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YCFH_ECO57
ID   YCFH_ECO57              Reviewed;         265 AA.
AC   P0AFQ9; P37346; P78057;
DT   20-DEC-2005, integrated into UniProtKB/Swiss-Prot.
DT   20-DEC-2005, sequence version 1.
DT   03-AUG-2022, entry version 97.
DE   RecName: Full=Uncharacterized metal-dependent hydrolase YcfH {ECO:0000305};
DE            EC=3.1.-.- {ECO:0000305};
GN   Name=ycfH; OrderedLocusNames=Z1739, ECs1478;
OS   Escherichia coli O157:H7.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=83334;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=O157:H7 / EDL933 / ATCC 700927 / EHEC;
RX   PubMed=11206551; DOI=10.1038/35054089;
RA   Perna N.T., Plunkett G. III, Burland V., Mau B., Glasner J.D., Rose D.J.,
RA   Mayhew G.F., Evans P.S., Gregor J., Kirkpatrick H.A., Posfai G.,
RA   Hackett J., Klink S., Boutin A., Shao Y., Miller L., Grotbeck E.J.,
RA   Davis N.W., Lim A., Dimalanta E.T., Potamousis K., Apodaca J.,
RA   Anantharaman T.S., Lin J., Yen G., Schwartz D.C., Welch R.A.,
RA   Blattner F.R.;
RT   "Genome sequence of enterohaemorrhagic Escherichia coli O157:H7.";
RL   Nature 409:529-533(2001).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=O157:H7 / Sakai / RIMD 0509952 / EHEC;
RX   PubMed=11258796; DOI=10.1093/dnares/8.1.11;
RA   Hayashi T., Makino K., Ohnishi M., Kurokawa K., Ishii K., Yokoyama K.,
RA   Han C.-G., Ohtsubo E., Nakayama K., Murata T., Tanaka M., Tobe T., Iida T.,
RA   Takami H., Honda T., Sasakawa C., Ogasawara N., Yasunaga T., Kuhara S.,
RA   Shiba T., Hattori M., Shinagawa H.;
RT   "Complete genome sequence of enterohemorrhagic Escherichia coli O157:H7 and
RT   genomic comparison with a laboratory strain K-12.";
RL   DNA Res. 8:11-22(2001).
CC   -!- COFACTOR:
CC       Name=a divalent metal cation; Xref=ChEBI:CHEBI:60240;
CC         Evidence={ECO:0000250|UniProtKB:P0AFQ7};
CC       Note=Binds 2 divalent metal cations per subunit.
CC       {ECO:0000250|UniProtKB:P0AFQ7};
CC   -!- SIMILARITY: Belongs to the metallo-dependent hydrolases superfamily.
CC       TatD-type hydrolase family. {ECO:0000305}.
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DR   EMBL; AE005174; AAG55846.1; -; Genomic_DNA.
DR   EMBL; BA000007; BAB34901.1; -; Genomic_DNA.
DR   PIR; B85673; B85673.
DR   PIR; F90813; F90813.
DR   RefSeq; NP_309505.1; NC_002695.1.
DR   RefSeq; WP_000480245.1; NZ_SWKA01000005.1.
DR   AlphaFoldDB; P0AFQ9; -.
DR   SMR; P0AFQ9; -.
DR   STRING; 155864.EDL933_1677; -.
DR   EnsemblBacteria; AAG55846; AAG55846; Z1739.
DR   EnsemblBacteria; BAB34901; BAB34901; ECs_1478.
DR   GeneID; 66670634; -.
DR   GeneID; 913835; -.
DR   KEGG; ece:Z1739; -.
DR   KEGG; ecs:ECs_1478; -.
DR   PATRIC; fig|386585.9.peg.1578; -.
DR   eggNOG; COG0084; Bacteria.
DR   HOGENOM; CLU_031506_4_0_6; -.
DR   OMA; DGPYEYR; -.
DR   Proteomes; UP000000558; Chromosome.
DR   Proteomes; UP000002519; Chromosome.
DR   GO; GO:0004536; F:deoxyribonuclease activity; 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; IPR015991; Hydrolase_TatD-type.
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   TIGRFAMs; TIGR00010; TIGR00010; 1.
DR   PROSITE; PS01137; TATD_1; 1.
DR   PROSITE; PS01091; TATD_3; 1.
PE   3: Inferred from homology;
KW   Hydrolase; Metal-binding; Reference proteome.
FT   CHAIN           1..265
FT                   /note="Uncharacterized metal-dependent hydrolase YcfH"
FT                   /id="PRO_0000201996"
FT   BINDING         7
FT                   /ligand="a divalent metal cation"
FT                   /ligand_id="ChEBI:CHEBI:60240"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250|UniProtKB:P0AFQ7"
FT   BINDING         9
FT                   /ligand="a divalent metal cation"
FT                   /ligand_id="ChEBI:CHEBI:60240"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250|UniProtKB:P0AFQ7"
FT   BINDING         94
FT                   /ligand="a divalent metal cation"
FT                   /ligand_id="ChEBI:CHEBI:60240"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250|UniProtKB:P0AFQ7"
FT   BINDING         94
FT                   /ligand="a divalent metal cation"
FT                   /ligand_id="ChEBI:CHEBI:60240"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250|UniProtKB:P0AFQ7"
FT   BINDING         130
FT                   /ligand="a divalent metal cation"
FT                   /ligand_id="ChEBI:CHEBI:60240"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250|UniProtKB:P0AFQ7"
FT   BINDING         155
FT                   /ligand="a divalent metal cation"
FT                   /ligand_id="ChEBI:CHEBI:60240"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250|UniProtKB:P0AFQ7"
FT   BINDING         205
FT                   /ligand="a divalent metal cation"
FT                   /ligand_id="ChEBI:CHEBI:60240"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250|UniProtKB:P0AFQ7"
SQ   SEQUENCE   265 AA;  29809 MW;  722C9450157620C5 CRC64;
     MFLVDSHCHL DGLDYESLHK DVDDVLAKAA ARDVKFCLAV ATTLPGYLHM RDLVGERDNV
     VFSCGVHPLN QNDPYDVEDL RRLAAEEGVV ALGETGLDYY YTPETKVRQQ ESFIHHIQIG
     RELNKPVIVH TRDARADTLA ILREEKVTDC GGVLHCFTED RETAGKLLDL GFYISFSGIV
     TFRNAEQLRD AARYVPLDRL LVETDSPYLA PVPHRGKENQ PAMVRDVAEY MAVLKGVAVE
     ELAQVTTDNF ARLFHIDASR LQSIR
 
 
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