YPDE_ECOLI
ID YPDE_ECOLI Reviewed; 345 AA.
AC P77585;
DT 27-MAR-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1997, sequence version 1.
DT 03-AUG-2022, entry version 132.
DE RecName: Full=Aminopeptidase YpdE;
DE EC=3.4.11.-;
GN Name=ypdE; OrderedLocusNames=b2384, JW2381;
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].
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 AS AN AMINOPEPTIDASE, CATALYTIC ACTIVITY, SUBSTRATE SPECIFICITY,
RP AND COFACTOR.
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: Has a broad aminopeptidase activity on non-blocked peptides
CC by progressively cleaving amino acids off the peptide substrate.
CC Aminopeptidase activity stops at the residue before the first proline
CC in the peptide. Cannot cleave when proline is the first N-terminal
CC residue. {ECO:0000269|PubMed:15901689}.
CC -!- COFACTOR:
CC Name=Co(2+); Xref=ChEBI:CHEBI:48828;
CC Evidence={ECO:0000269|PubMed:15901689, ECO:0000305};
CC Name=Ni(2+); Xref=ChEBI:CHEBI:49786;
CC Evidence={ECO:0000269|PubMed:15901689, ECO:0000305};
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC Evidence={ECO:0000269|PubMed:15901689, ECO:0000305};
CC Name=Cu(2+); Xref=ChEBI:CHEBI:29036;
CC Evidence={ECO:0000269|PubMed:15901689, ECO:0000305};
CC Note=Binds 2 divalent metal cations per subunit. Can use cobalt, and to
CC a lesser extent, nickel, manganese or copper.
CC {ECO:0000269|PubMed:15901689, ECO:0000305};
CC -!- SIMILARITY: Belongs to the peptidase M42 family. {ECO:0000305}.
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DR EMBL; U00096; AAC75443.1; -; Genomic_DNA.
DR EMBL; AP009048; BAA16254.1; -; Genomic_DNA.
DR PIR; E65012; E65012.
DR RefSeq; NP_416885.1; NC_000913.3.
DR RefSeq; WP_000366028.1; NZ_LN832404.1.
DR AlphaFoldDB; P77585; -.
DR SMR; P77585; -.
DR BioGRID; 4260561; 10.
DR BioGRID; 851189; 4.
DR DIP; DIP-48263N; -.
DR IntAct; P77585; 8.
DR STRING; 511145.b2384; -.
DR MEROPS; M42.008; -.
DR PaxDb; P77585; -.
DR PRIDE; P77585; -.
DR EnsemblBacteria; AAC75443; AAC75443; b2384.
DR EnsemblBacteria; BAA16254; BAA16254; BAA16254.
DR GeneID; 946848; -.
DR KEGG; ecj:JW2381; -.
DR KEGG; eco:b2384; -.
DR PATRIC; fig|1411691.4.peg.4344; -.
DR EchoBASE; EB3904; -.
DR eggNOG; COG1363; Bacteria.
DR HOGENOM; CLU_047249_0_2_6; -.
DR InParanoid; P77585; -.
DR OMA; YTLDNKA; -.
DR PhylomeDB; P77585; -.
DR BioCyc; EcoCyc:G7247-MON; -.
DR BioCyc; MetaCyc:G7247-MON; -.
DR PRO; PR:P77585; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; Chromosome.
DR GO; GO:0004177; F:aminopeptidase activity; IDA:EcoliWiki.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0070006; F:metalloaminopeptidase activity; IDA:EcoCyc.
DR GO; GO:0008237; F:metallopeptidase activity; IDA:EcoliWiki.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR Gene3D; 2.40.30.40; -; 1.
DR InterPro; IPR008007; Peptidase_M42.
DR InterPro; IPR023367; Peptidase_M42_dom2.
DR Pfam; PF05343; Peptidase_M42; 1.
DR PIRSF; PIRSF001123; PepA_GA; 1.
PE 1: Evidence at protein level;
KW Aminopeptidase; Cobalt; Hydrolase; Metal-binding; Metalloprotease;
KW Protease; Reference proteome.
FT CHAIN 1..345
FT /note="Aminopeptidase YpdE"
FT /id="PRO_0000071659"
FT ACT_SITE 198
FT /note="Proton acceptor"
FT /evidence="ECO:0000250"
FT BINDING 62
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 166
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 166
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 199
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 221
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 308
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
SQ SEQUENCE 345 AA; 37409 MW; FB2D88A5C11590A1 CRC64;
MDLSLLKALS EADAIASSEQ EVRQILLEEA DRLQKEVRFD GLGSVLIRLN ESTGPKVMIC
AHMDEVGFMV RSISREGAID VLPVGNVRMA ARQLQPVRIT TREECKIPGL LDGDRQGNDV
SAMRVDIGAR SYDEVMQAGI RPGDRVTFDT TFQVLPHQRV MGKAFDDRLG CYLLVTLLRE
LHDAELPAEV WLVASSSEEV GLRGGQTATR AVSPDVAIVL DTACWAKNFD YGAANHRQIG
NGPMLVLSDK SLIAPPKLTA WVETVAAEIG VPLQADMFSN GGTDGGAVHL TGTGVPTVVM
GPATRHGHCA ASIADCRDIL QMQQLLSALI QRLTRETVVQ LTDFR
