ID   Y454_HAEIN              Reviewed;         260 AA.
AC   P44718;
DT   01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1995, sequence version 1.
DT   03-AUG-2022, entry version 110.
DE   RecName: Full=Uncharacterized metal-dependent hydrolase HI_0454 {ECO:0000305};
DE            EC=3.1.-.- {ECO:0000305};
GN   OrderedLocusNames=HI_0454;
OS   Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales;
OC   Pasteurellaceae; Haemophilus.
OX   NCBI_TaxID=71421;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd;
RX   PubMed=7542800; DOI=10.1126/science.7542800;
RA   Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F.,
RA   Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M.,
RA   McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D.,
RA   Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., Weidman J.F.,
RA   Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., Utterback T.R.,
RA   Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., Fine L.D.,
RA   Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., Gnehm C.L., McDonald L.A.,
RA   Small K.V., Fraser C.M., Smith H.O., Venter J.C.;
RT   "Whole-genome random sequencing and assembly of Haemophilus influenzae
RT   Rd.";
RL   Science 269:496-512(1995).
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}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; L42023; AAC22112.1; -; Genomic_DNA.
DR   PIR; I64152; I64152.
DR   RefSeq; NP_438615.1; NC_000907.1.
DR   RefSeq; WP_010868988.1; NC_000907.1.
DR   STRING; 71421.HI_0454; -.
DR   EnsemblBacteria; AAC22112; AAC22112; HI_0454.
DR   KEGG; hin:HI_0454; -.
DR   PATRIC; fig|71421.8.peg.474; -.
DR   eggNOG; COG0084; Bacteria.
DR   HOGENOM; CLU_031506_4_0_6; -.
DR   OMA; DGPYEYR; -.
DR   PhylomeDB; P44718; -.
DR   BioCyc; HINF71421:G1GJ1-470-MON; -.
DR   Proteomes; UP000000579; Chromosome.
DR   GO; GO:0005829; C:cytosol; IBA:GO_Central.
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; PS01090; TATD_2; 1.
DR   PROSITE; PS01091; TATD_3; 1.
PE   3: Inferred from homology;
KW   Hydrolase; Metal-binding; Reference proteome.
FT   CHAIN           1..260
FT                   /note="Uncharacterized metal-dependent hydrolase HI_0454"
FT                   /id="PRO_0000201998"
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         95
FT                   /ligand="a divalent metal cation"
FT                   /ligand_id="ChEBI:CHEBI:60240"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250|UniProtKB:P0AFQ7"
FT   BINDING         95
FT                   /ligand="a divalent metal cation"
FT                   /ligand_id="ChEBI:CHEBI:60240"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250|UniProtKB:P0AFQ7"
FT   BINDING         131
FT                   /ligand="a divalent metal cation"
FT                   /ligand_id="ChEBI:CHEBI:60240"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250|UniProtKB:P0AFQ7"
FT   BINDING         156
FT                   /ligand="a divalent metal cation"
FT                   /ligand_id="ChEBI:CHEBI:60240"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250|UniProtKB:P0AFQ7"
FT   BINDING         206
FT                   /ligand="a divalent metal cation"
FT                   /ligand_id="ChEBI:CHEBI:60240"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250|UniProtKB:P0AFQ7"
SQ   SEQUENCE   260 AA;  29419 MW;  3A0F9966442AB56E CRC64;
     MFIVDSHCHL DALDYENLHK NISDVVEKAH ARDVKHLLAI GVTLSRFEQA YDSLREFNNV
     SLACGVHPLD FEEEPYDAER LLRLAQDPKV IAIGEIGLDY YYSADNKAAQ QAVFGSQIDI
     ANQLDKPVII HTRSAGDDTI AMLRQHRAEK CGGVIHCFTE TMEFXKKALD LGFYISCSGI
     VTFKNAEAIR EVIRYVPMER LLVETDSPYL APVPYRGKEN QPAYTREVCE YVATLKGVSA
     EAFAQITTQN FERLFKIRVE