ID   YIDJ_ECOLI              Reviewed;         497 AA.
AC   P31447; Q2M7Z1;
DT   01-JUL-1993, integrated into UniProtKB/Swiss-Prot.
DT   01-JUL-1993, sequence version 1.
DT   03-AUG-2022, entry version 136.
DE   RecName: Full=Uncharacterized sulfatase YidJ;
DE            EC=3.1.6.-;
GN   Name=yidJ; OrderedLocusNames=b3678, JW3654;
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=7686882; DOI=10.1006/geno.1993.1230;
RA   Burland V.D., Plunkett G. III, Daniels D.L., Blattner F.R.;
RT   "DNA sequence and analysis of 136 kilobases of the Escherichia coli genome:
RT   organizational symmetry around the origin of replication.";
RL   Genomics 16:551-561(1993).
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).
CC   -!- COFACTOR:
CC       Name=Ca(2+); Xref=ChEBI:CHEBI:29108; Evidence={ECO:0000250};
CC       Note=Binds 1 Ca(2+) ion per subunit. {ECO:0000250};
CC   -!- PTM: The conversion to 3-oxoalanine (also known as C-formylglycine,
CC       FGly), of a serine or cysteine residue in prokaryotes and of a cysteine
CC       residue in eukaryotes, is critical for catalytic activity.
CC       {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the sulfatase family. {ECO:0000305}.
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DR   EMBL; L10328; AAA62030.1; -; Genomic_DNA.
DR   EMBL; U00096; AAC76701.1; -; Genomic_DNA.
DR   EMBL; AP009048; BAE77615.1; -; Genomic_DNA.
DR   PIR; G65169; G65169.
DR   RefSeq; NP_418134.1; NC_000913.3.
DR   RefSeq; WP_000828527.1; NZ_SSZK01000035.1.
DR   AlphaFoldDB; P31447; -.
DR   SMR; P31447; -.
DR   BioGRID; 4261453; 6.
DR   STRING; 511145.b3678; -.
DR   PaxDb; P31447; -.
DR   PRIDE; P31447; -.
DR   EnsemblBacteria; AAC76701; AAC76701; b3678.
DR   EnsemblBacteria; BAE77615; BAE77615; BAE77615.
DR   GeneID; 948188; -.
DR   KEGG; ecj:JW3654; -.
DR   KEGG; eco:b3678; -.
DR   PATRIC; fig|1411691.4.peg.3026; -.
DR   EchoBASE; EB1656; -.
DR   eggNOG; COG3119; Bacteria.
DR   HOGENOM; CLU_006332_9_2_6; -.
DR   InParanoid; P31447; -.
DR   OMA; WGEHGLI; -.
DR   PhylomeDB; P31447; -.
DR   BioCyc; EcoCyc:EG11705-MON; -.
DR   PRO; PR:P31447; -.
DR   Proteomes; UP000000318; Chromosome.
DR   Proteomes; UP000000625; Chromosome.
DR   GO; GO:0110165; C:cellular anatomical entity; IEA:UniProt.
DR   GO; GO:0004065; F:arylsulfatase activity; IBA:GO_Central.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   Gene3D; 3.40.720.10; -; 1.
DR   InterPro; IPR017850; Alkaline_phosphatase_core_sf.
DR   InterPro; IPR032506; DUF4976.
DR   InterPro; IPR024607; Sulfatase_CS.
DR   InterPro; IPR000917; Sulfatase_N.
DR   Pfam; PF16347; DUF4976; 1.
DR   Pfam; PF00884; Sulfatase; 1.
DR   SUPFAM; SSF53649; SSF53649; 1.
DR   PROSITE; PS00523; SULFATASE_1; 1.
DR   PROSITE; PS00149; SULFATASE_2; 1.
PE   3: Inferred from homology;
KW   Calcium; Hydrolase; Metal-binding; Reference proteome.
FT   CHAIN           1..497
FT                   /note="Uncharacterized sulfatase YidJ"
FT                   /id="PRO_0000192685"
FT   ACT_SITE        52
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000250|UniProtKB:P15289"
FT   ACT_SITE        102
FT                   /evidence="ECO:0000250|UniProtKB:P15289"
FT   BINDING         12
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /evidence="ECO:0000250"
FT   BINDING         13
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /evidence="ECO:0000250"
FT   BINDING         52
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /note="via 3-oxoalanine"
FT                   /evidence="ECO:0000250"
FT   BINDING         284
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /evidence="ECO:0000250"
FT   BINDING         285
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /evidence="ECO:0000250"
FT   MOD_RES         52
FT                   /note="3-oxoalanine (Cys)"
FT                   /evidence="ECO:0000250|UniProtKB:P15289"
SQ   SEQUENCE   497 AA;  57295 MW;  2051C34EACEB412E CRC64;
     MKRPNFLFVM TDTQATNMVG CYSGKPLNTQ NIDSLAAEGI RFNSAYTCSP VCTPARAGLF
     TGIYANQSGP WTNNVAPGKN ISTMGRYFKD AGYHTCYIGK WHLDGHDYFG TGECPPEWDA
     DYWFDGANYL SELTEKEISL WRNGLNSVED LQANHIDETF TWAHRISNRA VDFLQQPARA
     DEPFLMVVSY DEPHHPFTCP VEYLEKYADF YYELGEKAQD DLANKPEHHR LWAQAMPSPV
     GDDGLYHHPL YFACNDFVDD QIGRVINALT PEQRENTWVI YTSDHGEMMG AHKLISKGAA
     MYDDITRIPL IIRSPQGERR QVDTPVSHID LLPTMMALAD IEKPEILPGE NILAVKEPRG
     VMVEFNRYEI EHDSFGGFIP VRCWVTDDFK LVLNLFTSDE LYDRRNDPNE MHNLIDDIRF
     ADVRSKMHDA LLDYMDKIRD PFRSYQWSLR PWRKDARPRW MGAFRPRPQD GYSPVVRDYD
     TGLPTQGVKV EEKKQKF