ID   Y081_HAEIN              Reviewed;         262 AA.
AC   P44500;
DT   01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1995, sequence version 1.
DT   03-AUG-2022, entry version 115.
DE   RecName: Full=Uncharacterized metal-dependent hydrolase HI_0081 {ECO:0000305};
DE            EC=3.1.-.- {ECO:0000305};
GN   OrderedLocusNames=HI_0081;
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; AAC21756.1; -; Genomic_DNA.
DR   PIR; A64142; A64142.
DR   RefSeq; NP_438254.1; NC_000907.1.
DR   RefSeq; WP_005693839.1; NC_000907.1.
DR   AlphaFoldDB; P44500; -.
DR   SMR; P44500; -.
DR   STRING; 71421.HI_0081; -.
DR   EnsemblBacteria; AAC21756; AAC21756; HI_0081.
DR   KEGG; hin:HI_0081; -.
DR   PATRIC; fig|71421.8.peg.82; -.
DR   eggNOG; COG0084; Bacteria.
DR   HOGENOM; CLU_031506_0_1_6; -.
DR   OMA; CHLDAGE; -.
DR   PhylomeDB; P44500; -.
DR   BioCyc; HINF71421:G1GJ1-82-MON; -.
DR   Proteomes; UP000000579; 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   3: Inferred from homology;
KW   Hydrolase; Metal-binding; Reference proteome.
FT   CHAIN           1..262
FT                   /note="Uncharacterized metal-dependent hydrolase HI_0081"
FT                   /id="PRO_0000202000"
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         98
FT                   /ligand="a divalent metal cation"
FT                   /ligand_id="ChEBI:CHEBI:60240"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250|UniProtKB:P0AFQ7"
FT   BINDING         98
FT                   /ligand="a divalent metal cation"
FT                   /ligand_id="ChEBI:CHEBI:60240"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250|UniProtKB:P0AFQ7"
FT   BINDING         138
FT                   /ligand="a divalent metal cation"
FT                   /ligand_id="ChEBI:CHEBI:60240"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250|UniProtKB:P0AFQ7"
FT   BINDING         162
FT                   /ligand="a divalent metal cation"
FT                   /ligand_id="ChEBI:CHEBI:60240"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250|UniProtKB:P0AFQ7"
FT   BINDING         212
FT                   /ligand="a divalent metal cation"
FT                   /ligand_id="ChEBI:CHEBI:60240"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250|UniProtKB:P0AFQ7"
SQ   SEQUENCE   262 AA;  29789 MW;  382D860E063DF852 CRC64;
     MHFFDTHTHL NYLQQFTGEP LSQLIDNAKQ ADVQKILVVA VKEADFKTIQ NMTALFPDNL
     CYGLGLHPLY IQEHAENDLI LLEQALKNRD TNCTAVAEIG LERAIPDLLT DELWAKQCHF
     FESQLYLAKQ FNLPVNIHSR KTHDQIFTFL KRIPLSKLGV VHGFSGSYDQ AKRFVDLGYK
     IGVGGTITYE RANKTRQAIA KLPLDALVLE TDSPDMPVFG FQGQPNRPER IVESFKALCT
     LRNEPAELIK KLTWENACQI FS