TATD_MYCTU
ID TATD_MYCTU Reviewed; 264 AA.
AC O08343; I6XWT3; L0T861;
DT 09-DEC-2015, integrated into UniProtKB/Swiss-Prot.
DT 01-JUL-1997, sequence version 1.
DT 03-AUG-2022, entry version 126.
DE RecName: Full=Uncharacterized metal-dependent hydrolase TatD {ECO:0000305};
DE EC=3.1.-.- {ECO:0000305};
GN Name=tatD {ECO:0000312|EMBL:CCP43758.1};
GN OrderedLocusNames=Rv1008 {ECO:0000312|EMBL:CCP43758.1};
OS Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv).
OC Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC Mycobacterium; Mycobacterium tuberculosis complex.
OX NCBI_TaxID=83332;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 25618 / H37Rv;
RX PubMed=9634230; DOI=10.1038/31159;
RA Cole S.T., Brosch R., Parkhill J., Garnier T., Churcher C.M., Harris D.E.,
RA Gordon S.V., Eiglmeier K., Gas S., Barry C.E. III, Tekaia F., Badcock K.,
RA Basham D., Brown D., Chillingworth T., Connor R., Davies R.M., Devlin K.,
RA Feltwell T., Gentles S., Hamlin N., Holroyd S., Hornsby T., Jagels K.,
RA Krogh A., McLean J., Moule S., Murphy L.D., Oliver S., Osborne J.,
RA Quail M.A., Rajandream M.A., Rogers J., Rutter S., Seeger K., Skelton S.,
RA Squares S., Squares R., Sulston J.E., Taylor K., Whitehead S.,
RA Barrell B.G.;
RT "Deciphering the biology of Mycobacterium tuberculosis from the complete
RT genome sequence.";
RL Nature 393:537-544(1998).
RN [2]
RP DISRUPTION PHENOTYPE.
RC STRAIN=H37Rv;
RX PubMed=16952959; DOI=10.1128/jb.00631-06;
RA Saint-Joanis B., Demangel C., Jackson M., Brodin P., Marsollier L.,
RA Boshoff H., Cole S.T.;
RT "Inactivation of Rv2525c, a substrate of the twin arginine translocation
RT (Tat) system of Mycobacterium tuberculosis, increases beta-lactam
RT susceptibility and virulence.";
RL J. Bacteriol. 188:6669-6679(2006).
RN [3]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC STRAIN=ATCC 25618 / H37Rv;
RX PubMed=21969609; DOI=10.1074/mcp.m111.011627;
RA Kelkar D.S., Kumar D., Kumar P., Balakrishnan L., Muthusamy B., Yadav A.K.,
RA Shrivastava P., Marimuthu A., Anand S., Sundaram H., Kingsbury R.,
RA Harsha H.C., Nair B., Prasad T.S., Chauhan D.S., Katoch K., Katoch V.M.,
RA Kumar P., Chaerkady R., Ramachandran S., Dash D., Pandey A.;
RT "Proteogenomic analysis of Mycobacterium tuberculosis by high resolution
RT mass spectrometry.";
RL Mol. Cell. Proteomics 10:M111.011627-M111.011627(2011).
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 -!- DISRUPTION PHENOTYPE: Not essential for growth.
CC {ECO:0000269|PubMed:16952959}.
CC -!- SIMILARITY: Belongs to the metallo-dependent hydrolases superfamily.
CC TatD-type hydrolase family. {ECO:0000305}.
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DR EMBL; AL123456; CCP43758.1; -; Genomic_DNA.
DR RefSeq; NP_215524.1; NC_000962.3.
DR RefSeq; WP_010886103.1; NC_000962.3.
DR AlphaFoldDB; O08343; -.
DR SMR; O08343; -.
DR STRING; 83332.Rv1008; -.
DR PaxDb; O08343; -.
DR PRIDE; O08343; -.
DR DNASU; 886047; -.
DR GeneID; 886047; -.
DR KEGG; mtu:Rv1008; -.
DR PATRIC; fig|83332.111.peg.1119; -.
DR TubercuList; Rv1008; -.
DR eggNOG; COG0084; Bacteria.
DR OMA; PNEAPRI; -.
DR PhylomeDB; O08343; -.
DR Proteomes; UP000001584; Chromosome.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0005886; C:plasma membrane; HDA:MTBBASE.
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 1: Evidence at protein level;
KW Hydrolase; Metal-binding; Reference proteome.
FT CHAIN 1..264
FT /note="Uncharacterized metal-dependent hydrolase TatD"
FT /id="PRO_0000434887"
FT BINDING 5
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P0AFQ7"
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 93
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P0AFQ7"
FT BINDING 93
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P0AFQ7"
FT BINDING 134
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P0AFQ7"
FT BINDING 158
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P0AFQ7"
FT BINDING 208
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P0AFQ7"
SQ SEQUENCE 264 AA; 29083 MW; 3F395346165982AB CRC64;
MVDAHTHLDA CGARDADTVR SLVERAAAAG VTAVVTVADD LESARWVTRA AEWDRRVYAA
VALHPTRADA LTDAARAELE RLVAHPRVVA VGETGIDMYW PGRLDGCAEP HVQREAFAWH
IDLAKRTGKP LMIHNRQADR DVLDVLRAEG APDTVILHCF SSDAAMARTC VDAGWLLSLS
GTVSFRTARE LREAVPLMPV EQLLVETDAP YLTPHPHRGL ANEPYCLPYT VRALAELVNR
RPEEVALITT SNARRAYGLG WMRQ
