AMPP_ECOLI
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 03-AUG-2022, entry version 195.
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; Proteobacteria; 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; P15034; -.
DR PRIDE; P15034; -.
DR EnsemblBacteria; AAC75946; AAC75946; b2908.
DR EnsemblBacteria; BAE76973; BAE76973; BAE76973.
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; GWADTEL; -.
DR PhylomeDB; P15034; -.
DR BioCyc; EcoCyc:EG10697-MON; -.
DR BioCyc; MetaCyc:EG10697-MON; -.
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: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:0008233; F:peptidase activity; IBA:GO_Central.
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; IPR001714; Pept_M24_MAP.
DR InterPro; IPR001131; Peptidase_M24B_aminopep-P_CS.
DR Pfam; PF05195; AMP_N; 1.
DR Pfam; PF00557; Peptidase_M24; 1.
DR PRINTS; PR00599; MAPEPTIDASE.
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 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
