YJJV_ECOLI
ID YJJV_ECOLI Reviewed; 259 AA.
AC P39408; P78143; Q2M5T9;
DT 01-FEB-1995, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1995, sequence version 2.
DT 03-AUG-2022, entry version 153.
DE RecName: Full=Uncharacterized metal-dependent hydrolase YjjV {ECO:0000305};
DE EC=3.1.-.- {ECO:0000305};
GN Name=yjjV; OrderedLocusNames=b4378, JW4341;
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 / MG1655 / ATCC 47076;
RX PubMed=7610040; DOI=10.1093/nar/23.12.2105;
RA Burland V.D., Plunkett G. III, Sofia H.J., Daniels D.L., Blattner F.R.;
RT "Analysis of the Escherichia coli genome VI: DNA sequence of the region
RT from 92.8 through 100 minutes.";
RL Nucleic Acids Res. 23:2105-2119(1995).
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 X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS) IN COMPLEX WITH ZINC IONS.
RG New York structural genomics research consortium (NYSGRC);
RT "Crystal structure of yjjV, tatD homolog from Escherichia coli K12, at 1.8
RT A resolution.";
RL Submitted (FEB-2009) to the PDB data bank.
CC -!- COFACTOR:
CC Name=a divalent metal cation; Xref=ChEBI:CHEBI:60240;
CC Evidence={ECO:0000269|Ref.4};
CC Note=Binds 2 divalent metal cations per subunit. {ECO:0000269|Ref.4};
CC -!- INTERACTION:
CC P39408; P0CE47: tufA; NbExp=2; IntAct=EBI-561387, EBI-301077;
CC -!- SIMILARITY: Belongs to the metallo-dependent hydrolases superfamily.
CC TatD-type hydrolase family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAA97274.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR EMBL; U14003; AAA97274.1; ALT_INIT; Genomic_DNA.
DR EMBL; U00096; AAC77331.2; -; Genomic_DNA.
DR EMBL; AP009048; BAE78367.1; -; Genomic_DNA.
DR PIR; S56602; S56602.
DR RefSeq; WP_000563040.1; NZ_LN832404.1.
DR RefSeq; YP_026291.2; NC_000913.3.
DR PDB; 1ZZM; X-ray; 1.80 A; A=1-259.
DR PDBsum; 1ZZM; -.
DR AlphaFoldDB; P39408; -.
DR SMR; P39408; -.
DR BioGRID; 4261644; 70.
DR DIP; DIP-12661N; -.
DR IntAct; P39408; 4.
DR STRING; 511145.b4378; -.
DR jPOST; P39408; -.
DR PaxDb; P39408; -.
DR PRIDE; P39408; -.
DR EnsemblBacteria; AAC77331; AAC77331; b4378.
DR EnsemblBacteria; BAE78367; BAE78367; BAE78367.
DR GeneID; 2847741; -.
DR KEGG; ecj:JW4341; -.
DR KEGG; eco:b4378; -.
DR PATRIC; fig|511145.12.peg.4524; -.
DR EchoBASE; EB2483; -.
DR eggNOG; COG0084; Bacteria.
DR HOGENOM; CLU_031506_0_1_6; -.
DR InParanoid; P39408; -.
DR OMA; CHLDAGE; -.
DR PhylomeDB; P39408; -.
DR BioCyc; EcoCyc:G7952-MON; -.
DR EvolutionaryTrace; P39408; -.
DR PRO; PR:P39408; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; Chromosome.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0016788; F:hydrolase activity, acting on ester bonds; IEA:InterPro.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR CDD; cd01310; TatD_DNAse; 1.
DR InterPro; IPR018228; DNase_TatD-rel_CS.
DR InterPro; IPR032466; Metal_Hydrolase.
DR InterPro; IPR001130; TatD-like.
DR Pfam; PF01026; TatD_DNase; 1.
DR PIRSF; PIRSF005902; DNase_TatD; 1.
DR SUPFAM; SSF51556; SSF51556; 1.
DR PROSITE; PS01137; TATD_1; 1.
DR PROSITE; PS01090; TATD_2; 1.
DR PROSITE; PS01091; TATD_3; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Hydrolase; Metal-binding; Reference proteome.
FT CHAIN 1..259
FT /note="Uncharacterized metal-dependent hydrolase YjjV"
FT /id="PRO_0000201999"
FT BINDING 9
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /ligand_label="1"
FT /evidence="ECO:0000269|Ref.4"
FT BINDING 11
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /ligand_label="1"
FT /evidence="ECO:0000269|Ref.4"
FT BINDING 97
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /ligand_label="1"
FT /evidence="ECO:0000269|Ref.4"
FT BINDING 97
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /ligand_label="2"
FT /evidence="ECO:0000269|Ref.4"
FT BINDING 133
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /ligand_label="2"
FT /evidence="ECO:0000269|Ref.4"
FT BINDING 157
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /ligand_label="2"
FT /evidence="ECO:0000269|Ref.4"
FT BINDING 207
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /ligand_label="1"
FT /evidence="ECO:0000269|Ref.4"
FT STRAND 5..8
FT /evidence="ECO:0007829|PDB:1ZZM"
FT TURN 15..19
FT /evidence="ECO:0007829|PDB:1ZZM"
FT HELIX 21..30
FT /evidence="ECO:0007829|PDB:1ZZM"
FT STRAND 33..39
FT /evidence="ECO:0007829|PDB:1ZZM"
FT HELIX 43..45
FT /evidence="ECO:0007829|PDB:1ZZM"
FT HELIX 46..55
FT /evidence="ECO:0007829|PDB:1ZZM"
FT STRAND 59..63
FT /evidence="ECO:0007829|PDB:1ZZM"
FT HELIX 67..72
FT /evidence="ECO:0007829|PDB:1ZZM"
FT HELIX 75..87
FT /evidence="ECO:0007829|PDB:1ZZM"
FT STRAND 90..101
FT /evidence="ECO:0007829|PDB:1ZZM"
FT HELIX 109..125
FT /evidence="ECO:0007829|PDB:1ZZM"
FT STRAND 130..136
FT /evidence="ECO:0007829|PDB:1ZZM"
FT HELIX 138..148
FT /evidence="ECO:0007829|PDB:1ZZM"
FT STRAND 154..156
FT /evidence="ECO:0007829|PDB:1ZZM"
FT HELIX 163..171
FT /evidence="ECO:0007829|PDB:1ZZM"
FT STRAND 175..178
FT /evidence="ECO:0007829|PDB:1ZZM"
FT HELIX 180..183
FT /evidence="ECO:0007829|PDB:1ZZM"
FT TURN 185..187
FT /evidence="ECO:0007829|PDB:1ZZM"
FT HELIX 190..196
FT /evidence="ECO:0007829|PDB:1ZZM"
FT HELIX 199..201
FT /evidence="ECO:0007829|PDB:1ZZM"
FT STRAND 202..204
FT /evidence="ECO:0007829|PDB:1ZZM"
FT HELIX 223..225
FT /evidence="ECO:0007829|PDB:1ZZM"
FT HELIX 226..236
FT /evidence="ECO:0007829|PDB:1ZZM"
FT HELIX 241..256
FT /evidence="ECO:0007829|PDB:1ZZM"
SQ SEQUENCE 259 AA; 28909 MW; 9BFB42FAA760DC67 CRC64;
MICRFIDTHC HFDFPPFSGD EEASLQRAAQ AGVGKIIVPA TEAENFARVL ALAENYQPLY
AALGLHPGML EKHSDVSLEQ LQQALERRPA KVVAVGEIGL DLFGDDPQFE RQQWLLDEQL
KLAKRYDLPV ILHSRRTHDK LAMHLKRHDL PRTGVVHGFS GSLQQAERFV QLGYKIGVGG
TITYPRASKT RDVIAKLPLA SLLLETDAPD MPLNGFQGQP NRPEQAARVF AVLCELRREP
ADEIAQALLN NTYTLFNVP
