YPDF_ECOLI
ID YPDF_ECOLI Reviewed; 361 AA.
AC P76524; P76951;
DT 27-MAR-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1997, sequence version 1.
DT 03-AUG-2022, entry version 141.
DE RecName: Full=Aminopeptidase YpdF;
DE EC=3.4.11.-;
GN Name=ypdF; OrderedLocusNames=b2385, JW2382;
OS Escherichia coli (strain K12).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=83333;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=9205837; DOI=10.1093/dnares/4.2.91;
RA Yamamoto Y., Aiba H., Baba T., Hayashi K., Inada T., Isono K., Itoh T.,
RA Kimura S., Kitagawa M., Makino K., Miki T., Mitsuhashi N., Mizobuchi K.,
RA Mori H., Nakade S., Nakamura Y., Nashimoto H., Oshima T., Oyama S.,
RA Saito N., Sampei G., Satoh Y., Sivasundaram S., Tagami H., Takahashi H.,
RA Takeda J., Takemoto K., Uehara K., Wada C., Yamagata S., Horiuchi T.;
RT "Construction of a contiguous 874-kb sequence of the Escherichia coli-K12
RT genome corresponding to 50.0-68.8 min on the linkage map and analysis of
RT its sequence features.";
RL DNA Res. 4:91-113(1997).
RN [2]
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 [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND SEQUENCE REVISION.
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 [4]
RP FUNCTION.
RX PubMed=15901689; DOI=10.1128/jb.187.11.3671-3677.2005;
RA Zheng Y., Roberts R.J., Kasif S., Guan C.;
RT "Characterization of two new aminopeptidases in Escherichia coli.";
RL J. Bacteriol. 187:3671-3677(2005).
CC -!- FUNCTION: Hydrolyzes the N-terminal methionine when the next amino acid
CC is alanine, proline or serine. The substrate preference for methionyl
CC aminopeptidase activity is Pro > Ala > Ser. Also able to hydrolyze the
CC Xaa-Pro peptide bond when the first amino acid is alanine, asparagine
CC or methionine. {ECO:0000269|PubMed:15901689}.
CC -!- COFACTOR:
CC Name=Co(2+); Xref=ChEBI:CHEBI:48828;
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC Name=Ni(2+); Xref=ChEBI:CHEBI:49786;
CC Note=Co(2+), Mn(2+) or Ni(2+).;
CC -!- INTERACTION:
CC P76524; P0A6F5: groEL; NbExp=2; IntAct=EBI-1128711, EBI-543750;
CC -!- SIMILARITY: Belongs to the peptidase M24 family. {ECO:0000305}.
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DR EMBL; U00096; AAC75444.1; -; Genomic_DNA.
DR EMBL; AP009048; BAA16255.2; -; Genomic_DNA.
DR PIR; F65012; F65012.
DR RefSeq; NP_416886.1; NC_000913.3.
DR RefSeq; WP_000173288.1; NZ_LN832404.1.
DR PDB; 5CNX; X-ray; 2.60 A; A/B/C=1-361.
DR PDBsum; 5CNX; -.
DR AlphaFoldDB; P76524; -.
DR SMR; P76524; -.
DR BioGRID; 4259189; 26.
DR BioGRID; 851194; 1.
DR DIP; DIP-48229N; -.
DR IntAct; P76524; 2.
DR STRING; 511145.b2385; -.
DR MEROPS; M24.039; -.
DR MEROPS; M42.008; -.
DR PaxDb; P76524; -.
DR PRIDE; P76524; -.
DR EnsemblBacteria; AAC75444; AAC75444; b2385.
DR EnsemblBacteria; BAA16255; BAA16255; BAA16255.
DR GeneID; 946853; -.
DR KEGG; ecj:JW2382; -.
DR KEGG; eco:b2385; -.
DR PATRIC; fig|1411691.4.peg.4343; -.
DR EchoBASE; EB3905; -.
DR eggNOG; COG0006; Bacteria.
DR HOGENOM; CLU_017266_4_0_6; -.
DR InParanoid; P76524; -.
DR OMA; YCSDRTR; -.
DR PhylomeDB; P76524; -.
DR BioCyc; EcoCyc:G7248-MON; -.
DR BioCyc; MetaCyc:G7248-MON; -.
DR BRENDA; 3.4.11.9; 2026.
DR PRO; PR:P76524; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; Chromosome.
DR GO; GO:0004177; F:aminopeptidase activity; IDA:EcoliWiki.
DR GO; GO:0070006; F:metalloaminopeptidase activity; IDA:EcoCyc.
DR GO; GO:0046914; F:transition metal ion binding; IDA:EcoCyc.
DR GO; GO:0006508; P:proteolysis; IDA:EcoCyc.
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; IPR001714; Pept_M24_MAP.
DR Pfam; PF01321; Creatinase_N; 1.
DR Pfam; PF00557; Peptidase_M24; 1.
DR PRINTS; PR00599; MAPEPTIDASE.
DR SUPFAM; SSF53092; SSF53092; 1.
DR SUPFAM; SSF55920; SSF55920; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Aminopeptidase; Hydrolase; Protease; Reference proteome.
FT CHAIN 1..361
FT /note="Aminopeptidase YpdF"
FT /id="PRO_0000185105"
FT HELIX 2..14
FT /evidence="ECO:0007829|PDB:5CNX"
FT STRAND 17..21
FT /evidence="ECO:0007829|PDB:5CNX"
FT HELIX 24..31
FT /evidence="ECO:0007829|PDB:5CNX"
FT STRAND 39..45
FT /evidence="ECO:0007829|PDB:5CNX"
FT STRAND 47..52
FT /evidence="ECO:0007829|PDB:5CNX"
FT TURN 53..55
FT /evidence="ECO:0007829|PDB:5CNX"
FT HELIX 56..62
FT /evidence="ECO:0007829|PDB:5CNX"
FT STRAND 66..75
FT /evidence="ECO:0007829|PDB:5CNX"
FT HELIX 77..87
FT /evidence="ECO:0007829|PDB:5CNX"
FT STRAND 92..95
FT /evidence="ECO:0007829|PDB:5CNX"
FT TURN 97..99
FT /evidence="ECO:0007829|PDB:5CNX"
FT HELIX 102..111
FT /evidence="ECO:0007829|PDB:5CNX"
FT STRAND 112..118
FT /evidence="ECO:0007829|PDB:5CNX"
FT HELIX 121..125
FT /evidence="ECO:0007829|PDB:5CNX"
FT HELIX 130..153
FT /evidence="ECO:0007829|PDB:5CNX"
FT HELIX 160..173
FT /evidence="ECO:0007829|PDB:5CNX"
FT STRAND 177..181
FT /evidence="ECO:0007829|PDB:5CNX"
FT STRAND 184..187
FT /evidence="ECO:0007829|PDB:5CNX"
FT HELIX 188..192
FT /evidence="ECO:0007829|PDB:5CNX"
FT STRAND 208..213
FT /evidence="ECO:0007829|PDB:5CNX"
FT STRAND 215..217
FT /evidence="ECO:0007829|PDB:5CNX"
FT STRAND 224..229
FT /evidence="ECO:0007829|PDB:5CNX"
FT TURN 237..239
FT /evidence="ECO:0007829|PDB:5CNX"
FT HELIX 243..258
FT /evidence="ECO:0007829|PDB:5CNX"
FT HELIX 266..279
FT /evidence="ECO:0007829|PDB:5CNX"
FT HELIX 283..285
FT /evidence="ECO:0007829|PDB:5CNX"
FT STRAND 290..293
FT /evidence="ECO:0007829|PDB:5CNX"
FT STRAND 295..305
FT /evidence="ECO:0007829|PDB:5CNX"
FT STRAND 317..320
FT /evidence="ECO:0007829|PDB:5CNX"
FT STRAND 323..326
FT /evidence="ECO:0007829|PDB:5CNX"
FT TURN 327..329
FT /evidence="ECO:0007829|PDB:5CNX"
FT STRAND 330..333
FT /evidence="ECO:0007829|PDB:5CNX"
FT STRAND 335..340
FT /evidence="ECO:0007829|PDB:5CNX"
FT STRAND 342..347
FT /evidence="ECO:0007829|PDB:5CNX"
SQ SEQUENCE 361 AA; 39624 MW; 34E97443005EB8D3 CRC64;
MTLLASLRDW LKAQQLDAVL LSSRQNKQPH LGISTGSGYV VISRESAHIL VDSRYYVEVE
ARAQGYQLHL LDATNTLTTI VNQIIADEQL QTLGFEGQQV SWETAHRWQS ELNAKLVSAT
PDVLRQIKTP EEVEKIRLAC GIADRGAEHI RRFIQAGMSE REIAAELEWF MRQQGAEKAS
FDTIVASGWR GALPHGKASD KIVAAGEFVT LDFGALYQGY CSDMTRTLLV NGEGVSAESH
LLFNVYQIVL QAQLAAISAI RPGVRCQQVD DAARRVITEA GYGDYFGHNT GHAIGIEVHE
DPRFSPRDTT TLQPGMLLTV EPGIYLPGQG GVRIEDVVLV TPQGAEVLYA MPKTVLLTGE
A
