.
DR   PDBsum; 2BH3; -.
DR   PDBsum; 2BHA; -.
DR   PDBsum; 2BHB; -.
DR   PDBsum; 2BHC; -.
DR   PDBsum; 2BHD; -.
DR   PDBsum; 2BN7; -.
DR   PDBsum; 2BWS; -.
DR   PDBsum; 2BWT; -.
DR   PDBsum; 2BWU; -.
DR   PDBsum; 2BWV; -.
DR   PDBsum; 2BWW; -.
DR   PDBsum; 2BWX; -.
DR   PDBsum; 2BWY; -.
DR   PDBsum; 2V3X; -.
DR   PDBsum; 2V3Y; -.
DR   PDBsum; 2V3Z; -.
DR   AlphaFoldDB; P15034; -.
DR   SMR; P15034; -.
DR   BioGRID; 4259236; 50.
DR   DIP; DIP-10459N; -.
DR   IntAct; P15034; 10.
DR   STRING; 511145.b2908; -.
DR   DrugBank; DB04092; Apstatin.
DR   MEROPS; M24.004; -.
DR   jPOST; P15034; -.
DR   PaxDb; 511145-b2908; -.
DR   EnsemblBacteria; AAC75946; AAC75946; b2908.
DR   GeneID; 947385; -.
DR   KEGG; ecj:JW2876; -.
DR   KEGG; eco:b2908; -.
DR   PATRIC; fig|1411691.4.peg.3824; -.
DR   EchoBASE; EB0691; -.
DR   eggNOG; COG0006; Bacteria.
DR   HOGENOM; CLU_017266_1_0_6; -.
DR   InParanoid; P15034; -.
DR   OMA; DSYFWYL; -.
DR   OrthoDB; 9806388at2; -.
DR   PhylomeDB; P15034; -.
DR   BioCyc; EcoCyc:EG10697-MONOMER; -.
DR   BioCyc; MetaCyc:EG10697-MONOMER; -.
DR   BRENDA; 3.1.8.1; 2026.
DR   BRENDA; 3.4.11.9; 2026.
DR   EvolutionaryTrace; P15034; -.
DR   PRO; PR:P15034; -.
DR   Proteomes; UP000000318; Chromosome.
DR   Proteomes; UP000000625; Chromosome.
DR   GO; GO:0005829; C:cytosol; IDA:EcoCyc.
DR   GO; GO:0032991; C:protein-containing complex; IDA:EcoCyc.
DR   GO; GO:0004177; F:aminopeptidase activity; IDA:EcoCyc.
DR   GO; GO:0042802; F:identical protein binding; IPI:EcoCyc.
DR   GO; GO:0030145; F:manganese ion binding; IDA:EcoCyc.
DR   GO; GO:0070006; F:metalloaminopeptidase activity; IEA:InterPro.
DR   GO; GO:0008235; F:metalloexopeptidase activity; IDA:EcoCyc.
DR   GO; GO:0051289; P:protein homotetramerization; IDA:EcoCyc.
DR   GO; GO:0006508; P:proteolysis; IBA:GO_Central.
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_NTD.
DR   InterPro; IPR036005; Creatinase/aminopeptidase-like.
DR   InterPro; IPR000994; Pept_M24.
DR   InterPro; IPR001714; Pept_M24_MAP.
DR   InterPro; IPR001131; Peptidase_M24B_aminopep-P_CS.
DR   PANTHER; PTHR43226:SF9; XAA-PRO AMINOPEPTIDASE; 1.
DR   PANTHER; PTHR43226; XAA-PRO AMINOPEPTIDASE 3; 1.
DR   Pfam; PF05195; AMP_N; 1.
DR   Pfam; PF00557; Peptidase_M24; 1.
DR   PRINTS; PR00599; MAPEPTIDASE.
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   1: Evidence at protein level;
KW   3D-structure; Aminopeptidase; Cytoplasm; Direct protein sequencing;
KW   Hydrolase; Manganese; Metal-binding; Metalloprotease; Protease;
KW   Reference proteome.
FT   INIT_MET        1
FT                   /note="Removed"
FT                   /evidence="ECO:0000269|PubMed:2659585"
FT   CHAIN           2..441
FT                   /note="Xaa-Pro aminopeptidase"
FT                   /id="PRO_0000185075"
FT   BINDING         261
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /ligand_label="2"
FT   BINDING         272
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /ligand_label="1"
FT   BINDING         272
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /ligand_label="2"
FT   BINDING         355
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /ligand_label="1"
FT   BINDING         384
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /ligand_label="1"
FT   BINDING         407
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /ligand_label="1"
FT   BINDING         407
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /ligand_label="2"
FT   HELIX           6..19
FT                   /evidence="ECO:0007829|PDB:2V3Z"
FT   STRAND          22..29
FT                   /evidence="ECO:0007829|PDB:2V3Z"
FT   STRAND          35..37
FT                   /evidence="ECO:0007829|PDB:2V3Z"
FT   HELIX           48..54
FT                   /evidence="ECO:0007829|PDB:2V3Z"
FT   STRAND          62..67
FT                   /evidence="ECO:0007829|PDB:2V3Z"
FT   STRAND          69..71
FT                   /evidence="ECO:0007829|PDB:2V3Z"
FT   STRAND          73..79
FT                   /evidence="ECO:0007829|PDB:2V3Z"
FT   HELIX           84..90
FT                   /evidence="ECO:0007829|PDB:2V3Z"
FT   HELIX           95..103
FT                   /evidence="ECO:0007829|PDB:2V3Z"
FT   STRAND          106..110
FT                   /evidence="ECO:0007829|PDB:2V3Z"
FT   HELIX           111..113
FT                   /evidence="ECO:0007829|PDB:2V3Z"
FT   HELIX           114..122
FT                   /evidence="ECO:0007829|PDB:2V3Z"
FT   STRAND          126..129
FT                   /evidence="ECO:0007829|PDB:2V3Z"
FT   HELIX           136..150
FT                   /evidence="ECO:0007829|PDB:2V3Z"
FT   HELIX           153..155
FT                   /evidence="ECO:0007829|PDB:2V3Z"
FT   STRAND          161..164
FT                   /evidence="ECO:0007829|PDB:2V3Z"
FT   HELIX           167..175
FT                   /evidence="ECO:0007829|PDB:2V3Z"
FT   HELIX           179..202
FT                   /evidence="ECO:0007829|PDB:2V3Z"
FT   HELIX           209..222
FT                   /evidence="ECO:0007829|PDB:2V3Z"
FT   STRAND          227..230
FT                   /evidence="ECO:0007829|PDB:2V3Z"
FT   STRAND          233..236
FT                   /evidence="ECO:0007829|PDB:2V3Z"
FT   HELIX           237..241
FT                   /evidence="ECO:0007829|PDB:2V3Z"
FT   STRAND          257..262
FT                   /evidence="ECO:0007829|PDB:2V3Z"
FT   STRAND          264..266
FT                   /evidence="ECO:0007829|PDB:2V3Z"
FT   STRAND          273..278
FT                   /evidence="ECO:0007829|PDB:2V3Z"
FT   HELIX           285..304
FT                   /evidence="ECO:0007829|PDB:2V3Z"
FT   HELIX           311..328
FT                   /evidence="ECO:0007829|PDB:2V3Z"
FT   HELIX           336..341
FT                   /evidence="ECO:0007829|PDB:2V3Z"
FT   TURN            342..348
FT                   /evidence="ECO:0007829|PDB:2V3Z"
FT   STRAND          358..362
FT                   /evidence="ECO:0007829|PDB:2V3Z"
FT   HELIX           369..371
FT                   /evidence="ECO:0007829|PDB:2V3Z"
FT   STRAND          380..383
FT                   /evidence="ECO:0007829|PDB:2V3Z"
FT   STRAND          386..389
FT                   /evidence="ECO:0007829|PDB:2V3Z"
FT   HELIX           397..399
FT                   /evidence="ECO:0007829|PDB:2V3Z"
FT   STRAND          402..405
FT                   /evidence="ECO:0007829|PDB:2V3Z"
FT   STRAND          407..413
FT                   /evidence="ECO:0007829|PDB:2V3Z"
FT   STRAND          416..421
FT                   /evidence="ECO:0007829|PDB:2V3Z"
FT   HELIX           428..439
FT                   /evidence="ECO:0007829|PDB:2V3Z"
SQ   SEQUENCE   441 AA;  49815 MW;  80A6A5BDD86D84B1 CRC64;
     MSEISRQEFQ RRRQALVEQM QPGSAALIFA APEVTRSADS EYPYRQNSDF WYFTGFNEPE
     AVLVLIKSDD THNHSVLFNR VRDLTAEIWF GRRLGQDAAP EKLGVDRALA FSEINQQLYQ
     LLNGLDVVYH AQGEYAYADV IVNSALEKLR KGSRQNLTAP ATMIDWRPVV HEMRLFKSPE
     EIAVLRRAGE ITAMAHTRAM EKCRPGMFEY HLEGEIHHEF NRHGARYPSY NTIVGSGENG
     CILHYTENEC EMRDGDLVLI DAGCEYKGYA GDITRTFPVN GKFTQAQREI YDIVLESLET
     SLRLYRPGTS ILEVTGEVVR IMVSGLVKLG ILKGDVDELI AQNAHRPFFM HGLSHWLGLD
     VHDVGVYGQD RSRILEPGMV LTVEPGLYIA PDAEVPEQYR GIGIRIEDDI VITETGNENL
     TASVVKKPEE IEALMVAARK Q
//